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O02768
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PGH2_RABIT
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Prostaglandin G/H synthase 2 (EC 1.14.99.1) (Cyclooxygenase-2) (COX-2) (PHS II) (Prostaglandin H2 synthase 2) (PGH synthase 2) (PGHS-2) (Prostaglandin-endoperoxide synthase 2)
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MLARALLLCAAVALSHAANPCCSNPCQNRGVCMTMGFDQYKCDCTRTGFYGENCSTPEFLTRIKLLLKPTPDTVHYILTHFKGVWNIVNSIPFLRNSIMKYVLTSRSHMIDSPPTYNVHYNYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGKKELPDSKDVVEKLLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDLKRGPAFTKGLGHGVDLNHIYGETLDRQHKLRLFKDGKMKYQVIDGEVYPPTVKDTQVEMIYPPHIPAHLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDTFQIDDQQYNYQQFLYNNSILLEHGLTQFVESFTRQIAGRVAGGRNVPPAVQKVAKASIDQSRQMKYQSLNEYRKRFLLKPYESFEELTGEKEMAAELEALYGDIDAVELYPALLVERPRPDAIFGESMVEMGAPFSLKGLMGNPICSPNYWKPSTFGGEVGFKIVNTASIQSLICNNVKGCPFTSFNVPDPQLTKTVTINASASHSRLEDINPTVLLKGRSTEL
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Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner,being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity).
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O02773
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MA1A1_PIG
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Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA (EC 3.2.1.113) (Man(9)-alpha-mannosidase) (Man9-mannosidase) (Mannosidase alpha class 1A member 1) (Processing alpha-1,2-mannosidase IA) (Alpha-1,2-mannosidase IA)
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MPVGGLLPLFSSPAGGGLGGGLGGGLGGGGGGGGRKGSGPSAFRLTEKFVLLLVFSAFITLCFGAIFFLPDSSKLLSGVLFHSSPALQPAADHKPGPGARAEDAADGRARPGEEGAPGDPAAALEDNLARIRENHERALMEAKETLQKLPEEIQRDILMEKEKVAQDQMSNRMGFRLPPVYLVPLIGAIDREPADAAVREKRAKIKEMMKHAWNNYKLYAWGKNELKPVSKGGHSSSLFGNIKGATIVDALDTLFIMKMKNEFEEAKAWVEEHLNFNVNAEVSVFEVNIRFIGGLISAYYLSGEEIFRKKAVELGVKLLPAFYTPSGIPWALLNIKSGIGRNWPWASGGSSILAEFGTLHLEFIHLSYLSGNPFFAEKVMNIRKVLNNLEKPQGLYPNYLNPNSGQWGQYHVSVGGLGDSFYEYLLKAWLMSDKTDLEAKKMYFDAIKAIETHLIRKSRNGLTYIAEWKGGLLEHKMGHLTCFAGGMFALGADDAPDGLTQHYLQLGAEIARTCHESYSRTFVKLGPEAFRFDGGVEAIATRQNEKYYILRPEVVETYLYMWRLTHDPKYRKWAWEAVEALEKHCRVNGGYSGLRDVYVSAQTYDDVQQSFFLAETLKYLYLIFSDDDLLPLEHWIFNTEAHPLPVLSRNIKKVEDNEK
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Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
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O02776
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PARG_BOVIN
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Poly(ADP-ribose) glycohydrolase (EC 3.2.1.143)
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MSAGPGCEPCTKRPRWDAAATSPPAASDARSFPGRQRRVLDSKDAPVQFRVPPSSSGCALGRAGQHRGSATSLVFKQKTITSWMDTKGIKTVESESLHSKENNNTREESMMSSVQKDNFYQHNMEKLENVSQLGFDKSPVEKGTQYLKQHQTAAMCKWQNEGPHSERLLESEPPAVTLVPEQFSNANVDQSSPKDDHSDTNSEESRDNQQFLTHVKLANAKQTMEDEQGREARSHQKCGKACHPAEACAGCQQEETDVVSESPLSDTGSEDVGTGLKNANRLNRQESSLGNSPPFEKESEPESPMDVDNSKNSCQDSEADEETSPGFDEQEDSSSAQTANKPSRFQPREADTELRKRSSAKGGEIRLHFQFEGGESRAGMNDVNAKRPGSTSSLNVECRNSKQHGRKDSKITDHFMRVPKAEDKRKEQCEMKHQRTERKIPKYIPPHLSPDKKWLGTPIEEMRRMPRCGIRLPPLRPSANHTVTIRVDLLRIGEVPKPFPTHFKDLWDNKHVKMPCSEQNLYPVEDENGERAAGSRWELIQTALLNRLTRPQNLKDAILKYNVAYSKKWDFTALIDFWDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSITMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCEKLLTRLHVTYEGTIEGNGQGMLQVDFANRFVGGGVTSAGLVQEEIRFLINPELIVSRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWARSHEDRSERDDWQRRTTEIVAIDALHFRRYLDQFVPEKIRRELNKAYCGFLRPGVSSENLSAVATGNWGCGAFGGDARLKALIQILAAAVAERDVVYFTFGDSELMRDIYSMHTFLTERKLTVGEVYKLLLRYYNEECRNCSTPGPDIKLYPFIYHAVESCTQTTNQPGQRTGA
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Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers. It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated. Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG. Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress. Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond. Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (By similarity).
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O02791
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GALC_MACMU
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Galactocerebrosidase (GALCERase) (EC 3.2.1.46) (Galactocerebroside beta-galactosidase) (Galactosylceramidase) (Galactosylceramide beta-galactosidase)
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MAEWLLSASRQRRVKAMTAAAGSAGRAAVPFLLCALLAPGGAYVLDDSDGLGREFDGIGAVSGGGATSRLLVNYPEPYRSQILDYLFKPNFGASLHILKVEIGGDGQTTDGTEPSHMHYALDENYFRGYEWWLMKEAKKRNPNITLIGLPWSFPGWLGKGFDWPYVNLQLTAYYVVTWIVGAKRYHDLDIDYIGIWNERSYNANYIKILRKMLNSQGLQRVKIIASDNLWESISAAMLLDAELFKVVDVIGAHYPGTHSVKDARLTGKKLWSSEDFSTLNSDTGAGCWGRILNQNYVNGYMTSTIAWNLVASYYEQLPYGRCGLMTAQEPWSGHYVVESPVWVSAHTTQFTQPGWYYLKTVGHLEKGGSYVALTDGLGNLTIIIETMSHKHSKCIRPFLPYFNVSQQFATFVLKGSFSEIPELQVWYTKLGKTSERFLFKQLDSLWLLDSNGSFTLKLQEDELFTLTTLTTGRKGSYLPPPKSQRFPSTYKDDFNVDYPFFSEAPNFADQTGVFEYFTNMEDPGEHHFTLRQVLNQRPITWAADASNTISIIGDYNWTNLTIKCDVYIETPDTGGVFIAGRVNKGGILIRSARGIFFWIFANGSYRVTGDLAGWIIYALGHVEVTAKTWYTLTLTIKGRFASGMLNDKSLWTDIPVNFPKNGWAAIGTHSFEFAQFDNFHVEATR
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Hydrolyzes the galactose ester bonds of glycolipids such as galactosylceramide and galactosylsphingosine. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon (By similarity).
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O02810
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PI4KB_BOVIN
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Phosphatidylinositol 4-kinase beta (PI4K-beta) (PI4Kbeta) (PtdIns 4-kinase beta) (EC 2.7.1.67)
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MGDTIVEPAPLKPTSEPAPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAISSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGATVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLGCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM
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Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane trafficking (By similarity).
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O02812
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MK14_CANLF
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Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
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MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGADLLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVVSFVPPPLDQEEMES
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Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression (By similarity). Phosphorylates S100A9 at 'Thr-113' (By similarity).
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O02824
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ADA1A_RABIT
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Alpha-1A adrenergic receptor (Alpha-1A adrenoreceptor) (Alpha-1A adrenoceptor) (Alpha-1C adrenergic receptor)
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MVFLSGNASDSSNCTHPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIISLCVISIDRYIGVSYPLRYPTIVTQRRGLRALLCVWAFSLVISVGPLFGWRQPAPDDETICQINEEPGYVLFSALGSFYVPLTIILAMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGVASAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPPETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLKIQCLRRKQSSKHALGYTLHAPSQALEGQHKDMVRIPVGSGETFYKISKTDGVCEWKFFSSMPRGSARITVPKDQSACTTARVRSKSFLQVCCCVGPSTPNPGENHQVPTIKIHTISLSENGEEV
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This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity).
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O02827
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MYLK_SHEEP
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Myosin light chain kinase, smooth muscle (MLCK) (smMLCK) (EC 2.7.11.18) (Telokin) [Cleaved into: Myosin light chain kinase, smooth muscle, deglutamylated form]
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FRLVEKKTGKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMKQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDIKNRLNCTQCLQHPWLXXXTKNMEAKKLSKHRMKKYMARRKWQKTGNAVRAIGRLSSMAMISGLSGRKSSTGSPTSPLNAEKLESEEDVSQAFLEAVAEEKPHVKPYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYQEDGNCSLIISDVCGDDDAKYTCKAVNSLGEATCTAELIVETMEEGEGEGGEEEEEE
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Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells (By similarity).
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O02828
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TAU_CAPHI
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Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau)
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MAEPRQEFDVMEDHAQGDYTLQDHEGDMEPGLKESPLQTPADDGSEEPGSETSDAKSTPTAEAEEAGIGDTSNLEDQAAGHVTQARMVSKGKDGTGPDDKKAKGADGKPGTKIATPRGAAPPGQKGQANATRIPAKTTPTPKTSPGTGESGKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSAAKSRLQAAPGPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
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Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.
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O02839
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MCP_PIG
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Membrane cofactor protein (CD antigen CD46)
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MMAFCALRKALPCRPENPFSSRCFVEILWVSLALVFLLPMPSDACDEPPKFESMRPQFLNTTYRPGDRVEYECRPGFQPMVPALPTFSVCQDDNTWSPLQEACRRKACSNLPDPLNGQVSYPNGDMLFGSKAQFTCNTGFYIIGAETVYCQVSGNVMAWSEPSPLCEKILCKPPGEIPNGKYTNSHKDVFEYNEVVTYSCLSSTGPDEFSLVGESSLFCIGKDEWSSDPPECKVVKCPYPVVPNGEIVSGFGSKFYYKAEVVFKCNAGFTLHGRDTIVCGANSTWEPEMPQCIKDSKPTDPPATPGPSHPGPPSPSDASPPKDAESLDGGIIAAIVVGVLAAIAVIAGGVYFFHHKYNKKRSK
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Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. May act as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity.
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O02840
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CADH5_PIG
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Cadherin-5 (Vascular endothelial cadherin) (VE-cadherin) (CD antigen CD144)
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MQVLVMLLAAAGTYLGLLTAPTAASNPGRQDTPSTLPLHRRQKRDWIWNQMHIDEEKNGSLPHYVGKIKSSVNHKNTKYQLKGESAGKVFRVDENTGDVYAFERLDREKIPEYQLVALVVDKNTEKNLESPSSFTIKVHDINDNWPVFTQLVFNASVPEMSVIGTSVIQLTAVDADDPTVADHASVIYRLKEGEEHFRIRGPGLIETASKNLDRETVPMYKIVVETQDAQGLRGDSGTATVFITLQDVNDNFPVFTQTRYTFSVPEDIRVGSPLGSLFVKDPDEPQNRKTKYSIVQGEYRDTFTIEPDPTRNEGIIKPMKPLDYERIQQYSFTIEATDPTIDLRYLSGTSTKNIARVIINVTDVDEPPNFKQPFYHFQLRENEKKPWIGSVLAVDPDAAQRSIGYSIRRTSDKGQFFGINKHGNIYNVKELDREVYPWYNLTVEAKELDSRGTPTGKESIVQVHIEVLDENDNAPEFAKPYEAKVCEDAPQGKLVVQISAIDKDVTPRDVKFKFSLSTEDSNFTLTDNHDNTANITVKHGYFDRERAKVHHLPILISDNGRPSLTGTSTLHVTVCKCNERGEFTLCEEMGAQVGVSIQALVAIFLCILTIAVISLLVYLRRRLRKQARAHGKSVPEIHEQLVTYDEEGGGEMDTTSYDVSVLNSVRHGGAKPPRPALDARPSLYAQVQKPPRHAPGAHAPGEMAAMIEVKKDEADHDGGGPPYDTLHIFGYEGAESIAESLSSLGTDSSDSDIDYDFLNDWGPRFKMLAELYGSDPREELLY
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Cadherins are calcium-dependent cell adhesion proteins (By similarity). They preferentially interact with themselves in a homophilic manner in connecting cells cadherins may thus contribute to the sorting of heterogeneous cell types (By similarity). This cadherin may play a important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions (By similarity). It associates with alpha-catenin forming a link to the cytoskeleton (By similarity). Acts in concert with KRIT1 and PALS1 to establish and maintain correct endothelial cell polarity and vascular lumen (By similarity). These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B (By similarity). Required for activation of PRKCZ and for localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction (By similarity).
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O02853
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PTGDS_BOVIN
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Prostaglandin-H2 D-isomerase (EC 5.3.99.2) (Glutathione-independent PGD synthase) (Lipocalin-type prostaglandin-D synthase) (Prostaglandin-D2 synthase) (PGD2 synthase) (PGDS) (PGDS2)
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MATPNRLWMALLLLGVLGVLQTPAPAQAALQPNFEEDKFLGRWFTSGLASNSSWFLEKKKVLSMCKSVVAPAADGGLNLTSTFLRKDQCETRTLLLRPAGPPGCYSYTSPHWSSTHEVSVAETDYETYALLYTEGVRGPGQDFRMATLYSRSQNPRAEVKEHFTTFAKSLGFTEEGIVFLPKTDKCMEEHP
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Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222, ECO:0000269|PubMed:9510973}.
|
O03042
|
RBL_ARATH
|
Ribulose bisphosphate carboxylase large chain (RuBisCO large subunit) (EC 4.1.1.39)
|
MSPQTETKASVGFKAGVKEYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEETQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALAALRLEDLRIPPAYTKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHAGTVVGKLEGDRESTLGFVDLLRDDYVEKDRSRGIFFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAVEGNEIIREACKWSPELAAACEVWKEITFNFPTIDKLDGQE
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (Probable). Binds to abscisic acid (ABA).
|
O03986
|
HS904_ARATH
|
Heat shock protein 90-4 (AtHSP90.4) (AtHsp90-4) (Heat shock protein 81-4) (Hsp81-4)
|
MADAETFAFQAEINQLLSLIINTFYSNKEIFLRELISNSSDALDKIRFESLTDKSKLDGQPELFIHIIPDKTNNTLTIIDSGIGMTKADLVNNLGTIARSGTKEFMEALAAGADVSMIGQFGVGFYSAYLVADKVVVTTKHNDDEQYVWESQAGGSFTVTRDTSGEALGRGTKMILYLKEDQMEYIEERRLKDLVKKHSEFISYPISLWIEKTIEKEISDDEEEEEKKDEEGKVEEIDEEKEKEEKKKKKIKEVTHEWDLVNKQKPIWMRKPEEINKEEYAAFYKSLSNDWEEHLAVKHFSVEGQLEFKAILFVPKRAPFDLFDTKKKPNNIKLYVRRVFIMDNCEDIIPDYLGFVKGIVDSEDLPLNISRETLQQNKILKVIRKNLVKKCLELFFEIAENKEDYNKFYEAFSKNLKLGIHEDSQNRTKIAELLRYHSTKSGDELTSLKDYVTRMKEGQNEIFYITGESKKAVENSPFLEKLKKKGYEVLYMVDAIDEYAIGQLKEFEGKKLVSATKEGLKLEETDDEKKKKEELKEKFEGLCKVIKDVLGDKVEKVIVSDRVVDSPCCLVTGEYGWTANMERIMKAQALKDSNTGGYMSSKKTMEINPENSIMDELRKRAEADKNDKSVKDLVLLLFETALLTSGFSLDEPNTFGSRIHRMLKLGLSIEEDDAVEADAEMPPLEDDADAEGSKMEEVD
|
Molecular chaperone which stabilizes unfolding protein intermediates and functions as a folding molecular chaperone that assists the non-covalent folding of proteins in an ATP-dependent manner.
|
O04017
|
NAC98_ARATH
|
Protein CUP-SHAPED COTYLEDON 2 (NAC domain-containing protein 98) (ANAC098) (NAC domain-containing protein CUC2)
|
MDIPYYHYDHGGDSQYLPPGFRFHPTDEELITHYLLRKVLDGCFSSRAIAEVDLNKCEPWQLPGRAKMGEKEWYFFSLRDRKYPTGLRTNRATEAGYWKATGKDREIFSSKTCALVGMKKTLVFYKGRAPKGEKSNWVMHEYRLEGKFSYHFISRSSKDEWVISRVFQKTTLASTGAVSEGGGGGGATVSVSSGTGPSKKTKVPSTISRNYQEQPSSPSSVSLPPLLDPTTTLGYTDSSCSYDSRSTNTTVTASAITEHVSCFSTVPTTTTALGLDVNSFSRLPPPLGFDFDPFPRFVSRNVSTQSNFRSFQENFNQFPYFGSSSASTMTSAVNLPSFQGGGGVSGMNYWLPATAEENESKVGVLHAGLDCIWNY
|
Transcription activator of STM and KNAT6. Involved in molecular mechanisms regulating shoot apical meristem (SAM) formation during embryogenesis and organ separation. Required for the fusion of septa of gynoecia along the length of the ovaries. Activates the shoot formation in callus in a STM-dependent manner. Controls leaf margin development and required for leaf serration. Involved in axillary meristem initiation and separation of the meristem from the main stem. Regulates the phyllotaxy throughout the plant development. Seems to act as an inhibitor of cell division.
|
O04019
|
PS6AB_ARATH
|
26S proteasome regulatory subunit 6A homolog B (26S proteasome AAA-ATPase subunit RPT5b) (Proteasome 26S subunit 6A homolog B) (Regulatory particle triple-A ATPase subunit 5b) (Tat-binding protein 1 homolog B) (TBP-1 homolog B)
|
MATAMAEDTSFEGDQLASMTTDDIGRASRLLANEIRILKEESQRTNLDLESVKEKIKENQEKIKLNKQLPYLVGNIVEILEMSPEDDAEEDGANIDLDSQRKGKCVVLKTSTRQTIFLPVVGLVDPDTLKPGDLVGVNKDSYLILDTLPSEYDSRVKAMEVDEKPTEDYNDIGGLEKQIQELVEAIVLPMTHKEQFEKLGIRPPKGVLLYGPPGTGKTLMARACAAQTNATFLKLAGPQLVQMFIGDGAKLVRDAFLLAKEKSPCIIFIDEIDAIGTKRFDSEVSGDREVQRTMLELLNQLDGFSSDDRIKVIAATNRADILDPALMRSGRLDRKIEFPHPTEEARGRILQIHSRKMNVNADVNFEELARSTDDFNGAQLKAVCVEAGMLALRRDATEVNHEDFNEGIIQVQAKKKASLNYYA
|
The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.
|
O04023
|
SRC2_ARATH
|
Protein SRC2 homolog (AtSRC2)
|
MECRSLDLTIISAEDLKDVQLIGKQDLYAVVSINGDARTKQKTKVDKDCGTKPKWKHQMKLTVDDAAARDNRLTLVFEIVADRPIAGDKPVGEVSVPVKELLDQNKGDEEKTVTYAVRLPNGKAKGSLKFSFKFGEKYTYGSSSGPHAPVPSAMDHKTMDQPVTAYPPGHGAPSAYPAPPAGPSSGYPPQGHDDKHDGVYGYPQQAGYPAGTGGYPPPGAYPQQGGYPGYPPQQQGGYPGYPPQGPYGYPQQGYPPQGPYGYPQQQAHGKPQKPKKHGKAGAGMGLGLGLGAGLLGGLLVGEAVSDIADMGDMGDMGDMGGFDF
|
May act as an activator of the calcium-dependent activation of RBOHF that mediates reactive oxygen species (ROS) production and may play a role in cold responses.
|
O04046
|
GGPP2_ARATH
|
Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 2 (GGPP synthase 2) (GGPS2) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase 2) (Dimethylallyltranstransferase 2) (EC 2.5.1.1) (Farnesyl diphosphate synthase 2) (Farnesyltranstransferase 2) (EC 2.5.1.29) (Geranyltranstransferase 2) (EC 2.5.1.10)
|
MEPQILFLYLSLFILSLNFFFTNLKPRLVRLFQPSLESRVKTALLSRKEVAAFLDSPIVEDEEGEEREEEEEGGIVSNANFTFEFDPYMMSKAESVNKALEEAIPVGEPLKIHEAMRYAILAAGKRVRPILCLASCELVGGQENAAMPAACAVEMIHTMSLIKDDLPCMDNDDLRRGKPTTHKVYGEGVAILSGGALLSLAFEHMTTAEISSERMVWAVRELARSIGTRGLVAGQAMDISSEGLDLNEVGLEHLEFIHVHKTAVLLETAAVLGAIIGGGSDEEIESVRKFARCIGLLFQVVDDILDETKSSEELGKTAGKDQLAGKLTYPKLIGLEKSKEFVKRLTKDARQHLQGFSSEKVAPLVALTTFIANRNK
|
Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase large subunit. In vitro, the large subunit catalyzes mainly the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate while the small subunit alone is inactive. Upon association of the two subunits, the product profile is not changed.
|
O04073
|
CTPA_TETOB
|
C-terminal processing peptidase, chloroplastic (EC 3.4.21.102) (D1 C-terminal processing protease) (Photosystem II D1 protein processing peptidase)
|
MHSRTNCLQTSVRAPQPHFRPFTAVKTCRQRCSTTAAAAKRDQAQEQQPWIQVGLGLAAAATAVAVGLGAAALPAQAVTSEQLLFLEAWRAVDRAYVDKSFNGQSWFKLRETYLKKEPMDRRAQTYDAIRKLLAVLDDPFTRFLEPSRLAALRRGTAGSVTGVGLEITYDGGSGKDVVVLTPAPGGPAEKAGARAGDVIVTVDGTAVKGLSLYDVSDLLQGEADSQVEVVLHAPGAPSNTRTLQLTRQKVTINPVTFTTCSNVAAAALPPGAAKQQLGYVRLATFNSNTTAAAQQAFTELSKQGVAGLVLDIRNNGGGLFPAGVNVARMLVDRGDLVLIADSQGIRDIYSADGNSIDSATPLVVLVNRGTASASEVLAGALKDSKRGLIAGERTFGKGLIQTVVDLSDGSGVAVTVARYQTPAGVDINKIGVSPDVQLDPEVLPTDLEGVCRVLGSDAAPRLFG
|
Protease involved in the C-terminal processing of the chloroplastic D1 protein of photosystem II. This proteolytic processing is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation.
|
O04121
|
CHMO_SPIOL
|
Choline monooxygenase, chloroplastic (EC 1.14.15.7)
|
MMAASASATTMLLKYPTTVCGIPNPSSNNNNDPSNNIVSIPQNTTNPTLKSRTPNKITTNAVAAPSFPSLTTTTPSSIQSLVHEFDPQIPPEDAHTPPSSWYTEPAFYSHELERIFYKGWQVAGISDQIKEPNQYFTGSLGNVEYLVSRDGEGKVHAFHNVCTHRASILACGSGKKSCFVCPYHGWVYGMDGSLAKASKAKPEQNLDPKELGLVPLKVAVWGPFVLISLDRSLEEGGDVGTEWLGTSAEDVKAHAFDPSLQFIHRSEFPMESNWKIFSDNYLDSSYHVPYAHKYYATELNFDTYDTQMIENVTIQRVEGSSNKPDGFDRVGIQAFYAFAYPNFAVERYGPWMTTMHIHPLGPRKCKLVVDYYIENSMLDDKDYIEKGIAINDNVQREDVVLCESVQRGLETPAYRSGRYVMPIEKGIHHFHCWLQQTLK
|
Catalyzes the first step of the osmoprotectant glycine betaine synthesis.
|
O04130
|
SERA2_ARATH
|
D-3-phosphoglycerate dehydrogenase 2, chloroplastic (PGDH) (EC 1.1.1.95)
|
MAFSSSCSSVKAVNSRWTSPSPSPSSRFAVLPAFLHRRYATSVKLTAISAALKTVEQTTLTEDNRFSTVGSDSDEYNPTLPKPRILVTEKLGEAGVNLLREFGDVDCSYDLSPEDLKKKVAESDALIVRSGTKVTREVFEAAKGRLKVVGRAGVGIDNVDLQAATEHGCLVVNAPTANTVAAAEHGIALLASMARNVAQADASIKAGKWERSKYVGVSLVGKTLAVMGFGKVGTEVARRAKGLGMTVISHDPYAPADRARALGVDLVSFDQAISTADFVSLHMPLTPATKKVFNDETFSKMKKGVRLINVARGGVIDEDALVRALDAGIVAQAALDVFCEEPPSKDSRLIQHENVTVTPHLGASTKEAQEGVAIEIAEAVAGALKGELSATAVNAPMVAPEVLSELTPYIVLAEKLGRLAVQLASGGKGVQSIRVVYRSARDRDDLDTRLLRAMITKGIIEPISDSYVNLVNADFIAKQKGLRISEERMVVDSSPEYPVDSIQVQILNVESNFAGAVSDAGDISIEGKVKYGVPHLTCVGSFGVDVSLEGNLILCRQVDQPGMIGQVGNILGEQNVNVNFMSVGRTVLRKQAIMAIGVDEEPDNKTLERIGGVSAIEEFVFLKL
|
Involved in the plastidial phosphorylated pathway of serine biosynthesis (PPSB).
|
O04147
|
CPD_ARATH
|
Cyclic phosphodiesterase (CPDase) (EC 3.1.4.37)
|
MEEVKKDVYSVWALPDEESEPRFKKLMEALRSEFTGPRFVPHVTVAVSAYLTADEAKKMFESACDGLKAYTATVDRVSTGTFFFQCVFLLLQTTPEVMEAGEHCKNHFNCSTTTPYMPHLSLLYAELTEEEKKNAQEKAYTLDSSLDGLSFRLNRLALCKTDTEDKTLETWETVAVCNLNP
|
Hydrolyzes ADP-ribose 1'',2''-cyclic phosphate (Appr>1) that is produced during tRNA splicing into ADP-ribose 1''-phosphate (Appr-1''p). Acts also on nucleoside 2',3'-cyclic phosphates.
|
O04151
|
CALR1_ARATH
|
Calreticulin-1
|
MAKLNPKFISLILFALVVIVSAEVIFEEKFEDGWEKRWVKSDWKKDDNTAGEWKHTAGNWSGDANDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYMKLLSDDVDQTKFGGDTPYSIMFGPDICGYSTKKVHAILTYNGTNHLIKKEVPCETDQLTHVYTFVLRPDATYSILIDNVEKQTGSLYSDWDLLPAKKIKDPSAKKPEDWDDKEYIPDPEDTKPAGYDDIPKEIPDTDAKKPEDWDDEEDGEWTAPTIPNPEYNGEWKPKKIKNPAYKGKWKAPMIDNPEFKDDPELYVFPKLKYVGVELWQVKSGSLFDNVLVSDDPEYAKKLAEETWGKHKDAEKAAFDEAEKKREEEESKDAPAESDAEEEAEDDDNEGDDSDNESKSEETKEAEETKEAEETDAAHDEL
|
Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
|
O04153
|
CALR3_ARATH
|
Calreticulin-3 (Protein PRIORITY IN SWEET LIFE 1)
|
MGLPQNKLSFFCFFFLVSVLTLAPLAFSEIFLEEHFEGGWKSRWVLSDWKRNEGKAGTFKHTAGKWPGDPDNKGIQTYNDAKHYAISAKIPEFSNKNRTLVVQYSVKIEQDIECGGAYIKLLSGYVNQKQFGGDTPYSLMFGPDICGTQTKKLHVIVSYQGQNYPIKKDLQCETDKLNHFYTFILRPDASYSVLVDNKEREFGSMYTDWDILPPRKIKVKNAKKPEDWDDREYIDDPNDVKPEGFDSIPREIPDRKAKEPEDWDEEENGLWEPPKIPNSAYKGPWKAKRIKNPNYKGKWKNPWIDNPEFEDDPDLYVLKSIKYAGIEVWQVKAGSIFDNILICDDPAYARSIVDDYFAQHRESEKELFAEAEKERKAREDEEARIAREEGERRRKERDHRYGDRRRRYKRPNPRDYMDDYHDEL
|
Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling.
|
O04157
|
RAG3B_ARATH
|
Ras-related protein RABG3b (AtRABG3b) (Ras-related protein Rab75) (AtRab75)
|
MSTRRRTLLKVIILGDSGVGKTSLMNQYVNNKFSQQYKATIGADFVTKELQIDDRLVTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNHLKSFESLDNWHNEFLTRASPRDPMAFPFILLGNKVDIDGGNSRVVSEKKAREWCAEKGNIVYFETSAKEDYNVDDSFLCITKLALANERDQDIYFQPDTGSVPEQRGGCAC
|
Intracellular vesicle trafficking and protein transport. Functions in autophagy. Involved in xylem and tracheary element differentiation.
|
O04196
|
ISOA1_ARATH
|
Isoamylase 1, chloroplastic (AtISA1) (EC 3.2.1.68) (Protein REDUCED GRAVITROPIC 3)
|
MDAIKCSSSFLHHTKLNTLFSNHTFPKISAPNFKPLFRPISISAKDRRSNEAENIAVVEKPLKSDRFFISDGLPSPFGPTVRDDGVNFSVYSTNSVSATICLISLSDLRQNKVTEEIQLDPSRNRTGHVWHVFLRGDFKDMLYGYRFDGKFSPEEGHYYDSSNILLDPYAKAIISRDEFGVLGPDDNCWPQMACMVPTREEEFDWEGDMHLKLPQKDLVIYEMHVRGFTRHESSKIEFPGTYQGVAEKLDHLKELGINCIELMPCHEFNELEYYSYNTILGDHRVNFWGYSTIGFFSPMIRYASASSNNFAGRAINEFKILVKEAHKRGIEVIMDVVLNHTAEGNEKGPIFSFRGVDNSVYYMLAPKGEFYNYSGCGNTFNCNHPVVRQFILDCLRYWVTEMHVDGFRFDLGSIMSRSSSLWDAANVYGADVEGDLLTTGTPISCPPVIDMISNDPILRGVKLIAEAWDAGGLYQVGMFPHWGIWSEWNGKFRDVVRQFIKGTDGFSGAFAECLCGSPNLYQGGRKPWHSINFICAHDGFTLADLVTYNNKNNLANGEENNDGENHNYSWNCGEEGDFASISVKRLRKRQMRNFFVSLMVSQGVPMIYMGDEYGHTKGGNNNTYCHDNYMNYFRWDKKEEAHSDFFRFCRILIKFRDECESLGLNDFPTAKRLQWHGLAPEIPNWSETSRFVAFSLVDSVKKEIYVAFNTSHLATLVSLPNRPGYRWEPFVDTSKPSPYDCITPDLPERETAMKQYRHFLDANVYPMLSYSSIILLLSPIKDP
|
Involved in the trimming of pre-amylopectin chains. Accelerates the crystallization of nascent amylopectin molecules during starch synthesis. ISA1 and ISA2 work exclusively together as a multimeric holoenzyme. ISA1-ISA2 removes preferentially branches that are very close to other branches. Promotes negative gravitropic responses in shoots by facilitating starch granules (statoliths) formation in hypocotyls.
|
O04197
|
COI1_ARATH
|
Coronatine-insensitive protein 1 (COI-1) (F-box/LRR-repeat protein 2) (AtCOI1) (AtFBL2)
|
MEDPDIKRCKLSCVATVDDVIEQVMTYITDPKDRDSASLVCRRWFKIDSETREHVTMALCYTATPDRLSRRFPNLRSLKLKGKPRAAMFNLIPENWGGYVTPWVTEISNNLRQLKSVHFRRMIVSDLDLDRLAKARADDLETLKLDKCSGFTTDGLLSIVTHCRKIKTLLMEESSFSEKDGKWLHELAQHNTSLEVLNFYMTEFAKISPKDLETIARNCRSLVSVKVGDFEILELVGFFKAAANLEEFCGGSLNEDIGMPEKYMNLVFPRKLCRLGLSYMGPNEMPILFPFAAQIRKLDLLYALLETEDHCTLIQKCPNLEVLETRNVIGDRGLEVLAQYCKQLKRLRIERGADEQGMEDEEGLVSQRGLIALAQGCQELEYMAVYVSDITNESLESIGTYLKNLCDFRLVLLDREERITDLPLDNGVRSLLIGCKKLRRFAFYLRQGGLTDLGLSYIGQYSPNVRWMLLGYVGESDEGLMEFSRGCPNLQKLEMRGCCFSERAIAAAVTKLPSLRYLWVQGYRASMTGQDLMQMARPYWNIELIPSRRVPEVNQQGEIREMEHPAHILAYYSLAGQRTDCPTTVRVLKEPI
|
Required for jasmonate-regulated plant fertility and defense processes, and for coronatine and/or other elicitors perceptions/responses. Seems to not be required for meiosis. Required for the regulation of some genes induced by wounding, but not for all. Component of SCF(COI1) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including the ribulose bisphosphate carboxylase small chain 1B RBCS-1B and the histone deacetylase HDA6). These SCF complexes play crucial roles in regulating response to jasmonate, and their interactions with the COP9 signalosome (CSN) appear to be important for their activity. Interacts with TIFY10A and inositol pentakisphosphate to form a high-affinity jasmonates coreceptor. Involved in the regulation of plant gene expression during plant-pathogen interactions with Pseudomonas syringae and Alternaria brassicicola.
|
O04200
|
PXN_ARATH
|
Peroxisomal nicotinamide adenine dinucleotide carrier (Peroxisomal NAD carrier) (Peroxisomal membrane protein 38, (PMP36)) (AtPMP38) (Protein ABERRANT PEROXISOME MORPHOLOGY 3) (Solute carrier family 25 member 17)
|
MSDALINGLAGAGGGIIAQLLTYPLQTVNTRQQTERDLKREKRKLGTIEHMCQVVKQEGWERLYGGLAPSLAGTAASQGVYYYFYQVFRNRAEATALARKKKGLGDGSVGMFASLLVAAFAGSVNVLMTNPIWVIVTRMQTHRKMTKDQTAAPESPSSNAEALVAVEPRPYGTFNTIREVYDEAGITGFWKGVIPTLIMVSNPSMQFMLYETMLTKLKKKRALKGSNNVTALETFLLGAVAKLGATVTTYPLLVVKSRLQAKQVTTGDKRQQYKGTLDAILKMIRYEGLYGFYKGMSTKIVQSVLAAAVLFMIKEELVKGAKLLLSNATSS
|
Mediates the NAD(+) import into peroxisomes. Favors the NAD(+)(in)/AMP(out) antiport exchange, but is also able to catalyze a low unidirectional transport that might be essential under special conditions. Transports CoA, dephospho-CoA, acetyl-CoA, adenosine 3',5'-diphosphate (PAP), NAD(+), AMP, ADP and NADH, but has no activity with ATP, GTP, GDP, NADPH, NADP(+) or FAD. Required for peroxisomes proliferation.
|
O04202
|
EIF3F_ARATH
|
Eukaryotic translation initiation factor 3 subunit F (eIF3f) (eIF-3-epsilon) (eIF3 p32 subunit)
|
MAATSEHTILQFVSPSSTASATTSVLTARIHPLVIFNVCDCFVRRPDSAERVIGTLLGSILPDGTVDIRNSYAVPHNESSDQVAVDIDYHHNMLASHLKVNSKETIVGWYSTGAGVNGGSSLIHDFYAREVPNPIHLTVDTGFTNGEGTIKAFVSSNLSLGDRQLVAHFQEIPVDLRMVDAERVGFDVLKATSVDKLPNDLEGMELTMERLLTLINDVYKYVDSVVGGQIAPDNNIGRFIADAVASLPKLPPQVFDNLVNDSLQDQLLLLYLSSITRTQLSLAEKLNTAAQML
|
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation (Potential). Involved in cell growth and differentiation, especially during embryogenesis and male gametophyte germination. Regulates sensitivity to sugars (e.g. sucrose). {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:20444226}.
|
O04209
|
CLC2_ARATH
|
Clathrin light chain 2
|
MSAFEDDSFVILNDDASESVPVSGSFDATDSFSAFDGSLQVEDSVDDVFAAPSSDYGAYSNGDGIFGSNGDHDGPILPPPSEMESDEGFALREWRRQNAIQLEEKEKREKELLKQIIEEADQYKEEFHKKIEVTCENNKAANREKEKLYLENQEKFYAESSKNYWKAIAELVPKEVPTIEKRRGKKEQQDPKKPTVSVIQGPKPGKPTDLTRMRQILVKLKHNPPSHLKLTSQPPSEEAAAPPKNVPETKPTEAVTAA
|
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
|
O04211
|
ELF4_ARATH
|
Protein EARLY FLOWERING 4 (Protein ARRHYTHMIC 44)
|
MKRNGETKRRRNVAEEAEQGEDPAMWENLDRNFRQVQSVLDRNRSLIQQVNDNHQSRMADNMSKNVALIQELNGNISKVVNMYSDLNTSFSSGFHGGKNGHDGGGAAGTRA
|
Component of the central CCA1/LHY-TOC1 feedback loop in the circadian clock that promotes clock accuracy and is required for sustained rhythms in the absence of daily light/dark cycles. Part of a corepressor complex consisting of ELF4, ELF3, and LUX involved in the transcriptional regulation of APRR9. Increases ELF3 nuclear distribution and localization in nuclear bodies. Required for responsiveness to continuous red, by regulating phytochrome B (phyB) signaling (including during seedling de-etiolation) and gene expression. Mediates both entrainment to an environmental cycle and circadian rhythm sustainability under constant conditions. Controls flowering time. Necessary for light-induced expression of both CCA1 and LHY.
|
O04226
|
P5CS1_ORYSJ
|
Delta-1-pyrroline-5-carboxylate synthase 1 (OsP5CS1) [Includes: Glutamate 5-kinase (GK) (EC 2.7.2.11) (Gamma-glutamyl kinase); Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase)]
|
MASVDPSRSFVRDVKRVIIKVGTAVVSRQDGRLALGRVGALCEQVKELNSLGYEVILVTSGAVGVGRQRLRYRKLVNSSFADLQKPQMELDGKACAAVGQSGLMALYDMLFNQLDVSSSQLLVTDSDFENPKFREQLTETVESLLDLKVIPIFNENDAISTRKAPYEDSSGIFWDNDSLAGLLALELKADLLILLSDVDGLYSGPPSEPSSKIIHTYIKEKHQQEITFGDKSRVGRGGMTAKVKAAVLASNSGTPVVITSGFENRSILKVLHGEKIGTLFHKNANLWESSKDVSTREMAVAARDCSRHLQNLSSEERKKILLDVADALEANEDLIRSENEADVAAAQVAGYEKPLVARLTIKPGKIASLAKSIRTLANMEDPINQILKKTEVADDLVLEKTSCPLGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAIRSNTILHKVITDAIPRNVGEKLIGLVTTRDEIADLLKLDDVIDLVIPRGSNKLVSQIKASTKIPVLGHADGICHVYIDKSADMDMAKHIVMDAKIDYPAACNAMETLLVHKDLMKSPGLDDILVALKTEGVNIYGGPIAHKALGFPKAVSFHHEYSSMACTVEFVDDVQSAIDHIHRYGSAHTDCIVTTDDKVAETFLRRVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWILRGRGQVVNGDKDVVYTHKSLPLQ
|
P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants. Involved in abiotic stress tolerance. {ECO:0000269|Ref.8}.
|
O04291
|
ATB14_ARATH
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Homeobox-leucine zipper protein ATHB-14 (HD-ZIP protein ATHB-14) (Homeodomain transcription factor ATHB-14) (Protein PHABULOSA)
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MMMVHSMSRDMMNRESPDKGLDSGKYVRYTPEQVEALERVYTECPKPSSLRRQQLIRECPILSNIEPKQIKVWFQNRRCREKQRKEAARLQTVNRKLNAMNKLLMEENDRLQKQVSNLVYENGHMKHQLHTASGTTTDNSCESVVVSGQQHQQQNPNPQHQQRDANNPAGLLSIAEEALAEFLSKATGTAVDWVQMIGMKPGPDSIGIVAISRNCSGIAARACGLVSLEPMKVAEILKDRPSWLRDCRSVDTLSVIPAGNGGTIELIYTQMYAPTTLAAARDFWTLRYSTCLEDGSYVVCERSLTSATGGPTGPPSSNFVRAEMKPSGFLIRPCDGGGSILHIVDHVDLDAWSVPEVMRPLYESSKILAQKMTVAALRHVRQIAQETSGEVQYGGGRQPAVLRTFSQRLCRGFNDAVNGFVDDGWSPMGSDGAEDVTVMINLSPGKFGGSQYGNSFLPSFGSGVLCAKASMLLQNVPPAVLVRFLREHRSEWADYGVDAYAAASLRASPFAVPCARAGGFPSNQVILPLAQTVEHEESLEVVRLEGHAYSPEDMGLARDMYLLQLCSGVDENVVGGCAQLVFAPIDESFADDAPLLPSGFRIIPLEQKSTPNGASANRTLDLASALEGSTRQAGEADPNGCNFRSVLTIAFQFTFDNHSRDSVASMARQYVRSIVGSIQRVALAIAPRPGSNISPISVPTSPEALTLVRWISRSYSLHTGADLFGSDSQTSGDTLLHQLWNHSDAILCCSLKTNASPVFTFANQTGLDMLETTLVALQDIMLDKTLDEPGRKALCSEFPKIMQQGYAHLPAGVCASSMGRMVSYEQATVWKVLEDDESNHCLAFMFVNWSFV
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Probable transcription factor involved in the determination of adaxial-abaxial polarity in ovule primordium. Specifies adaxial leaf fates.
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O04292
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ATBH9_ARATH
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Homeobox-leucine zipper protein ATHB-9 (HD-ZIP protein ATHB-9) (Homeodomain transcription factor ATHB-9) (Protein PHAVOLUTA)
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MMAHHSMDDRDSPDKGFDSGKYVRYTPEQVEALERVYAECPKPSSLRRQQLIRECPILCNIEPRQIKVWFQNRRCREKQRKESARLQTVNRKLSAMNKLLMEENDRLQKQVSNLVYENGFMKHRIHTASGTTTDNSCESVVVSGQQRQQQNPTHQHPQRDVNNPANLLSIAEETLAEFLCKATGTAVDWVQMIGMKPGPDSIGIVAVSRNCSGIAARACGLVSLEPMKVAEILKDRPSWFRDCRCVETLNVIPTGNGGTIELVNTQIYAPTTLAAARDFWTLRYSTSLEDGSYVVCERSLTSATGGPNGPLSSSFVRAKMLSSGFLIRPCDGGGSIIHIVDHVDLDVSSVPEVLRPLYESSKILAQKMTVAALRHVRQIAQETSGEVQYSGGRQPAVLRTFSQRLCRGFNDAVNGFVDDGWSPMSSDGGEDITIMINSSSAKFAGSQYGSSFLPSFGSGVLCAKASMLLQNVPPLVLIRFLREHRAEWADYGVDAYSAASLRATPYAVPCVRTGGFPSNQVILPLAQTLEHEEFLEVVRLGGHAYSPEDMGLSRDMYLLQLCSGVDENVVGGCAQLVFAPIDESFADDAPLLPSGFRVIPLDQKTNPNDHQSASRTRDLASSLDGSTKTDSETNSRLVLTIAFQFTFDNHSRDNVATMARQYVRNVVGSIQRVALAITPRPGSMQLPTSPEALTLVRWITRSYSIHTGADLFGADSQSCGGDTLLKQLWDHSDAILCCSLKTNASPVFTFANQAGLDMLETTLVALQDIMLDKTLDDSGRRALCSEFAKIMQQGYANLPAGICVSSMGRPVSYEQATVWKVVDDNESNHCLAFTLVSWSFV
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Probable transcription factor involved in the determination of adaxial-abaxial polarity in ovule primordium. Specifies adaxial leaf fates. Binds to the DNA sequence 5'-GTAAT[GC]ATTAC-3'.
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O04294
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IMPA3_ARATH
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Importin subunit alpha-3 (IMPa-3) (Karyopherin subunit alpha-2) (KAP-alpha-2) (Protein MODIFIER OF SNC1 6)
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MSLRPSAKTEVRRNRYKVAVDAEEGRRRREDNLVEIRKNKREENLQKKRFTSSMAFGSATGQTEQDLSSANQLKDNLPAMVAGIWSEDSNSQLEATNLLRKLLSIEQNPPINEVVQSGVVPRVVKFLSRDDFPKLQFEAAWALTNIASGTSENTNVIIESGAVPIFIQLLSSASEDVREQAVWALGNVAGDSPKCRDLVLSYGAMTPLLSQFNENTKLSMLRNATWTLSNFCRGKPPPAFEQTQPALPVLERLVQSMDEEVLTDACWALSYLSDNSNDKIQAVIEAGVVPRLIQLLGHSSPSVLIPALRTIGNIVTGDDLQTQMVLDQQALPCLLNLLKNNYKKSIKKEACWTISNITAGNADQIQAVIDAGIIQSLVWVLQSAEFEVKKEAAWGISNATSGGTHDQIKFMVSQGCIKPLCDLLTCPDLKVVTVCLEALENILVVGEAEKNLGHTGEDNLYAQMIDEAEGLEKIENLQSHDNNDIYDKAVKILETFWTEDNEEEGNDENHAPQSGFQFGSTNVPPGQFNFI
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Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope (By similarity). Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation. May be involved in the regulation of pathogen-induced salicylic acid accumulation.
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O04300
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RGP1_PEA
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Probable UDP-arabinopyranose mutase 1 (EC 5.4.99.30) (Reversibly glycosylated polypeptide 1) (RGP1) (UDP-L-arabinose mutase 1) (UDP-glucose:protein transglucosylase) (UPTG)
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MASLPKPTPLLKDELDIVIPTIRNLDFLEMWRPFFEQYHLIIVQDGDPSKVIKVPEGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPTGHEINALEQHIKNLLSPSTPFFFNTLYDPYREGTDFVRGYPFSLREGVPTAVSHGLWLNIPDYDAPTQLVKPHERNTRFVDAVLTIPKGSLFPMCGMNLAFNRELIGPAMYFGLMGDGQPIGRYDDMWAGWCIKVICDHLGYGVKTGLPYIWHSKASNPFVNLKKEYKGIFWQEEIIPFFQAATLSKDCTSVQKCYIELSKQVKEKLGTIDPYFIKLADAMVTWVEAWDEINNNKSEETTSTKASEVAATK
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Probable UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides (By similarity). Was initially shown to possess an autoglycosylating activity which is dependent on the presence of UDP-glucose and manganese.
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O04308
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MPPA2_ARATH
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Probable mitochondrial-processing peptidase subunit alpha-2, chloroplastic/mitochondrial (Alpha-MPP 2) (Complex III subunit II) (Core protein II) (Cytochrome b-c1 complex subunit 2-2, mitochondrial) (Inactive zinc metalloprotease alpha-2) (Ubiquinol-cytochrome c oxidoreductase core protein 2-2)
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MYRTAASRAKALKGILNHNFRASRYASSSAVATSSSSSSWLSGGYSSSLPSMNIPLAGVSLPPPLSDHVEPSKLKTTTLPNGLTIATEMSPNPAASIGLYVDCGSIYETPQFRGATHLLERMAFKSTLNRSHFRLVREIEAIGGNTSASASREQMGYTIDALKTYVPEMVEVLIDSVRNPAFLDWEVNEELRKVKVEIGEFATNPMGFLLEAVHSAGYSGALANPLYAPESAITGLTGEVLENFVFENYTASRMVLAASGVDHEELLKVVEPLLSDLPNVPRPAEPKSQYVGGDFRQHTGGEATHFALAFEVPGWNNEKEAIIATVLQMLMGGGGSFSAGGPGKGMHSWLYLRLLNQHQQFQSCTAFTSVFNNTGLFGIYGCTSPEFASQGIELVASEMNAVADGKVNQKHLDRAKAATKSAILMNLESRMIAAEDIGRQILTYGERKPVDQFLKTVDQLTLKDIADFTSKVITKPLTMATFGDVLNVPSYDSVSKRFR
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Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins. Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
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O04314
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JAL30_ARATH
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PYK10-binding protein 1 (Jacalin-related lectin 30) (Jasmonic acid-induced protein)
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MAQKVEAQGGKGANLWDDGSTHDAVTKIQLAAGIDGIQYVQFDYVKNGQPEQAPLRGTKGRVLPADPFVINHPDEHLVSVEGWYSPEGIIQGIKFISNKKTSDVIGSDEGTHFTLQVKDKKIIGFHGSAGGNLNSLGAYFAPLTTTTPLTPAKQLTAFGSDDGTVWDDGAYVGVKKVYVGQAQDGISAVKFVYDKSPEEVTGEEHGKSTLLGFEEFVLDYPSEYITAVDGTYDKIFGSDGSVITMLRFKTNKQTSPPFGLEAGTVFELKEEGHKIVGFHGRADVLLHKIGVHVRPLSN
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Inhibitor-type lectin that may regulate the correct polymerization of BGLU23/PYK10 upon tissue damage. Activates BGLU21, BGLU22 and BGLU23.
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O04316
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JAL29_ARATH
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Thiohydroximate-O-sulfate sulfur/sulfate-lyase (nitrile-forming) NSP4 (EC 4.8.1.5) (Jacalin-related lectin 29) (Nitrile-specifier protein 4) (AtNSP4)
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MAQKVEAQGGNGGNQWDDGSEYDAVTKIQVAAGGNGIEYVKFTYVKNGQTEEAPLRGVKGRSFEADPFVINHPEEHLVSVEGRYNPEGLILGLTFKSNKKTSDLIGYEDGTPFTLQVQDKKIVGFYGFAGNNLHSLGAYFAPLTNVTPLNAKKLEAKGGDTGDIWDDGVYDNVRKVYVGQAQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEIDADDYIVYVEGYREKVNGMTSEMITFLSFKTYKGKTSQPIEQRPGIKFVLQGGKIVGFHGRSTDVLDSLGAYISLSPTPNLHGKWTKVDENGDGPGLRCSHDIAQVGNKIYSFGGEFTPNQPIDKHLYVFDIESRTWSISPATGDIPTLSCLGVCMVSIGSTLYVFGGRDASRQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLNTLDSYNIVDKKWFHCSTPGDSLTARGGAGLEVVQGKVWVVYGFNGCEVDDVHYYDPVQDKWTQVETFGVRPSERSVFASAALGKHIVIFGGEIAMDPLAHVGPGQLTDGTFALDTETLQWERLDKFGGEEETPSSRGWTASTTATIGGKKGLVMHGGKAPTNDRFDDLFFYGIDSA
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Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate and benzylglucosinolate (glucotropaeolin) to their corresponding simple nitriles in the presence of myrosinase.
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O04318
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JAL27_ARATH
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Thiohydroximate-O-sulfate sulfur/sulfate-lyase (nitrile-forming) NSP3 (EC 4.8.1.5) (Jacalin-related lectin 27) (Nitrile-specifier protein 3) (AtNSP3)
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MAQKLVAQGGETGDVWDDGVYDNVTKVYVGQGQYGIAFVKFEYANGSEVVVGDEHGEKTELGVEEFEIDSDDYIVYVEGYREKVSDMTSEMITFLSFKTSKGKTSQPIVKKPGVKFVLHGGKIVGFHGRSTDVLHSLGAYVSLPSTPKLLGNWIKVEQNGEGPGLRCSHGIAQVGNKIYSFGGELIPNQPIDKHLYVFDLETRTWSIAPATGDVPHLSCLGVRMVSVGSTLYTFGGRDFSRQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVGAMDRIKTLDSYNIVDKTWFHCSNPGDSFSIRGGAGLEVVQGKVWIVYGFNGCEVDDVHFYDPAEDKWTQVETFGVKPNERSVFASAAIGKHIVIFGGEIAMDPRAHVGPGQLIDGTFALDTETLQWERLDKFEGTPSSRGWTASTTGTIDGKKGLVMHGGKAPTNDRFDDLFFYGIDSV
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Specifier protein responsible for constitutive and herbivore-induced simple nitrile formation, especially in roots. Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate and benzylglucosinolate (glucotropaeolin) to their corresponding simple nitriles in the presence of myrosinase.
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O04331
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PHB3_ARATH
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Prohibitin-3, mitochondrial (Atphb3) (Protein ENHANCED ETHYLENE RESPONSE 3)
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MGSQQAAVSFLSNLAKAAFGLGTAATVLNTSLFTVDGGERAVIFDRFRGVMDQTVGEGTHFLIPILQRPHIFDIRTKPHTFSSISGTKDLQMVNLTLRVLSRPEVSRLPYIFQTLGLEYDEKVLPSIGNEVLKAVVAQFNADQLLTERPHVSALVRESLITRAKDFNIVLDDVAITHLSYGVEFSRAVEQKQVAQQEAERSKFVVMKADQERRAAVIRAEGESEAAQLISDATAKAGMGLIELRRIEASREIASTLARSPNVAYLPGGQSMLFALNR
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Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins (By similarity). Necessary for mitochondrial and cell metabolism and biogenesis. Required to regulate the ethylene-mediated signaling involved in growth maintenance in the presence of ethylene. Functions in nitric oxide (NO)-mediated responses and in hydrogen peroxide-induced NO accumulation. {ECO:0000250, ECO:0000269|PubMed:17525078, ECO:0000269|PubMed:17883375, ECO:0000269|PubMed:20068191}.
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O04350
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TBCA_ARATH
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Tubulin-folding cofactor A (AtTFCA) (CFA) (Protein KIESEL) (TCP1-chaperonin cofactor A) (Tubulin-specific chaperone A)
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MATIRNLKIKTSTCKRIVKELHSYEKEVEREAAKTADMKDKGADPYDLKQQENVLGESRMMIPDCHKRLESALADLKSTLAELEETDEKEGPEIEDAKKTVADVEKQFPTEDA
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Tubulin-folding protein involved in the control of the alpha-/beta-tubulin monomer balance. Functions as a reservoir of bound and non-toxic beta-tubulin. Required in the developing embryo.
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O04373
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ILL4_ARATH
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IAA-amino acid hydrolase ILR1-like 4 (EC 3.5.1.-) (jasmonoyl-L-amino acid hydrolase) (EC 3.5.1.127)
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MSFFKWVSFVLILHLLNPTLISCSSNGLSQIPSKFLTLAKRNDFFDWMVGIRRRIHENPELGYEEVETSKLVRAELEKMGVSYKYPVAVTGVVGYVGTGHAPFVALRADMDALAMQEMVEWEHKSKVPGKMHACGHDAHTTMLLGAAKLLKEHEEELQGTVVLVFQPAEEGGGGAKKIVEAGVLENVSAIFGLHVTNQLALGQVSSREGPMLAGSGFFKAKISGKGGHAALPQHTIDPILAASNVIVSLQHLVSREADPLDSQVVTVAKFEGGGAFNVIPDSVTIGGTFRAFSTKSFMQLKKRIEQVITRQASVNMCNATVDFIEEEKPFFPPTVNDKALHQFFKNVSGDMLGIENYVEMQPLMGSEDFSFYQQAIPGHFSFVGMQNKARSPMASPHSPYFEVNEELLPYGASLHASMATRYLLELKASTLNKSNKKDEL
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Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA), including IAA-Ala, IAA-Asn, IAA-Cys, IAA-Glu, IAA-Met, IAA-Ser and IAA-Gly. Has a lower efficiency with IAA-Phe, IAA-Leu and IAA-Val and no activity with IAA-Ile. Important for IAA-Leu hydrolysis in roots. Also hydrolyzes amino acid conjugates of jasmonic acid and 12-hydroxy jasmonic acid.
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O04378
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SYP23_ARATH
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Syntaxin-23 (AtPLP) (AtSYP23) (AtPEP12-like protein)
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MSFQDLEAGRGRSLASSRNINGGGSRQDTTQDVASGIFQINTSVSTFHRLVNTLGTPKDTPELREKLHKTRLYIGQLVKDTSAKLKEASETDHQRGVNQKKKIVDAKLAKDFQAVLKEFQKAQRLAAERETVYAPLVHKPSLPSSYTSSEIDVNGDKHPEQRALLVESKRQELVLLDNEIAFNEAVIEEREQGIQEIQQQIGEVHEIFKDLAVLVHDQGNMIDDIGTHIDNSYAATAQGKSHLVRHQRHKDQILL
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May function in the docking or fusion of transport vesicles with the prevacuolar membrane.
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O04379
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AGO1_ARATH
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Protein argonaute 1
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MVRKRRTDAPSEGGEGSGSREAGPVSGGGRGSQRGGFQQGGGQHQGGRGYTPQPQQGGRGGRGYGQPPQQQQQYGGPQEYQGRGRGGPPHQGGRGGYGGGRGGGPSSGPPQRQSVPELHQATSPTYQAVSSQPTLSEVSPTQVPEPTVLAQQFEQLSVEQGAPSQAIQPIPSSSKAFKFPMRPGKGQSGKRCIVKANHFFAELPDKDLHHYDVTITPEVTSRGVNRAVMKQLVDNYRDSHLGSRLPAYDGRKSLYTAGPLPFNSKEFRINLLDEEVGAGGQRREREFKVVIKLVARADLHHLGMFLEGKQSDAPQEALQVLDIVLRELPTSRYIPVGRSFYSPDIGKKQSLGDGLESWRGFYQSIRPTQMGLSLNIDMSSTAFIEANPVIQFVCDLLNRDISSRPLSDADRVKIKKALRGVKVEVTHRGNMRRKYRISGLTAVATRELTFPVDERNTQKSVVEYFHETYGFRIQHTQLPCLQVGNSNRPNYLPMEVCKIVEGQRYSKRLNERQITALLKVTCQRPIDREKDILQTVQLNDYAKDNYAQEFGIKISTSLASVEARILPPPWLKYHESGREGTCLPQVGQWNMMNKKMINGGTVNNWICINFSRQVQDNLARTFCQELAQMCYVSGMAFNPEPVLPPVSARPEQVEKVLKTRYHDATSKLSQGKEIDLLIVILPDNNGSLYGDLKRICETELGIVSQCCLTKHVFKMSKQYMANVALKINVKVGGRNTVLVDALSRRIPLVSDRPTIIFGADVTHPHPGEDSSPSIAAVVASQDWPEITKYAGLVCAQAHRQELIQDLFKEWKDPQKGVVTGGMIKELLIAFRRSTGHKPLRIIFYRDGVSEGQFYQVLLYELDAIRKACASLEAGYQPPVTFVVVQKRHHTRLFAQNHNDRHSVDRSGNILPGTVVDSKICHPTEFDFYLCSHAGIQGTSRPAHYHVLWDENNFTADGLQSLTNNLCYTYARCTRSVSIVPPAYYAHLAAFRARFYMEPETSDSGSMASGSMARGGGMAGRSTRGPNVNAAVRPLPALKENVKRVMFYC
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Involved in RNA-mediated post-transcriptional gene silencing (PTGS). Main component of the RNA-induced silencing complex (RISC) that binds to a short guide RNA such as microRNA (miRNA) or small interfering RNA (siRNA). RISC uses the mature miRNA or siRNA as a guide for slicer-directed cleavage of homologous mRNAs to repress gene expression. Requires DRB1 for directional loading of the small RNA duplex (guide stand and passenger strand) onto RISC for passenger strand degradation. Unlike animal RISC that associates in high molecular weight complex, Arabidopsis RISC is probably composed only of the AGO1 protein and associated RNA without any other proteins. Associates mainly with miRNAs of 21 nucleotide in length and preferentially recruits small RNAs with a 5' terminal uridine. Associates with 22 nucleotide miRNAs to trigger RDR6-dependent secondary siRNAs biogenesis. This pathway amplifies silencing by using the target RNA as substrate to generate secondary siRNAs. Binds to miR168 which targets its own mRNA for repression, establishing a homeostatic regulatory loop. Involved in antiviral RNA silencing by contributing to viral RNA clearance. Is capable of targeting viral RNAs with more compact structures than AGO7 which favors less structured RNA targets. May not associate with 24 nucleotide siRNAs involved in chromatin silencing. Essential for multiple processes in development. Essential for proper development of leaves and floral organs, and formation of axillary meristems. Like AGO10, required for stem cell function and organ polarity.
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O04385
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IEMT_CLABR
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(Iso)eugenol O-methyltransferase (EC 2.1.1.146) (S-adenosysl-L-methionine:(Iso)eugenol O-methyltransferase) (IEMT)
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MGSTGNAEIQIIPTHSSDEEANLFAMQLASAAVLPMALKAAIELDVLEIMAKSVPPSGYISPAEIAAQLPTTNPEAPVMLDRVLRLLASYSVVTYTLRELPSGKVERLYGLAPVCKFLTKNEDGVSLAPFLLTATDKVLLEPWFYLKDAILEGGIPFNKAYGMNEFDYHGTDHRFNKVFNKGMSSNSTITMKKILEMYNGFEGLTTIVDVGGGTGAVASMIVAKYPSINAINFDLPHVIQDAPAFSGVEHLGGDMFDGVPKGDAIFIKWICHDWSDEHCLKLLKNCYAALPDHGKVIVAEYILPPSPDPSIATKVVIHTDALMLAYNPGGKERTEKEFQALAMASGFRGFKVASCAFNTYVMEFLKTA
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Catalyzes the methylation of the para-4-hydroxyl of both eugenol and (iso)eugenol to methyleugenol and isomethyleugenol, respectively. The resulting products are part of a complex mixture of low-molecular-weight volatile compounds emitted by the flowers to attract pollinators.
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O04468
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STMP6_ARATH
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Secreted transmembrane peptide 6 (Phytocytokine STMP6) (Precursor of secreted transmembrane peptide 6)
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MGMKSPNIAAFMLPLLLILFTLSSQLKVVESTGRKLAWGFSGTPIVYTPPSRSCGTSPAVFTSKWRRPRPCRLPPGSYIPASDQSP
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Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation (By similarity). Prevents general growth and development.
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O04479
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AS2_ARATH
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Protein ASYMMETRIC LEAVES 2 (LOB domain-containing protein 6)
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MASSSTNSPCAACKFLRRKCQPECVFAPYFPPDQPQKFANVHKVFGASNVTKLLNELHPSQREDAVNSLAYEADMRLRDPVYGCVGVISLLQHQLRQLQIDLSCAKSELSKYQSLGILAATHQSLGINLLAGAADGTATAVRDHYHHHQFFPREQMFGGLDVPAGNNYDGGILAIGQITQFQQPRAAAGDDGRRTVDPS
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Negative regulator of cell proliferation in the adaxial side of leaves. Regulates the formation of a symmetric lamina and the establishment of venation. Positively regulates LATERAL ORGAN BOUNDARIES (LOB) within the shoot apex, and the class III HD-ZIP genes REV, PHB, and PHV. Interacts directly with ASYMMETRIC LEAVES 1 (AS1) to repress the knox homeobox genes KNAT1, KNAT2, and KNAT6 and the abaxial determinants ARF3, KAN2 and YAB5. May act in parallel with the RDR6-SGS3-AGO7 pathway, an endogenous RNA silencing pathway, to regulate the leaf morphogenesis. Required for the binding of AS1 to the KNOX genes. Involved in leaf polarity establishment by functioning cooperatively with RH10 or RID2 to repress abaxial genes ARF3, ARF4, KAN1, KAN2, YAB1 and YAB5, and the knox homeobox genes KNAT1, KNAT2, KNAT6, and STM to promote adaxial development in leaf primordia at shoot apical meristems at high temperatures.
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O04482
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UCH2_ARATH
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Ubiquitin carboxyl-terminal hydrolase 2 (EC 3.4.19.12)
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MSWCTIESDPGVFTELIQQMQVKGVQVEELYSLDSDSLNNLRPVYGLIFLFKWQAGEKDERPTIQDQVSNLFFANQVINNACATQAILAILLNSPEVDIGPELSALKEFTKNFPSDLKGLAINNSDSIRAAHNSFARPEPFVPEEQKAATKDDDVYHFISYIPVDGVLYELDGLKEGPISLGPCPGDQTGIEWLQMVQPVIQERIERYSQSEIRFNLLAVIKNRKDIYTAELKELQRQREQLLQQANTCVDKSEAEAVNALIAEVGSGIEAASDKIVMEEEKFMKWRTENIRRKHNYIPFLFNFLKLLAEKKQLKPLIEKAKKQKTESST
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Ubiquitin-protein hydrolase involved in the release of ubiquitin attached via both peptide and isopeptide linkages. Able to cleave 'Lys-48'-linked polyubiquitin chains. Involved in the direct or indirect regulation of AUX/IAA proteins stability. Acts as a linker between the TREX-2 complex and 26S proteasome.
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O04492
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DRB1_ARATH
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Double-stranded RNA-binding protein 1 (Protein HYPONASTIC LEAVES 1) (dsRNA-binding protein 1) (AtDRB1)
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MTSTDVSSGVSNCYVFKSRLQEYAQKYKLPTPVYEIVKEGPSHKSLFQSTVILDGVRYNSLPGFFNRKAAEQSAAEVALRELAKSSELSQCVSQPVHETGLCKNLLQEYAQKMNYAIPLYQCQKVETLGRVTQFTCTVEIGGIKYTGAATRTKKDAEISAGRTALLAIQSDTKNNLANYNTQLTVLPCEKKTIQAAIPLKETVKTLKARKAQFKKKAQKGKRTVAKNPEDIIIPPQPTDHCQNDQSEKIETTPNLEPSSCMNGLKEAAFGSVETEKIETTPNLEPPSCMNGLKEAAFGSVETEKIETTPNLEPPSCMNGLKEAAFGSVETEKIETTPNLEPSSCMNGLKEAAFGSVETEKIETTPNLEPPSCMNGLKEAAFGSVETEKIETTPNLESSSCMSGLKEAAFGSVETEASHA
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Double-stranded RNA-binding protein involved in RNA-mediated post-transcriptional gene silencing (PTGS). Functions in the microRNAs (miRNAs) biogenesis by assisting DICER-LIKE 1 (DCL1) in the accurate processing from primary miRNAs (pri-miRNAs) to miRNAs in the nucleus. Forms a complex with SERRATE (SE) and DCL1 to promote accurate processing of pri-miRNAs by DCL1. Binds and assist DCL1 for accurate processing of precursor miRNAs (pre-miRNA). Indirectly involved in the production of trans-acting small interfering RNAs (ta-siRNAs) derived from the TAS1, TAS2 or TAS3 endogenous transcripts by participating in the production of their initiating miRNAs. Involved with argonaute 1 (AGO1) in the guide strand selection from miRNA duplexes, presumably by directional loading of the miRNA duplex (guide stand and passenger strand) onto the RNA-induced silencing complex (RISC) for passenger strand degradation. Does not participate in sense transgene-induced post-transcriptional gene silencing (S-PTGS). Involved in several plant development aspects and response to hormones through its role in miRNAs processing.
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O04499
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PMG1_ARATH
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2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1 (BPG-independent PGAM 1) (Phosphoglyceromutase 1) (EC 5.4.2.12) (PGAM-I 1)
|
MATSSAWKLDDHPKLPKGKTIAVIVLDGWGESAPDQYNCIHNAPTPAMDSLKHGAPDTWTLIKAHGTAVGLPSEDDMGNSEVGHNALGAGRIFAQGAKLCDQALASGKIFEGEGFKYVSESFETNTLHLVGLLSDGGVHSRLDQLQLLIKGSAERGAKRIRVHILTDGRDVLDGSSVGFVETLEADLVALRENGVDAQIASGGGRMYVTLDRYENDWEVVKRGWDAQVLGEAPHKFKNAVEAVKTLRKEPGANDQYLPPFVIVDESGKAVGPIVDGDAVVTFNFRADRMVMHAKALEYEDFDKFDRVRYPKIRYAGMLQYDGELKLPSRYLVSPPEIDRTSGEYLTHNGVSTFACSETVKFGHVTFFWNGNRSGYFNEKLEEYVEIPSDSGISFNVQPKMKALEIGEKARDAILSGKFDQVRVNIPNGDMVGHTGDIEATVVACEAADLAVKMIFDAIEQVKGIYVVTADHGNAEDMVKRDKSGKPALDKEGKLQILTSHTLKPVPIAIGGPGLAQGVRFRKDLETPGLANVAATVMNLHGFVAPSDYEPTLIEVVE
|
Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA). Required for guard cell function (e.g. blue light-, abscisic acid- (ABA), and low CO(2)-regulated stomatal movements) and fertility (e.g. pollen grains production).
|
O04523
|
TBL27_ARATH
|
Xyloglucan O-acetyltransferase 1 (EC 2.3.1.-) (Protein ALTERED XYLOGLUCAN 4) (Protein TRICHOME BIREFRINGENCE-LIKE 27)
|
MGLNEQQNVPSQRKIIVFIVLAFIPIALFRLCFNNPFSSIKDTSLQDSAANVVITSFSSSSQEEESQESFDHIQDEPLCDYTQGNWVRDEIGPLYNGSTCGTIKDGQNCFRHGRPDSGYLYWKWKPNECDIPRFDSNRFLDLMRDKHLAFIGDSMARNQLESLLCLLSTVSSPDLVYRNGEDNKFRRWRFESHNVTVSVYWSPFLVAGLEKSGNLDHNVLHIDRVDERWGNDLERFDTVVVSVGHWFLHPAVYYESGSVLGCHSCETSNCTEVGFYDVFRKAIRTTLRAVAGSGREVILTTFSPSHFEGRPWDSLGACNMTKPYEGKVLEGLDLDMRKIEIEEYTAAAAEVRLEVLDVTAMSVLRPDGHPGPYMYADPFKNGVPERIPNDCLHWCLPGPVDTWNEIMIEMLRRWKV
|
Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains. Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers. Involved in xyloglucan specific O-acetylation in roots and rosette leaves.
|
O04529
|
2MMP_ARATH
|
Metalloendoproteinase 2-MMP (At2-MMP) (EC 3.4.24.-)
|
MRFCVFGFLSLFLIVSPASAWFFPNSTAVPPSLRNTTRVFWDAFSNFTGCHHGQNVDGLYRIKKYFQRFGYIPETFSGNFTDDFDDILKAAVELYQTNFNLNVTGELDALTIQHIVIPRCGNPDVVNGTSLMHGGRRKTFEVNFSRTHLHAVKRYTLFPGEPRWPRNRRDLTYAFDPKNPLTEEVKSVFSRAFGRWSDVTALNFTLSESFSTSDITIGFYTGDHGDGEPFDGVLGTLAHAFSPPSGKFHLDADENWVVSGDLDSFLSVTAAVDLESVAVHEIGHLLGLGHSSVEESIMYPTITTGKRKVDLTNDDVEGIQYLYGANPNFNGTTSPPSTTKHQRDTGGFSAAWRIDGSSRSTIVSLLLSTVGLVLWFLP
|
Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses (By similarity). Required for plant growth, morphogenesis, and development with particular relevance for flowering and senescence. Active on McaPLGLDpaAR-NH(2) (QF24) and myelin basic protein (MBP) and, to some extent, on beta-casein.
|
O04616
|
CUT1A_ARATH
|
Protein CURVATURE THYLAKOID 1A, chloroplastic
|
MAISVAASSSMAVMVPRVPAVSTRCSAVPYLPPRSFGRSSFTVPLKLVSGNGLQKVELLKTRASSEETSSIDTNELITDLKEKWDGLENKSTVLIYGGGAIVAVWLSSIVVGAINSVPLLPKVMELVGLGYTGWFVYRYLLFKSSRKELAEDIESLKKKIAGSE
|
Determines thylakoid architecture by inducing membrane curvature.
|
O04663
|
IF4E4_ARATH
|
Eukaryotic translation initiation factor isoform 4E (eIF(iso)4E) (Protein LOSS OF SUSCEPTIBILITY TO POTYVIRUS 1) (eIF-(iso)4F 25 kDa subunit) (eIF-(iso)4F p28 subunit) (eIF4Eiso protein) (mRNA cap-binding protein)
|
MATDDVNEPLPAAAELPATEAEKQPHKLERKWSFWFDNQSKKGAAWGASLRKAYTFDTVEDFWGLHETIFQTSKLTANAEIHLFKAGVEPKWEDPECANGGKWTWVVTANRKEALDKGWLETLMALIGEQFDEADEICGVVASVRPQSKQDKLSLWTRTKSNEAVLMGIGKKWKEILDVTDKITFNNHDDSRRSRFTV
|
Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. Mediates susceptibility to Turnipmosaic potyvirus (TuMV) and Tobacco etch potyvirus (TEV).
|
O04705
|
GAO1D_WHEAT
|
Gibberellin 20 oxidase 1-D (EC 1.14.11.-) (GA 20-oxidase 1-D) (Gibberellin C-20 oxidase 1-D) (Protein Wga20) (TaGA20ox1-D) (Ta20ox1D)
|
MVQPVFDAAVLSGRADIPSQFIWPEGESPTPDAAEELHVPLIDIGGMLSGDPAAAAEVTRLVGEACERHGFFQVVNHGIDAELLADAHRCVDNFFTMPLPEKQRALRHPGESCGYASSFTGRFASKLPWKETLSFRSCPSDPALVVDYIVATLGEDHRRLGEVYARYCSEMSRLSLEIMEVLGESLGVGRAHYRRFFEGNDSIMRLNYYPPCQRPLETLGTGPHCDPTSLTILHQDNVGGLQVHTEGRWRSIRPRADAFVVNIGDTFMALSNGRYKSCLHRAVVNSRVPRKSLAFFLCPEMDKVVAPPGTLVDAANPRAYPDFTWRSLLDFTQKHYRADMKTLEVFSSWIVQQQQPQPART
|
Key oxidase enzyme in the biosynthesis of gibberellin that catalyzes the conversion of GA12 and GA53 to GA9 and GA20 respectively, via a three-step oxidation at C-20 of the GA skeleton.
|
O04714
|
GCR1_ARATH
|
G-protein coupled receptor 1
|
MSAVLTAGGGLTAGDRSIITAINTGASSLSFVGSAFIVLCYCLFKELRKFSFKLVFYLALSDMLCSFFLIVGDPSKGFICYAQGYTTHFFCVASFLWTTTIAFTLHRTVVKHKTDVEDLEAMFHLYVWGTSLVVTVIRSFGNNHSHLGPWCWTQTGLKGKAVHFLTFYAPLWGAILYNGFTYFQVIRMLRNARRMAVGMSDRVDQFDNRAELKVLNRWGYYPLILIGSWAFGTINRIHDFIEPGHKIFWLSVLDVGTAALMGLFNSIAYGFNSSVRRAIHERLELFLPERLYRWLPSNFRPKNHLILHQQQQQRSEMVSLKTEDQQ
|
Together with GPA1, may regulate the cell cycle via a signaling cascade that uses phosphatidylinositol-specific phospholipase C (PI-PLC) as an effector and inositol 1,4,5-trisphosphate(IP(3)) as a second messenger. Promotes PI-PLC activity and IP(3) accumulation. Involved in the blue light (BL) signaling. Together with GPA1 and ADT3, required for BL-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated seedlings. Probably involved in cytokinin signal transduction. Plays a positive role in gibberellin- (GA) and brassinosteroid- (BR) regulated seed germination, probably independently of a heterotrimeric G-protein. Mediates seed dormancy abolition, and promotes seed germination and flowering.
|
O04719
|
P2C77_ARATH
|
Protein phosphatase 2C 77 (AtPP2C77) (EC 3.1.3.16) (Protein ABSCISIC ACID-INSENSITIVE 2) (Protein phosphatase 2C ABI2) (PP2C ABI2)
|
MDEVSPAVAVPFRPFTDPHAGLRGYCNGESRVTLPESSCSGDGAMKDSSFEINTRQDSLTSSSSAMAGVDISAGDEINGSDEFDPRSMNQSEKKVLSRTESRSLFEFKCVPLYGVTSICGRRPEMEDSVSTIPRFLQVSSSSLLDGRVTNGFNPHLSAHFFGVYDGHGGSQVANYCRERMHLALTEEIVKEKPEFCDGDTWQEKWKKALFNSFMRVDSEIETVAHAPETVGSTSVVAVVFPTHIFVANCGDSRAVLCRGKTPLALSVDHKPDRDDEAARIEAAGGKVIRWNGARVFGVLAMSRSIGDRYLKPSVIPDPEVTSVRRVKEDDCLILASDGLWDVMTNEEVCDLARKRILLWHKKNAMAGEALLPAEKRGEGKDPAAMSAAEYLSKMALQKGSKDNISVVVVDLKGIRKFKSKSLN
|
Repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), high light stress, response to glucose, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as H(2)O(2) and oxidative burst in response to ABA and dehydration. Represses GHR1 and, to some extent, SRK2E/OST1, kinases involved in the regulation of SLAC1-dependent stomatal closure. Controls negatively fibrillin that is involved in mediating ABA-induced photoprotection. May be implicated in ABA content regulation. Involved in acquired thermotolerance of root growth and seedling survival. Required for the Erwinia amylovora harpin-induced (HrpN) drought tolerance. Involved in the hydrotropic response.
|
O04795
|
PERA_IPOBA
|
Anionic peroxidase (EC 1.11.1.7) (SwPA1)
|
MASFMKQLSLVLSFIALALAGCAVYQNTQTAMKDQLKVTPTWLDNTLKSTNLLSLGLGKPSGGKLGDEACVFSAVKEVVVAAINAEARMGASLIRLFFHDCFVDGCDAGLLLNDTATFTGEQTAAGNNNSVRGFAVIEQAKQNVKTQMPDMSVSCADILSIAARDSFEKFSGSTYTVTLGRKDARTANFTGANTQLVGPNENLTSQLTKFAAKGFNGTEMVALLGSHTIGFARCPLLCISTFINPARVSTLNCNCSGTVNATGLVGLDPTPTTWDQRYFSDVVNDQGLLFSDNELLKGNTTNAAVRRYRDAMGAFLTDFAAAMVKMSNLPPSPGVALEIRDVCSRVNANSVDPCEESRLLASPD
|
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. May contribute to protection against cold-induced oxidative stress.
|
O04796
|
PERN_IPOBA
|
Neutral peroxidase (EC 1.11.1.7) (SwPN1)
|
MASFVARLTLALSFIALALAGYSLVQNTLSSPTHTRLNLIPTWLDSTFDSADVLSYLGFGKSSGRLSDSNCVFSAVKEIVDAAITAETRMGASLIRLHFHDCFVDGCDGGILLNDTANFTGEQGAPANSNSVRGFSVIDQAKRNAQTKCADTPVSCADVLAIAARDAFRKFTNQTYNITLGRQDARTANLTGANTQLPAPFDNLSIQTAKFADKGFNQREMVVLAGAHTVGFSRCAVLCTSTNLNQNRSATLQCTCPASANDTGLVGLDPSPGTFDKKYFEELVKGQGLLFSDQELMQSNATVTAVRRYRDATGAFLTDFAAAMVKMSNLPPSAGVQLEIRNVCSRVN
|
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. May contribute to protection against cold-induced oxidative stress.
|
O04846
|
ATCA1_ARATH
|
Alpha carbonic anhydrase 1, chloroplastic (AtaCA1) (AtalphaCA1) (EC 4.2.1.1) (Alpha carbonate dehydratase 1)
|
MKIMMMIKLCFFSMSLICIAPADAQTEGVVFGYKGKNGPNQWGHLNPHFTTCAVGKLQSPIDIQRRQIFYNHKLNSIHREYYFTNATLVNHVCNVAMFFGEGAGDVIIENKNYTLLQMHWHTPSEHHLHGVQYAAELHMVHQAKDGSFAVVASLFKIGTEEPFLSQMKEKLVKLKEERLKGNHTAQVEVGRIDTRHIERKTRKYYRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLDTSFKNNSRPCQPLNGRRVEMFHDHERVDKKETGNKKKKPN
|
Reversible hydration of carbon dioxide.
|
O04862
|
FOLM_PEA
|
Folate synthesis bifunctional protein, mitochondrial [Includes: 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) (EC 2.7.6.3) (2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase) (7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase) (PPPK); Dihydropteroate synthase (DHPS) (EC 2.5.1.15)]
|
MSILKCLGVRGNQLCAARNYLKVLGFSSFHTAPNSSIEIQTQDEEVVIALGSNVGDRLHNFKEALKLMRKSGIHITRHASLYETAPAYVTDQPRFLNSAVRADTKLGPHELLAALKRIEKDMGRTDGIRYGPRPIDLDILFYGKFKVRSDILTVPHERIWERPFVMAPLMDLLGTAIDSDTVASWHSFSGHSGGLNALWEKLGGESLIGEEGMYRVMPVANGLLDWSRRTLVMGILNLTPDSFSDGGNFQSVKSAVSQARLMISEGADIIDIGAQSTRPMASRISAEEELGRLIPVLEAVMSIPEVEGKLISVDTFYSEVALEAVRKGAHIINDVSAGKLDASMFKVMAELDVPYVAMHMRGDPSTMQDSENLKYDNVCKDISSELYSRVREAEISGIPAWRIIMDPGIGFSKKTEDNLAALTGIPDIREEISKRSLAISHAPILIGPSRKRFLGEICSRPSAVDRDPATIASVTAGVLCGANIVRVHNVKDNLDAVKLCDAILKQKSSPIKFKQ
|
Catalyzes the first two consecutive steps of tetrahydrofolate biosynthesis.
|
O04905
|
KCY3_ARATH
|
UMP-CMP kinase 3 (EC 2.7.4.14) (Deoxycytidylate kinase) (CK) (dCMP kinase) (Uridine monophosphate/cytidine monophosphate kinase) (UMP/CMP kinase) (UMP/CMPK)
|
MGSVDAANGSGKKPTVIFVLGGPGSGKGTQCAYIVEHYGYTHLSAGDLLRAEIKSGSENGTMIQNMIKEGKIVPSEVTIKLLQKAIQENGNDKFLIDGFPRNEENRAAFEKVTEIEPKFVLFFDCPEEEMEKRLLGRNQGREDDNIETIRKRFKVFLESSLPVIHYYEAKGKVRKINAAKPIEAVFEEVKAIFSPEAEKVEA
|
Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Does not act on dCMP and dUMP.
|
O04921
|
HEMH2_ARATH
|
Ferrochelatase-2, chloroplastic (AtFC2) (EC 4.98.1.1) (Ferrochelatase-II) (AtFC-II) (Heme synthase 2) (Protoheme ferro-lyase 2)
|
MNCPAMTASPSSSSSSSYSTFRPPPPLLPQLSNDSQRSVVMHCTRLPFEAFAATSSNRLLGKHSLPLRAALVTSNPLNISSSSVISDAISSSSVITDDAKIGVLLLNLGGPETLDDVQPFLFNLFADPDIIRLPPVFQFLQKPLAQFISVARAPKSKEGYASIGGGSPLRHITDAQAEELRKCLWEKNVPAKVYVGMRYWHPFTEEAIEQIKRDGITKLVVLPLYPQFSISTSGSSLRLLERIFREDEYLVNMQHTVIPSWYQREGYIKAMANLIQSELGKFGSPNQVVIFFSAHGVPLAYVEEAGDPYKAEMEECVDLIMEELDKRKITNAYTLAYQSRVGPVEWLKPYTEEAITELGKKGVENLLAVPISFVSEHIETLEEIDVEYKELALKSGIKNWGRVPALGTEPMFISDLADAVVESLPYVGAMAVSNLEARQSLVPLGSVEELLATYDSQRRELPAPVTMWEWGWTKSAETWNGRAAMLAVLALLVLEVTTGKGFLHQWGILPSL
|
Catalyzes the last step of heme biosynthesis by inserting ferrous iron into protoporphyrin IX to produce protoheme. Produces heme for photosynthetic cytochromes, and for proteins involved in abiotic and biotic stress responses. May play a role in the quality control of individual chloroplasts during photo-oxidative stress through regulation of heme biosynthesis.
|
O04951
|
PP2A5_ARATH
|
Serine/threonine-protein phosphatase PP2A-5 catalytic subunit (EC 3.1.3.16) (Protein phosphatase 2A isoform 5)
|
MPPATGDIDRQIEQLMECKALSETEVKMLCEHAKTILVEEYNVQPVKCPVTVCGDIHGQFYDLIELFRIGGSSPDTNYLFMGDYVDRGYYSVETVSLLVALKVRYRDRLTILRGNHESRQITQVYGFYDECLRKYGNANVWKHFTDLFDYLPLTALIESQVFCLHGGLSPSLDTLDNIRSLDRIQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDIATQFNHTNGLSLISRAHQLVMEGFNWCQEKNVVTVFSAPNYCYRCGNMAAILEIGENMDQNFLQFDPAPRQVEPETTRKTPDYFL
|
Associates with the serine/threonine-protein phosphatase PP2A regulatory subunits A and B' to positively regulates beta-oxidation of fatty acids and protoauxins in peroxisomes by dephosphorylating peroxisomal beta-oxidation-related proteins. Involved in the positive regulation of salt stress responses. May function by increasing chloride channel activities on vacuolar membranes.
|
O04983
|
ACCC_ARATH
|
Biotin carboxylase, chloroplastic (EC 6.3.4.14) (Acetyl-coenzyme A carboxylase biotin carboxylase subunit A)
|
MDASMITNSKSITSPPSLALGKSGGGGVIRSSLCNLMMPSKVNFPRQRTQTLKVSQKKLKRATSGGLGVTCSGGDKILVANRGEIAVRVIRTAHEMGIPCVAVYSTIDKDALHVKLADEAVCIGEAPSNQSYLVIPNVLSAAISRGCTMLHPGYGFLSENALFVEMCRDHGINFIGPNPDSIRVMGDKATARETMKNAGVPTVPGSDGLLQSTEEAVRVANEIGFPVMIKATAGGGGRGMRLAKEPGEFVKLLQQAKSEAAAAFGNDGCYLEKFVQNPRHIEFQVLADKFGNVVHFGERDCSIQRRNQKLLEEAPSPALTAELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGSFYFMEMNTRIQVEHPVTEMIYSVDLIEEQIRVAMGEKLRYKQEDIVLRGHSIECRINAEDPFKGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIERMKRALNDTIITGVPTTINYHKLILDVEDFKNGKVDTAFIVKHEEELAEPQEIVAVKDLTNATV
|
This protein is a component of the acetyl coenzyme A carboxylase complex first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
|
O05131
|
PBPA_NEIGO
|
Penicillin-binding protein 1A (PBP-1a) (PBP1a) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)]
|
MIKKILTTCFGLFFGFCVFGVGLVAIAILVTYPKLPSLDSLQHYQPKMPLTIYSADGEVIGMYGEQRREFTKIGDFPEVLRNAVIAAEDKRFYRHWGVDVWGVARAAVGNVVSGSVQSGASTITQQVAKNFYLSSEKTFTRKFNEVLLAYKIEQSLSKDKILELYFNQIYLGQRAYGFASAAQIYFNKNVRDLTLAEAAMLAGLPKAPSAYNPIVNPERAKLRQKYILNNMLEEKMITVQQRDQALNEELHYERFVRKIDQSALYVAEMVRRELYEKYGEDAYTQGFKVYTTVRTDHQKAATEALRKALRNFDRGSSYRGAENYIDLSKSEDVEETVSQYLSGLYTVDKMVPAVVLDVTKKKNVVIQLPGGRRVALDRRALGFAARAVDNEKMGEDRIRRGAVIRVKNNGGRWAVVQEPLLQGALVSLDAKTGAVRALVGGYDFHSKTFNRAVQAMRQPGSTFKPFVYSAALSKGMTASTVVNDAPISLPGKGPNGSVWTPKNSDGRYSGYITLRQALTASKNMVSIRILMSIGVGYAQQYIRRFGFRPSELPASLSMALGTGETTPLKVAEAYSVFANGGYRVSSHVIDKIYDRDGRLRAQMQPLVAGQNAPQAIDPRNAYIMYKIMQDVVRVGTARGAAALGRTDIAGKTGTTNDNKDAWFVGFNPDVVTAVYIGFDKPKSMGRAGYGGTIAVPVWVDYMRFALKGKQGKGMKMPEGVVSSNGEYYMKERMVTDPGLMLDNSGIAPQPSRRAKEDDEAAVENEQQGRSDETRQDVQETPVLPSNTDSKQQQLDSLF
|
Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). Essential for cell wall synthesis.
|
O05207
|
TOP6B_SACSH
|
Type 2 DNA topoisomerase 6 subunit B (EC 5.6.2.2) (Type II DNA topoisomerase VI subunit B) (TopoVI-B)
|
MSAKEKFTSLSPAEFFKRNPELAGFPNPARALYQTVRELIENSLDATDVHGILPNIKITIDLIDDARQIYKVNVVDNGIGIPPQEVPNAFGRVLYSSKYVNRQTRGMYGLGVKAAVLYSQMHQDKPIEIETSPVNSKRIYTFKLKIDINKNEPIIVERGSVENTRGFHGTSVAISIPGDWPKAKSRIYEYIKRTYIITPYAEFIFKDPEGNVTYYPRLTNKIPKPPQEVKPHPYGVDREEIKILINNLKRDYTIKEFLVNEFQSIGDTTADKILELAGLKPNKKVKNLTEEEITRLVETFKKDEDFRSPSADSLSVIGEDLIELGLKKIFNPDFAASITRKPKAYQGHPFIVEAGVAFGGSIPVGEEPIVLRYANKIPLIYDEKSDVIWKVVEELDWKRYGIESDQYQMVVMVHLCSTKIPYKSAGKESIAEVENIEKEIKNALMEVARKLKQYLSEKRKEQEAKKKLLAYLKYIPEVSRSLATFLASGNKELVSKYQNEISEGLFKLISKKLDLINIEEYRKVYRVDSE
|
Relaxes both positive and negative supercoils and exhibits a strong decatenase and unknotting activity it cannot introduce DNA supercoils. ATP is absolutely required for DNA cleavage the nonhydrolyzable analog AMP-PNP generates nicked or linear products from a supercoiled dsDNA substrate. Generates staggered two-nucleotide long 5' overhangs. The enzyme is covalently attached transiently to the 5'-ends of the cleaved strands.
|
O05208
|
TOP6A_SACSH
|
Type 2 DNA topoisomerase 6 subunit A (EC 5.6.2.2) (Type II DNA topoisomerase VI subunit A)
|
MSSEFISKVDKEARRKAANILRDKFLNLVEQLKKGEPLVMEIPMRTLSNAIYDEKRKLLLLGEKKLRRNFLDLNEAKRFMQTVLMASIIYDALVSDEYPTIRDLYYRGKHSLLLKSIEGNKIVSEENTWDEQKESDSVIVDIEVFTSLLREEMLILSKEKGKVVGNLRIRSGNDVIDLSKTGHGAYAIEPTPDLIDFIDVDAEFVLVVEKDAVFQQLHRAGFWKQYKSILITSAGQPDRATRRFVRRLNEELKLPVYILTDADPYGWYIFSVFRIGSISLSYESERLATPDAKFLGVSMGDIFGNSRKKPYLSEAERKNYIIKAKDADIKRAEEIKNYEWFKTKAWQEEINTFLQRKAKLEIEAMASKGLKFLAFQYIPEKITNKDYIA
|
Relaxes both positive and negative supercoils and exhibits a strong decatenase and unknotting activity it cannot introduce DNA supercoils. ATP is absolutely required for DNA cleavage the nonhydrolyzable analog AMP-PNP generates nicked or linear products from a supercoiled dsDNA substrate. Generates staggered two-nucleotide long 5' overhangs. The enzyme is covalently attached transiently to the 5'-ends of the cleaved strands.
|
O05306
|
LOGH_MYCTU
|
Cytokinin riboside 5'-monophosphate phosphoribohydrolase (EC 3.2.2.n1) (Protein LONELY GUY homolog) (LOG homolog)
|
MSAKIDITGDWTVAVYCAASPTHAELLELAAEVGAAIAGRGWTLVWGGGHVSAMGAVASAARACGGWTVGVIPKMLVYRELADHDADELIVTDTMWERKQIMEDRSDAFIVLPGGVGTLDELFDAWTDGYLGTHDKPIVMVDPWGHFDGLRAWLNGLLDTGYVSPTAMERLVVVDNVKDALRACAPS
|
Catalyzes the hydrolytic removal of ribose 5'-monophosphate from nitrogen N6-modified adenosines, the final step of bioactive cytokinin synthesis. Is involved in the synthesis of isopentenyladenine (iP) and 2-methylthio-iP (2MeS-iP), the most abundant cytokinins detected in M.tuberculosis lysates and supernatants. Is also able to convert trans-zeatin-riboside monophosphate (tZRMP) to trans-zeatin (tZ) in vitro however, it may not be involved in the biosynthesis of this minor cytokinin in vivo. Accumulation of Rv1205 sensitizes M.tuberculosis to nitric oxide since cytokinin breakdown products synergize with NO to kill M.tuberculosis. Shows a slow AMP hydrolase activity, but is not able to hydrolyze ATP. Displays no lysine decarboxylase (LDC) activity (L-lysine conversion to cadaverine).
|
O05307
|
FAC6_MYCTU
|
Medium/long-chain-fatty-acid--CoA ligase FadD6 (EC 6.2.1.2) (EC 6.2.1.3) (FACL6)
|
MSDYYGGAHTTVRLIDLATRMPRVLADTPVIVRGAMTGLLARPNSKASIGTVFQDRAARYGDRVFLKFGDQQLTYRDANATANRYAAVLAARGVGPGDVVGIMLRNSPSTVLAMLATVKCGAIAGMLNYHQRGEVLAHSLGLLDAKVLIAESDLVSAVAECGASRGRVAGDVLTVEDVERFATTAPATNPASASAVQAKDTAFYIFTSGTTGFPKASVMTHHRWLRALAVFGGMGLRLKGSDTLYSCLPLYHNNALTVAVSSVINSGATLALGKSFSASRFWDEVIANRATAFVYIGEICRYLLNQPAKPTDRAHQVRVICGNGLRPEIWDEFTTRFGVARVCEFYAASEGNSAFINIFNVPRTAGVSPMPLAFVEYDLDTGDPLRDASGRVRRVPDGEPGLLLSRVNRLQPFDGYTDPVASEKKLVRNAFRDGDCWFNTGDVMSPQGMGHAAFVDRLGDTFRWKGENVATTQVEAALASDQTVEECTVYGVQIPRTGGRAGMAAITLRAGAEFDGQALARTVYGHLPGYALPLFVRVVGSLAHTTTFKSRKVELRNQAYGADIEDPLYVLAGPDEGYVPYYAEYPEEVSLGRRPQG
|
Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA). May play a role in the uptake of fatty acids by trapping them metabolically as CoA esters. May also play an important role in the channeling of fatty acids into triacylglycerol (TAG) for use by Mycobacterium during its dormancy.
|
O05394
|
MCCB_BACSU
|
Cystathionine gamma-lyase (EC 4.4.1.1) (Gamma-cystathionase) (Homocysteine gamma-lyase) (EC 4.4.1.2)
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MKKKTLMIHGGITGDEKTGAVSVPIYQVSTYKQPKAGQHTGYEYSRTANPTRTALEALVTELESGEAGYAFSSGMAAITAVMMLFNSGDHVVLTDDVYGGTYRVMTKVLNRLGIESTFVDTSSREEVEKAIRPNTKAIYIETPTNPLLKITDLTLMADIAKKAGVLLIVDNTFNTPYFQQPLTLGADIVLHSATKYLGGHSDVVGGLVVTASKELGEELHFVQNSTGGVLGPQDSWLLMRGIKTLGLRMEAIDQNARKIASFLENHPAVQTLYYPGSSNHPGHELAKTQGAGFGGMISFDIGSEERVDAFLGNLKLFTIAESLGAVESLISVPARMTHASIPRERRLELGITDGLIRISVGIEDAEDLLEDIGQALENI
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Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide.
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O05442
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CPNT_MYCTU
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Outer membrane channel protein CpnT (Channel protein with necrosis-inducing toxin) [Cleaved into: N-terminal channel domain; Tuberculosis necrotizing toxin (TNT) (NAD(+) glycohydrolase) (EC 3.2.2.5)]
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MAPLAVDPAALDSAGGAVVAAGAGLGAVISSLTAALAGCAGMAGDDPAGAVFGRSYDGSAAALVQAMSVARNGLCNLGDGVRMSAHNYSLAEAMSDVAGRAAPLPAPPPSGCVGVGAPPSAVGGGGGAPKGWGWVAPYIGMIWPNGDSTKLRAAAVAWRSAGTQFALTEIQSTAGPMGVIRAQQLPEAGLIESAFADAYASTTAVVGQCHQLAAQLDAYAARIDAVHAAVLDLLARICDPLTGIKEVWEFLTDQDEDEIQRIAHDIAVVVDQFSGEVDALAAEITAVVSHAEAVITAMADHAGKQWDRFLHSNPVGVVIDGTGQQLKGFGEEAFGMAKDSWDLGPLRASIDPFGWYRSWEEMLTGMAPLAGLGGENAPGVVESWKQFGKSLIHWDEWTTNPNEALGKTVFDAATLALPGGPLSKLGSKGRDILAGVRGLKERLEPTTPHLEPPATPPRPGPQPPRIEPPESGHPAPAPAAKPAPVPANGPLPHSPTESKPPPVDRPAEPVAPSSASAGQPRVSAATTPGTHVPHGLPQPGEHVPAQAPPATTLLGGPPVESAPATAHQPQWATTPAAPAAAPHSTPGGVHSTESGPHGRSLSAHGSEPTHDGASHGSGHGSGSEPPGLHAPHREQQLAMHSNEPAGEGWHRLSDEAVDPQYGEPLSRHWDFTDNPADRSRINPVVAQLMEDPNAPFGRDPQGQPYTQERYQERFNSVGPWGQQYSNFPPNNGAVPGTRIAYTNLEKFLSDYGPQLDRIGGDQGKYLAIMEHGRPASWEQRALHVTSLRDPYHAYTIDWLPEGWFIEVSEVAPGCGQPGGSIQVRIFDHQNEMRKVEELIRRGVLRQ
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Has a dual function in uptake of nutrients and induction of host cell death. The N-terminal domain (NTD) forms an outer membrane channel and is used for uptake of nutrients across the outer membrane. The secreted C-terminal toxic domain (TNT) acts as a glycohydrolase, which hydrolyzes the essential cellular coenzyme NAD(+) in the cytosol of infected macrophages, leading to necrotic host cell death. Both functions are required for survival, replication and cytotoxicity of M.tuberculosis in macrophages.
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O05461
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MYCP1_MYCTU
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Mycosin-1 (EC 3.4.21.-) (MycP1 protease)
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MHRIFLITVALALLTASPASAITPPPIDPGALPPDVTGPDQPTEQRVLCASPTTLPGSGFHDPPWSNTYLGVADAHKFATGAGVTVAVIDTGVDASPRVPAEPGGDFVDQAGNGLSDCDAHGTLTASIIAGRPAPTDGFVGVAPDARLLSLRQTSEAFEPVGSQANPNDPNATPAAGSIRSLARAVVHAANLGVGVINISEAACYKVSRPIDETSLGASIDYAVNVKGVVVVVAAGNTGGDCVQNPAPDPSTPGDPRGWNNVQTVVTPAWYAPLVLSVGGIGQTGMPSSFSMHGPWVDVAAPAENIVALGDTGEPVNALQGREGPVPIAGTSFAAAYVSGLAALLRQRFPDLTPAQIIHRITATARHPGGGVDDLVGAGVIDAVAALTWDIPPGPASAPYNVRRLPPPVVEPGPDRRPITAVALVAVGLTLALGLGALARRALSRR
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May play a dual role in regulation of ESX-1 secretion and virulence. Acts as a protease that cleaves EspB. Essential for ESX-1 function, required for early replication in macrophages and full virulence in mice.
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O05512
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MANB_BACSU
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Mannan endo-1,4-beta-mannosidase (EC 3.2.1.78) (1,4-beta-D-mannan mannanohydrolase) (Beta-mannanase) (Glucomannan utilization protein G)
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MFKKHTISLLIIFLLASAVLAKPIEAHTVSPVNPNAQQTTKTVMNWLAHLPNRTENRVLSGAFGGYSHDTFSMAEADRIRSATGQSPAIYGCDYARGWLETANIEDSIDVSCNGDLMSYWKNGGIPQISLHLANPAFQSGHFKTPITNDQYKKILDSSTVEGKRLNAMLSKIADGLQELENQGVPVLFRPLHEMNGEWFWWGLTSYNQKDNERISLYKQLYKKIYHYMTDTRGLDHLIWVYSPDANRDFKTDFYPGASYVDIVGLDAYFQDAYSINGYDQLTALNKPFAFTEVGPQTANGSFDYSLFINAIKQKYPKTIYFLAWNDEWSAAVNKGASALYHDSWTLNKGEIWNGDSLTPIVE
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Involved in the degradation of glucomannan. Catalyzes the endo hydrolysis of beta-1,4-linked mannan, galactomannan and glucomannan.
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O05542
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ADHA_GLUOX
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Alcohol dehydrogenase (quinone), dehydrogenase subunit (ADH) (EC 1.1.5.5) (Alcohol dehydrogenase (quinone), acceptor subunit) (Alcohol dehydrogenase (quinone), subunit I) (Ethanol:Q2 reductase) (G3-ADH subunit I) (Quinohemoprotein alcohol dehydrogenase) (Quinohemoprotein-cytochrome c complex) (Ubiquinol oxidase)
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MTSGLLTPIKVTKKRLLSCAAALAFSAAVPVAFAQEDTGTAITSSDNGGHPGDWLSYGRSYSEQRYSPLDQINTENVGKLKLAWHYDLDTNRGQEGTPLIVNGVMYATTNWSKMKALDAATGKLLWSYDPKVPGNIADRGCCDTVSRGAAYWNGKVYFGTFDGRLIALDAKTGKLVWSVYTIPKEAQLGHQRSYTVDGAPRIAKGKVLIGNGGAEFGARGFVSAFDAETGKLDWRFFTVPNPENKPDGAASDDILMSKAYPTWGKNGAWKQQGGGGTVWDSLVYDPVTDLVYLGVGNGSPWNYKFRSEGKGDNLFLGSIVAINPDTGKYVWHFQETPMDEWDYTSVQQIMTLDMPVNGEMRHVIVHAPKNGFFYIIDAKTGKFITGKPYTYENWANGLDPVTGRPNYVPDALWTLTGKPWLGIPGELGGHNFAAMAYSPKTKLVYIPAQQIPLLYDGQKGGFKAYHDAWNLGLDMNKIGLFDDNDPEHVAAKKDFLKVLKGWTVAWDPEKMAPAFTINHKGPWNGGLLATAGNVIFQGLANGEFHAYDATNGNDLYSFPAQSAIIAPPVTYTANGKQYVAVEVGWGGIYPFLYGGVARTSGWTVNHSRVIAFSLDGKDSLPPKNELGFTPVKPVPTYDEARQKDGYFMYQTFCSACHGDNAISGGVLPDLRWSGAPRGRESFYKLVGRGALTAYGMDRFDTSMTPEQIEDIRNFIVKRANESYDDEVKARENSTGVPNDQFLNVPQSTADVPTADHP
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Dehydrogenase component of the alcohol dehydrogenase multicomponent enzyme system which is involved in the production of acetic acid and in the ethanol oxidase respiratory chain. Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the oxidation of ethanol to acetaldehyde by transferring electrons to the ubiquinone embedded in the membrane phospholipids. The electrons transfer from ethanol to membranous ubiquinone occurs from pyrroloquinoline quinone (PQQ) to one heme c in subunit I (AdhA), and finally to two heme c in subunit II (AdhB). Besides ubiquinone reduction, ADH also has a ubiquinol (QH2) oxidation reaction which mediates electron transfer from ubiquinol to the non-energy generating bypass oxidase system. The electrons transfer occurs from ubiquinol (QH2) to the additional heme c within subunit II (AdhB). Also able to use quinone analogs such as 2,3-dimethoxy-5-methyl-6-n-decyl-1,4-benzoquinone (DB) and 2,3-dimethoxy-5-methyl-6-n-pentyl-1,4-benzoquinone (PB).
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O05581
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PAT_MYCTU
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Acetyltransferase Pat (EC 2.3.1.-) (GCN5-like enzyme) (GCN5-related N-acetyltransferase) (GNAT) (Protein acetyltransferase) (Pat)
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MDGIAELTGARVEDLAGMDVFQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDGVAIIARALPGMIVGEIALLRDSPRSATVTTIEPLTGWTGGRGAFATMVHIPGVGERLLRTARQRLAAFVSPIPVRLADGTQLMLRPVLPGDRERTVHGHIQFSGETLYRRFMSARVPSPALMHYLSEVDYVDHFVWVVTDGSDPVADARFVRDETDPTVAEIAFTVADAYQGRGIGSFLIGALSVAARVDGVERFAARMLSDNVPMRTIMDRYGAVWQREDVGVITTMIDVPGPGELSLGREMVDQINRVARQVIEAVG
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Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS). This acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes.
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O05877
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PK21_MYCTU
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GDP-polyphosphate phosphotransferase (EC 2.7.4.-) (Polyphosphate kinase PPK2)
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MDIPSVDVSTATNDGASSRAKGHRSAAPGRRKISDAVYQAELFRLQTEFVKLQEWARHSGARLVVIFEGRDGAGKGGAIKRITEYLNPRVARIAALPAPTDRERGQWYYQRYIAHLPAKGEIVLFDRSWYNRAGVEKVMGFCTPQEYVLFLRQTPIFEQMLIDDGILLRKYWFSVSDAEQLRRFKARRNDPVRQWKLSPMDLESVYRWEDYSRAKDEMMVHTDTPVSPWYVVESDIKKHARLNMMAHLLSTIDYADVEKPKVKLPPRPLVSGNYRRPPRELSTYVDDYVATLIAR
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Uses inorganic polyphosphate (polyP) as a donor to convert GDP to GTP. In addition, modulates nucleotide triphosphate synthesis catalyzed by the nucleoside diphosphate kinase (Ndk) in favor of GTP production over CTP or UTP. Plays an important role in survival of M.tuberculosis in macrophages.
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O05927
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CYSH_PSEAE
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Adenosine 5'-phosphosulfate reductase (APS reductase) (EC 1.8.4.10) (5'-adenylylsulfate reductase) (Thioredoxin-dependent 5'-adenylylsulfate reductase)
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MLPFATIPATERNSAAQHQDPSPMSQPFDLPALASSLADKSPQDILKAAFEHFGDELWISFSGAEDVVLVDMAWKLNRNVKVFSLDTGRLHPETYRFIDQVREHYGIAIDVLSPDPRLLEPLVKEKGLFSFYRDGHGECCGIRKIEPLKRKLAGVRAWATGQRRDQSPGTRSQVAVLEIDGAFSTPEKPLYKFNPLSSMTSEEVWGYIRMLELPYNSLHERGYISIGCEPCTRPVLPNQHEREGRWWWEEATHKECGLHAGNLISKA
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Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor. {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000269|PubMed:10613872, ECO:0000269|PubMed:11940598, ECO:0000269|PubMed:16289027}.
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O06218
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AHPR_MYCTU
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Alkyl hydroperoxide reductase Rv2159c (EC 1.11.1.-) (Alkylhydroperoxidase Rv2159c)
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MKFVNHIEPVAPRRAGGAVAEVYAEARREFGRLPEPLAMLSPDEGLLTAGWATLRETLLVGQVPRGRKEAVAAAVAASLRCPWCVDAHTTMLYAAGQTDTAAAILAGTAPAAGDPNAPYVAWAAGTGTPAGPPAPFGPDVAAEYLGTAVQFHFIARLVLVLLDETFLPGGPRAQQLMRRAGGLVFARKVRAEHRPGRSTRRLEPRTLPDDLAWATPSEPIATAFAALSHHLDTAPHLPPPTRQVVRRVVGSWHGEPMPMSSRWTNEHTAELPADLHAPTRLALLTGLAPHQVTDDDVAAARSLLDTDAALVGALAWAAFTAARRIGTWIGAAAEGQVSRQNPTG
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Involved in protection against oxidative stresses. May play a significant role in maintaining the cellular homeostasis during stress and virulence of M.tuberculosis. In vitro, catalyzes the decomposition of cumene hydroperoxide (CHP) to acetophenone.
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O06319
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CULP4_MYCTU
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Phospholipase Culp4 (EC 3.1.1.-) (Cutinase-like protein 4) (Culp4)
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MIPRPQPHSGRWRAGAARRLTSLVAAAFAAATLLLTPALAPPASAGCPDAEVVFARGTGEPPGLGRVGQAFVSSLRQQTNKSIGTYGVNYPANGDFLAAADGANDASDHIQQMASACRATRLVLGGYSQGAAVIDIVTAAPLPGLGFTQPLPPAADDHIAAIALFGNPSGRAGGLMSALTPQFGSKTINLCNNGDPICSDGNRWRAHLGYVPGMTNQAARFVASRI
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A2-type phospholipase, which is probably involved in the degradation of macrophage membrane. Hydrolyzes dipalmitoylphosphatidylcholine. Also shows moderate esterase activity and hydrolyzes the p-nitrophenol-linked aliphatic ester pNP-butyrate (C4). Does not exhibit cutinase activity.
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O06350
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LIPF_MYCTU
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Carboxylesterase/phospholipase LipF (EC 3.1.1.1) (EC 3.1.4.3)
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MSSYYARRPLQSSGCSNSDSCWDGAPIEITESGPSVAGRLAALASRMTIKPLMTVGSYLSPLPLPLGFVDFACRVWRPGQGTVRTTINLPNATAQLVRAPGVRAADGAGRVVLYLHGGAFVMCGPNSHSRIVNALSGFAESPVLIVDYRLIPKHSLGMALDDCHDAYQWLRARGYRPEQIVLAGDSAGGYLALALAQRLQCDDEKPAAIVAISPLLQLAKGPKQDHPNIGTDAMFPARAFDALAAWVRAAAAKNMVDGRPEDLYEPLDHIESSLPPTLIHVSGSEVLLHDAQLGAGKLAAAGVCAEVRVWPGQAHLFQLATPLVPEATRSLRQIGQFIRDATADSSLSPVHRSRYVAGSPRAASRGAFGQSPI
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Hydrolyzes short-chain esters. Shows maximal activity with triacetin and p-nitrophenyl acetate. Has no enzyme activity on triacylglycerides or p-nitrophenyl esters (p-NP) with long fatty acids (tricaprin, p-NP caprylate, or p-NP caprate) experiments performed with enzyme missing the first 97 residues. Has phospholipase C activity, making 1,2-DAG phosphocholine experiments performed with enzyme missing the first 97 residues.
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O06428
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NPPPS_MYCTU
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Nonaprenyl diphosphate synthase (EC 2.5.1.85) ((2E,6E)-farnesyl diphosphate synthase) (E,E-FPP synthase) (FPP synthase) (EC 2.5.1.10) (Geranylgeranyl diphosphate synthase) (GGPP synthase) (GGPS) (EC 2.5.1.29)
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MRTPATVVAGVDLGDAVFAAAVRAGVARVEQLMDTELRQADEVMSDSLLHLFNAGGKRFRPLFTVLSAQIGPQPDAAAVTVAGAVIEMIHLATLYHDDVMDEAQVRRGAPSANAQWGNNVAILAGDYLLATASRLVARLGPEAVRIIADTFAQLVTGQMRETRGTSENVDSIEQYLKVVQEKTGSLIGAAGRLGGMFSGATDEQVERLSRLGGVVGTAFQIADDIIDIDSESDESGKLPGTDVREGVHTLPMLYALRESGPDCARLRALLNGPVDDDAEVREALTLLRASPGMARAKDVLAQYAAQARHELALLPDVPGRRALAALVDYTVSRHG
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Catalyzes the sequential condensations of isopentenyl pyrophosphate (IPP) with geranyl diphosphate (GPP) to yield (2E,6E)-farnesyl diphosphate (E,E-FPP), with E,E-FPP to yield geranylgeranyl diphosphate (GGPP) and with GGPP to yield nonaprenyl diphosphate. May also have weak activity with dimethylallyl diphosphate (DMAPP).
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O06543
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AMACR_MYCTU
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Alpha-methylacyl-CoA racemase (AMACR) (EC 5.1.99.4) (MtMCR)
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MAGPLSGLRVVELAGIGPGPHAAMILGDLGADVVRIDRPSSVDGISRDAMLRNRRIVTADLKSDQGLELALKLIAKADVLIEGYRPGVTERLGLGPEECAKVNDRLIYARMTGWGQTGPRSQQAGHDINYISLNGILHAIGRGDERPVPPLNLVGDFGGGSMFLLVGILAALWERQSSGKGQVVDAAMVDGSSVLIQMMWAMRATGMWTDTRGANMLDGGAPYYDTYECADGRYVAVGAIEPQFYAAMLAGLGLDAAELPPQNDRARWPELRALLTEAFASHDRDHWGAVFANSDACVTPVLAFGEVHNEPHIIERNTFYEANGGWQPMPAPRFSRTASSQPRPPAATIDIEAVLTDWDG
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Catalyzes the epimerization of (2R)- and (2S)-methylacyl-coenzyme A (CoA) thioesters. Accepts as substrates a wide range of alpha-methylacyl-CoAs, including (2R)-2-methylmyristoyl-CoA and (2S)-2-methylmyristoyl-CoA, (2R)-pristanoyl-CoA and (2S)-pristanoyl-CoA, and the cholesterol esters (25R)-3-oxo-cholest-4-en-26-oyl-CoA and (25S)-3-oxo-cholest-4-en-26-oyl-CoA. Can also catalyze the interconversion of the non-physiologic substrates (2R)-ibuprofenoyl-CoA and (2S)-ibuprofenoyl-CoA, which are potential competitive inhibitors of the enzyme.
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O06582
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PRPD_MYCTU
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2-methylcitrate dehydratase (2-MC dehydratase) (EC 4.2.1.79) (Aconitate hydratase) (ACN) (Aconitase) (EC 4.2.1.3)
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MPDQDTKVRFFRVFCWCPVLRMVRIMLMHAVRAWRSADDFPCTEHMAYKIAQVAADPVDVDPEVADMVCNRIIDNAAVSAASMVRRPVTVARHQALAHPVRHGAKVFGVEGSYSADWAAWANGVAARELDFHDTFLAADYSHPADNIPPLVAVAQQLGVCGAELIRGLVTAYEIHIDLTRGICLHEHKIDHVAHLGPAVAAGIGTMLRLDQETIYHAIGQALHLTTSTRQSRKGAISSWKAFAPAHAGKVGIEAVDRAMRGEGSPAPIWEGEDGVIAWLLAGPEHTYRVPLPAPGEPKRAILDSYTKQHSAEYQSQAPIDLACRLRERIGDLDQIASIVLHTSHHTHVVIGTGSGDPQKFDPDASRETLDHSLPYIFAVALQDGCWHHERSYAPERARRSDTVALWHKISTVEDPEWTRRYHCADPAKKAFGARAEVTLHSGEVIVDELAVADAHPLGTRPFERKQYVEKFTELADGVVEPVEQQRFLAVVESLADLESGAVGGLNVLVDPRVLDKAPVIPPGIFR
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Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield the cis isomer of 2-methyl-aconitate. Could also catalyze the dehydration of citrate and the hydration of cis-aconitate (By similarity).
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O06644
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FCTA_OXAFO
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Formyl-CoA:oxalate CoA-transferase (FCOCT) (EC 2.8.3.16) (Formyl-coenzyme A transferase)
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MTKPLDGINVLDFTHVQAGPACTQMMGFLGANVIKIERRGSGDMTRGWLQDKPNVDSLYFTMFNCNKRSIELDMKTPEGKELLEQMIKKADVMVENFGPGALDRMGFTWEYIQELNPRVILASVKGYAEGHANEHLKVYENVAQCSGGAAATTGFWDGPPTVSGAALGDSNSGMHLMIGILAALEMRHKTGRGQKVAVAMQDAVLNLVRIKLRDQQRLERTGILAEYPQAQPNFAFDRDGNPLSFDNITSVPRGGNAGGGGQPGWMLKCKGWETDADSYVYFTIAANMWPQICDMIDKPEWKDDPAYNTFEGRVDKLMDIFSFIETKFADKDKFEVTEWAAQYGIPCGPVMSMKELAHDPSLQKVGTVVEVVDEIRGNHLTVGAPFKFSGFQPEITRAPLLGEHTDEVLKELGLDDAKIKELHAKQVV
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Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy. Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. It can also use succinate as acceptor.
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O06652
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HADDL_PSES4
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2-haloacid dehalogenase, configuration-inverting (EC 3.8.1.10) (DL-2-haloacid dehalogenase) (DL-DEXi)
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MSHRPILKNFPQVDHHQASGKLGDLYNDIHDTLRVPWVAFGIRVMSQFEHFVPAAWEALKPQISTRYAEEGADKVREAAIIPGSAPANPTPALLANGWSEEEIAKLKATLDGLNYGNPKYLILISAWNEAWHGRDAGGGAGKRLDSVQSERLPYGLPQGVEKFHLIDPEAADDQVQCLLRDIRDAFLHHGPASDYRVLAAWPDYLEIAFRDTLKPVALTTEFELTTSRIRKIAREHVRGFDGAGGVAWRDMADRMTPEEIAGLTGVLFMYNRFIADITVAIIRLKQAFGSAEDATENKFRVWPTEKG
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Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the corresponding (R)- and (S)-hydroxyalkanoic acids, respectively, with inversion of configuration at C-2. Acts on 2-haloalkanoic acids whose carbon chain lengths are five or less.
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O06728
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YISP_BACSU
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Farnesyl diphosphate phosphatase YisP (EC 3.1.7.6)
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MKEIKEAYQQCGQIVGEYAPACFKALSYLPLKQRQASWAVLSFCHTAASADEKVLPAFEAKADHVYQRTNNGKQHLWKAFDHAYRTFTLESEPFREFIAAQKEDAKPYDDLDELLMYAYRTGGAAGLMLLPILTRRKQDQLKQAAVSLGLAIQLVRFLSDLGTDQQKNRIPRQVMQQFGYTEADLQKGTVNKAFTMTWEYIAFEAEAYLEECQDALPLFPQYSQKTVKAALHLHRAVLEKIRAKQHDVFQYHFALTETEVKQILSDI
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A farnesyl diphosphate (FPP) phosphatase. Involved in biofilm formation, its disruption blocks biofilm synthesis which is restored by exogenous farnesol. Releases diphosphate from FPP, was initally suggested to be a squalene synthase. Diphosphate release is higher from FPP than geranyl pyrophosphate (GPP) or geranylgeranyl pyrophosphate (GGPP). Biofilm synthesis is partially restored by exogenous squalene, beta-carotene or retinol. Required for integrity of cell membrane lipid rafts. Involved in spatial organization of membranes, required for the flotillin-like proteins FloT and FloA to function correctly.
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O06769
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NCASE_MYCTU
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Neutral ceramidase (N-CDase) (NCDase) (EC 3.5.1.23) (Acylsphingosine deacylase) (N-acylsphingosine amidohydrolase)
|
MLSVGRGIADITGEAADCGMLGYGKSDQRTAGIHQRLRSRAFVFRDDSQDGDARLLLIVAELPLPMQNVNEEVLRRLADLYGDTYSEQNTLITATHTHAGPGGYCGYLLYNLTTSGFRPATFAAIVDGIVESVEHAHADVAPAEVSLSHGELYGASINRSPSAFDRNPPADKAFFPKRVDPHTTLVRIDRGEATVGVIHFFATHGTSMTNRNHLISGDNKGFAAYHWERTVGGADYLAGQPDFIAAFAQTNPGDMSPNVDGPLSPEAPPDREFDNTRRTGLCQFEDAFTQLSGATPIGAGIDARFTYVDLGSVLVRGEYTPDGEERRTGRPMFGAGAMAGTDEGPGFHGFRQGRNPFWDRLSRAMYRLARPTAAAQAPKGIVMPARLPNRIHPFVQEIVPVQLVRIGRLYLIGIPGEPTIVAGLRLRRMVASIVGADLADVLCVGYTNAYIHYVTTPEEYLEQRYEGGSTLFGRWELCALMQTVAELAEAMRDGRPVTLGRRPRPTRELSWVRGAPADAGSFGAVIAEPSATYRPGQAVEAVFVSALPNNDLRRGGTYLEVVRREGASWVRIADDGDWATSFRWQRQGRAGSHVSIRWDVPGDTTPGQYRIVHHGTARDRNGMLTAFSATTREFTVV
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Catalyzes the cleavage of the N-acyl linkage of the ceramides (Cers) to yield sphingosine (Sph) and free fatty acid. Also catalyzes the synthesis of Cers from Sph and fatty acid. Cers containning C6-C24 fatty acids are well hydrolyzed, and Cers with mono unsaturated fatty acids are much more hydrolyzed than those with saturated fatty acids.
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O06961
|
TDCD_SALTY
|
Propionate kinase (EC 2.7.2.15)
|
MNEFPVVLVINCGSSSIKFSVLDVATCDVLMAGIADGMNTENAFLSINGDKPINLAHSNYEDALKAIAFELEKRDLTDSVALIGHRIAHGGELFTQSVIITDEIIDNIRRVSPLAPLHNYANLSGIDAARHLFPAVRQVAVFDTSFHQTLAPEAYLYGLPWEYFSSLGVRRYGFHGTSHRYVSRRAYELLDLDEKDSGLIVAHLGNGASICAVRNGQSVDTSMGMTPLEGLMMGTRSGDVDFGAMAWIAKETGQTLSDLERVVNKESGLLGISGLSSDLRVLEKAWHEGHERARLAIKTFVHRIARHIAGHAASLHRLDGIIFTGGIGENSVLIRQLVIEHLGVLGLTLDVEMNKQPNSHGERIISANPSQVICAVIPTNEEKMIALDAIHLGNVKAPVEFA
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Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. It can also use acetyl phosphate as phosphate group acceptor.
|
O06967
|
BMRA_BACSU
|
Multidrug resistance ABC transporter ATP-binding/permease protein BmrA (EC 7.6.2.-)
|
MPTKKQKSKSKLKPFFALVRRTNPSYGKLAFALALSVVTTLVSLLIPLLTKQLVDGFSMSNLSGTQIGLIALVFFVQAGLSAYATYALNYNGQKIISGLRELLWKKLIKLPVSYFDTNASGETVSRVTNDTMVVKELITTHISGFITGIISVIGSLTILFIMNWKLTLLVLVVVPLAALILVPIGRKMFSISRETQDETARFTGLLNQILPEIRLVKASNAEDVEYGRGKMGISSLFKLGVREAKVQSLVGPLISLVLMAALVAVIGYGGMQVSSGELTAGALVAFILYLFQIIMPMGQITTFFTQLQKSIGATERMIEILAEEEEDTVTGKQIENAHLPIQLDRVSFGYKPDQLILKEVSAVIEAGKVTAIVGPSGGGKTTLFKLLERFYSPTAGTIRLGDEPVDTYSLESWREHIGYVSQESPLMSGTIRENICYGLERDVTDAEIEKAAEMAYALNFIKELPNQFDTEVGERGIMLSGGQRQRIAIARALLRNPSILMLDEATSSLDSQSEKSVQQALEVLMEGRTTIVIAHRLSTVVDADQLLFVEKGEITGRGTHHELMASHGLYRDFAEQQLKMNADLENKAG
|
An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).
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O07006
|
PADC_BACSU
|
Phenolic acid decarboxylase PadC (PAD) (EC 4.1.1.102)
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MENFIGSHMIYTYENGWEYEIYIKNDHTIDYRIHSGMVAGRWVRDQEVNIVKLTEGVYKVSWTEPTGTDVSLNFMPNEKRMHGIIFFPKWVHEHPEITVCYQNDHIDLMKESREKYETYPKYVVPEFAEITFLKNEGVDNEEVISKAPYEGMTDDIRAGRL
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Involved in the decarboxylation and detoxification of phenolic derivatives. It is able to catalyze the decarboxylation of ferulic, p-coumaric and caffeic acids.
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O07012
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BGAL2_BACSU
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Beta-galactosidase GanA (Beta-gal) (EC 3.2.1.23) (Beta-1,4-galactooligomerase) (Galactooligomerase)
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MLHGGDYNPDQWLDRPDILADDIKLMKLSHTNTFSVGIFAWSALEPEEGVYQFEWLDDIFERIHSIGGRVILATPSGARPAWLSQTYPEVLRVNASRVKQLHGGRHNHCLTSKVYREKTRHINRLLAERYGHHPALLMWHISNEYGGDCHCDLCQHAFREWLKSKYDNSLKTLNHAWWTPFWSHTFNDWSQIESPSPIGENGLHGLNLDWRRFVTDQTISFYENEIIPLKELTPDIPITTNFMADTPDLIPYQGLDYSKFAKHVDAISWDAYPVWHNDWESTADLAMKVGFINDLYRSLKQQPFLLMECTPSAVNWHNVNKAKRPGMNLLSSMQMIAHGSDSVLYFQYRKSRGSSEKLHGAVVDHDNSPKNRVFQEVAKVGETLERLSEVVGTKRPAQTAILYDWENHWALEDAQGFAKATKRYPQTLQQHYRTFWEHDIPVDVITKEQDFSPYKLLIVPMLYLISEDTVSRLKAFTADGGTLVMTYISGVVNEHDLTYTGGWHPDLQAIFGVEPLETDTLYPKDRNAVSYRSQIYEMKDYATVIDVKTASVEAVYQEDFYARTPAVTSHEYQQGKAYFIGARLEDQFQRDFYEGLITDLSLSPVFPVRHGKGVSVQARQDQDNDYIFVMNFTEEKQLVTFDQSVKDIMTGDILSGDLTMEKYEVRIVVNTH
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Involved in galactan degradation. Hydrolyzes galactooligosaccharides released by the endo-beta-1,4-galactanase GanB from galactan. Degrades galactotetraose, galactotriose and galactobiose, generating galactose as the end product. It is unable to use lactose. In vitro, shows maximal activity with o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-galactopyranoside (PNPG) as substrates, trace activity with p-nitrophenyl-alpha-L-arabinopyranoside and o-nitrophenyl-beta-D-fucopyranoside as substrates, but no activity with p-nitrophenyl-alpha-D-galactopyranoside, p-nitrophenyl-beta-D-glucopyranoside, o-nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-D-mannopyranoside or p-nitrophenyl-alpha-L-arabinofuranoside as substrates.
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O07427
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MGLL_MYCTU
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Monoacylglycerol lipase (MGL) (EC 3.1.1.23)
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MTTTRTERNFAGIGDVRIVYDVWTPDTAPQAVVVLAHGLGEHARRYDHVAQRLGAAGLVTYALDHRGHGRSGGKRVLVRDISEYTADFDTLVGIATREYPGCKRIVLGHSMGGGIVFAYGVERPDNYDLMVLSAPAVAAQDLVSPVVAVAAKLLGVVVPGLPVQELDFTAISRDPEVVQAYNTDPLVHHGRVPAGIGRALLQVGETMPRRAPALTAPLLVLHGTDDRLIPIEGSRRLVECVGSADVQLKEYPGLYHEVFNEPERNQVLDDVVAWLTERL
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Involved in the hydrolysis of exogenous host lipids during chronic infection (Probable). Catalyzes the hydrolysis of both monoacylglycerols (MAG) and diacylglycerols (DAG), with a preference for MAG. It hydrolyzes 2-MAG, 1-3-MAG and MAG with short, medium and long chain fatty acids such as 1-monobutyroyl-rac-glycerol (MC4), 1-mono-octanoyl-rac-glycerol (MC8), 1-monodecanoyl-rac-glycerol (MC10), 1-monolauroyl-rac-glycerol (MC12), 1-monomyristoyl-rac-glycerol (MC14) and 1-mono-oleyl-rac-glycerol (MC18:1). Also able to hydrolyze DAG with short (DiC6) and medium (DiC10) fatty acid chains, but not with longest fatty acid chains. Can also hydrolyze vinyl laurate (VC12), vinyl butyrate (VC4) and vinyl propionate (VC3). Induces an inflammatory response and cell apoptosis in the host cells. Increases expression of IL-6, NF-kappaB, TLR-2, TLR-6, TNF-alpha, and MyD88 in mouse alveolar macrophage RAW264.7 cells. Persistent expression induces RAW264.7 cell apoptosis in vitro.
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O07431
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CAMT_MYCTU
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Catechol O-methyltransferase (COMT) (EC 2.1.1.6)
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MGMDQQPNPPDVDAFLDSTLVGDDPALAAALAASDAAELPRIAVSAQQGKFLCLLAGAIQARRVLEIGTLGGFSTIWLARGAGPQGRVVTLEYQPKHAEVARVNLQRAGVADRVEVVVGPALDTLPTLAGGPFDLVFIDADKENNVAYIQWAIRLARRGAVIVVDNVIRGGGILAESDDADAVAARRTLQMMGEHPGLDATAIQTVGRKGWDGFALALVR
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Catechol O-methyltransferase that can use various catechol-like compounds such as gallic acid (GA), 3,4-dihydroxy-5-methoxy-benzoic acid (5OMeBA), protocatechuic acid (PCA), 3,4-dihydroxy-benzaldehyde (DHA), dopamine, caffeic acid (CA), luteolin, quercetin, and 5-hydroxyuridine.
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O07532
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LYTF_BACSU
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Peptidoglycan endopeptidase LytF (EC 3.4.-.-) (Autolysin LytF) (Cell wall-associated polypeptide CWBP49') (Gamma-D-glutamate-meso-diaminopimelate muropeptidase LytF) (Peptidoglycan hydrolase LytF) (Vegetative cell wall hydrolase LytF)
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MKKKLAAGLTASAIVGTTLVVTPAEAATIKVKSGDSLWKLAQTYNTSVAALTSANHLSTTVLSIGQTLTIPGSKSSTSSSTSSSTTKKSGSSVYTVKSGDSLWLIANEFKMTVQELKKLNGLSSDLIRAGQKLKVSGTVSSSSSSSKKSNSNKSSSSSSKSSSNKSSSSSSSTGTYKVQLGDSLWKIANKVNMSIAELKVLNNLKSDTIYVNQVLKTKSSGSDTSSKDNSSKSNQTSATTKYTVKSGDSLWKIANNYNLTVQQIRNINNLKSDVLYVGQVLKLTGKASSGSSSSSSSSSNASSGTTTTYTVKSGDSLWVIAQKFNVTAQQIREKNNLKTDVLQVGQKLVISGKASSSSSSGSSNTTSSTSAKINTMISAAKAQLGVPYRWGGTTPSGFDCSGFIYYVLNKVTSVSRLTAAGYWNTMKSVSQPAVGDFVFFSTYKAGPSHVGIYLGNGEFINANDSGVVISNMNNSYWKQRYLGAKRYF
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Cell wall hydrolase that cleaves gamma-D-glutamate-meso-diaminopimelate bonds in peptidoglycan. LytF is necessary and sufficient for vegetative daughter cell separation, and also seems to play a role in cell autolysis.
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O07566
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NTDA_BACSU
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3-oxo-glucose-6-phosphate:glutamate aminotransferase (EC 2.6.1.104) (3-dehydro-glucose-6-phosphate--glutamate transaminase) (Kanosamine 6-phosphate transaminase)
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MQKQVKISGKSKENMSLLKHLKGDVQGKELVIEDSIVNERWKQVLKEKIDIEHDLFNYQKNREISKVPFLPVDRLITNDEVEDILNTLTEVLPTGKFTSGPYLEQFEKVLSTYLHKRYVIATSSGTDAIMIGLLALGLNPGDEVIMPANSFSATENAVLASGGVPIYVDINPQTFCIDPDKIEEAITPYTKFILPVHLYGKHSDMQHIRQIANRYKLKVIEDACQGIGLTDLGKYADITTLSFNPYKNFGVCGKAGAIATDNEELAKKCIQFSYHGFEVNVKNKKVINFGFNSKMDNLQAAIGLERMKYLSLNNFKRLFLADRYITQLAELQNKGYIELPELSEDHVWHLFPIKVRTEDRADIMTKLNEDFGVQTDVYYPILSHMQKTPLVQDKYAGLQLVHTEKAHSQVLHLPLYPSFTLEEQDRVMEGLFHVIKQEIGV
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Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the reversible pyridoxal phosphate-dependent transamination of 3-dehydro-alpha-D-glucose 6-phosphate to form alpha-D-kanosamine-6-phosphate. It can only use alpha-anomer and glutamate is the only amino donor.
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O07600
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FABH2_BACSU
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Beta-ketoacyl-[acyl-carrier-protein] synthase III 2 (Beta-ketoacyl-ACP synthase III 2) (KAS III 2) (EC 2.3.1.180) (EC 2.3.1.300) (3-oxoacyl-[acyl-carrier-protein] synthase 3 2) (3-oxoacyl-[acyl-carrier-protein] synthase III 2) (Branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase 2) (bFabH2)
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MSKAKITAIGTYAPSRRLTNADLEKIVDTSDEWIVQRTGMRERRIADEHQFTSDLCIEAVKNLKSRYKGTLDDVDMILVATTTSDYAFPSTACRVQEYFGWESTGALDINATCAGLTYGLHLANGLITSGLHQKILVIAGETLSKVTDYTDRTTCVLFGDAAGALLVERDEETPGFLASVQGTSGNGGDILYRAGLRNEINGVQLVGSGKMVQNGREVYKWAARTVPGEFERLLHKAGLSSDDLDWFVPHSANLRMIESICEKTPFPIEKTLTSVEHYGNTSSVSIVLALDLAVKAGKLKKDQIVLLFGFGGGLTYTGLLIKWGM
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Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for branched chain acyl-CoA, determining the biosynthesis of branched-chain of fatty acids instead of straight-chain.
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O07623
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SBOA_BACSU
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Subtilosin-A (Antilisterial bacteriocin subtilosin)
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MKKAVIVENKGCATCSIGAACLVDGPIPDFEIAGATGLFGLWG
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Has bacteriocidal activity against some Gram-positive bacteria such as Listeria, some species of Bacillus and E.faecium. A single mutation (Thr-14-Ile) confers hemolytic activity against rabbit and human blood.
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O07732
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LIPJ_MYCTU
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Bifunctional lipase/adenylate cyclase LipJ [Includes: Lipase (EC 3.1.1.-); Adenylate cyclase (EC 4.6.1.1) (Adenylyl cyclase)]
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MAQAPHIHRTRYAKCGDMDIAYQVLGDGPTDLLVLPGPFVPIDSIDDEPSLYRFHRRLASFSRVIRLDHRGVGLSSRLAAITTLGPKFWAQDAIAVMDAVGCEQATIFAPSFHAMNGLVLAADYPERVRSLIVVNGSARPLWAPDYPVGAQVRRADPFLTVALEPDAVERGFDVLSIVAPTVAGDDVFRAWWDLAGNRAGPPSIARAVSKVIAEADVRDVLGHIEAPTLILHRVGSTYIPVGHGRYLAEHIAGSRLVELPGTDTLYWVGDTGPMLDEIEEFITGVRGGADAERMLATIMFTDIVGSTQHAAALGDDRWRDLLDNHDTIVCHEIQRFGGREVNTAGDGFVATFTSPSAAIACADDIVDAVAALGIEVRIGIHAGEVEVRDASHGTDVAGVAVHIGARVCALAGPSEVLVSSTVRDIVAGSRHRFAERGEQELKGVPGRWRLCVLMRDDATRTR
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May play a role in cell wall modulation. The N-terminal domain exhibits lipolytic activity. In vitro, hydrolyzes various p-nitrophenyl (pNP) esters. pNP-decanoate (C10) is the best substrate, followed by pNP-octonate (C8), pNP-laurate (C12) and pNP-butyrate (C4). Exhibits lower activity with pNP-acetate (C2), pNP-myristate (C14) and pNP-palmitate (C16). Can also use tributyrin. The C-terminal domain catalyzes the biosynthesis of cyclic AMP (cAMP) from ATP. It has a guanylyl cyclase side-activity, corresponding to 7% of the adenylate cyclase activity.
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