accession stringlengths 6 10 | name stringlengths 6 11 | Full Name stringlengths 1 147 ⌀ | taxon stringlengths 3 46 ⌀ | sequence stringlengths 16 2.75k | function stringlengths 6 5.51k | AlphaFoldDB stringlengths 6 10 |
|---|---|---|---|---|---|---|
Q62737 | CY24A_RAT | p22-phox | Rattus | MGQIEWAMWANEQALASGLILITGGIVATAGRFTQWYFGAYSIVAGVLICLLEYPRGKRKKGSTMERCGQKYLTAVVKLFGPLTRNYYVRAVLHLLLSVPAGFLLATILGTVCLAIASVIYLLAAIRGEQWTPIEPKPKERPQVGGTIKQPPTNPPPRPPAEVRKKPSEAEEEAASAGGPQVNPIPVTDEVV | Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide. | Q62737 |
Q1I2G6 | HEM6_PSEE4 | Oxygen-dependent coproporphyrinogen-III oxidase | Pseudomonas | MTSRTEAVKAYLLDLQDRICSALETEDGGARFVEDAWVRDAGGGGRTRVIGEGKVIEKGGVNFSHVFGAGLPPSASAHRPELAGRGFEALGVSLVIHPHNPHVPTSHANVRFFIAEKEGEEAVWWFGGGFDLTPYYGNEEDCVHWHRVAEQACAPFGADVYPRYKAWCDRYFHLKHRGEPRGIGGLFFDDLNEWDFDTCFAFMRAIGDAYVDAYLPIIQRRKDTPYTAKQREFQEYRRGRYVEFNLVYDRGTLFGLQSGGRTESILMSLPPQVRWGYDWKAEPGSEEARLTDYFLQDRDWLAQ | Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. | Q1I2G6 |
B0JI44 | PCXA_MICAN | Proton extrusion protein PcxA | Microcystis | MNLNRILQGVNQWLLQTPERSLDEAYHAALKIKEIEDKHFQGRKVANEFSNYGSSTNSYFIAEVKGYLQKIKVRLTEFKASRSIVNTFGPNQPTINNGVITVTTDVCLKKLQFIDSIIGKYQDNYWQEDIQDVPKSIQNRNFEQETAKNKTSRNRSFLAAGSIEDEEIIKSNKSQKATEKPGVLPRSFVNTFNRIKQEIDPQAEESEEAVLKKFRNSRYKTAISLKFILLLIIVPLLTQQLTKTFLITPLVNKYFQQQEQFIFINQDLEEEAFSELRRFEEALHFRGMIGLAPKLSNEEIEGEITKKAAVLSEEFRQRGLNAIANIFADICSLIAFGFVVAFSRREIEIVKSFLDGILYNLSDSAKAFLIILFTDIFVGFHSPHGWEVILEGLSRHFGLPENRQFNFLFIATFPVILDTVLKYWIFRYLNRISPSAVATYRNMNE | Involved in light-induced Na(+)-dependent proton extrusion. Also seems to be involved in CO(2) transport. | B0JI44 |
Q7ZX60 | P4R3A_XENLA | SMEK homolog 2-A | Xenopus | MSDTRRRVKVYTLNEDRQWDDRGTGHVSSTYVERLKGMSLLVRAESDGSLLLESKINPNTAYQKQQDTLIVWSEAENYDLALSFQEKAGCDEIWEKICQVQGKDPSVEVTQDPIDESEEERFEEMPETSNLIDLPTCELGKLEEIADLVTSVLSSPIRREKLALALENEGYIKKLLQLFQTCENLDNTEGLHHLYEIIRGILFLNKAALFEVMFSDECIMDVVGCLEYDPALAQPKRHREFLTKTAKFKEVIPITDSELRQKIHQTYRVQYIQDVILPTPSVFEENFLSTLTSFIFFNKVEIVSMLQEDEKFLSEVFAQLTDEATDDDKRRELVNFFKEFCAFSQTLQPQNRDAFFKTLANLGILPALEIVMGMDDLQVRAAATDIFSYLVEFSPSMVREFVMQEAQQSDDDILLINVVIEQMICDSDPELGGAVQLMGLLRTLIDPENMLATANKTEKSEFLNFFYNHCMHVLTAPLLANTSEDKLEKDAVFGSIKTSTVCPDNYQTAQLLALILELLTFCVEHHTYHIKNYIMNKDLLRRVLILMNSKHTFLALCALRFMRRIIGLKDEFYNRYIIKGNLFDPVINALLDNGTRYNLLNSAIIELFEFIRVEDIKSLTSHIVENFYKALEPIEYVQTFKGLKTRYEQEKDRQSQKLSSVPSILRSNRFRRDARALEDDEELWFNEDDEEEGEAVVPPVEKTKPEDDFPEGYEKFLETKKAKELEDKENLPKRTSVGAFKFTFSHSVSAANGANSTNSKSVAAHTPPATSNGSSSKNTSLTTTVASTKGSLIGLVDYPDDEDEEEEEDASPRKRPRLGS | Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). | Q7ZX60 |
Q0P5L5 | SUMF1_BOVIN | Sulfatase-modifying factor 1 | Bos | MAAPALGPARGCGAELTLVLLLSLFLLLGWAAGGEEAGPEAGAPSLVGSCGCGNPQRPGAQGSSAAAHRYSREANAPGSVPGGRPSPPTKMVPIPAGVFTMGTDDPQIKQDGEAPARRVAIDAFYMDAYEVSNAEFEKFVNSTGYLTEAEKFGDSFVFEGMLSEQVKSDIQQAVAAAPWWLPVKGANWRHPEGPDSTVLHRPDHPVLHVSWNDAVAYCTWAGKRLPTEAEWEYSCRGGLQNRLFPWGNKLQPKGQHYANIWQGEFPVTNTGEDGFRGTAPVDAFPPNGYGLYNIVGNAWEWTSDWWTVHHSAEETINPKGPPSGKDRVKKGGSYMCHKSYCYRYRCAARSQNTPDSSASNLGFRCAADHLPTTG | Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent. 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile. Known substrates include GALNS, ARSA, STS and ARSE. | Q0P5L5 |
P12312 | PSBM_THEVL | Photosystem II reaction center protein M | Thermostichus | MEVNQLGFIATALFVLVPSVFLIILYVQTESQQKSS | One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation . This subunit is found at the monomer-monomer interface. Probably involved in dimerization of PSII; at the monomer-monomer interface the only protein-protein contacts observed are between the 2 PsbM subunits. Lipids, chlorophylls and carotenoids contribute strongly to PSII dimerization. | P12312 |
Q03046 | CEFD_AMYLA | Isopenicillin N epimerase | Amycolatopsis | MVATAWANAREQVSLDPAVTNLNAGSCGPLPRPVFDRVTVRARMAAGPMDFLSRQLPPLLWTARERLAGYLGARPERLAFATNVTGAVNLVASSVQPHLAAGGEILLSDQEYAPMRWCWERVARHQGLVVRTFRLPVQPLGSPDEVVEAATAAMGPRTRLLFFSHVVSSTGLVLPATRLCEEARRRGVLTVVDGAQAPGFTDLDLAALPCDYYAGSGHKWLLAPTGVGFLHFAEDQGGVLRPPQVSWGYRPDGENPSDERNRFGSTDRLRNLECEGTRDLCPWLAVPSAIDFQAGLGHGRVRERMRELAAFTRERLSGWRGLEPVTPAHPGLSGAMTAFRLPPGTDTAGLRHGLWDRFRIDVPVLDRPDGPLLRVSTHFYNTETEVERLAEALKELSK | Catalyzes the reversible isomerization between isopenicillin N and penicillin N. | Q03046 |
Q0RB94 | PANC4_FRAAA | Pantoate-activating enzyme 4 | Frankia | MLVRDRAELRAALVALDRAASSHPPAAAQDAGPARAASRHDRPVRAVVMTMGALHEGHASLLRAARARADQVVATIFVNPLQFGAGEDLDRYPRTLAADLAVCAREGVDVVFAPAVIHDPPPLVRFGAGPLGAVLEGASRPGHFDGMLTLVGTMLHLVQPDLAFFGRKDAQQLVCIRRMVADLAFDVTVIGVETAREPDGLARSSRNVYLTAEQRTEALALSRALAAGAAASADGAPAVLAAARAVLDAADGVDVDYLELAGPEDLGPVRGGPALLLVAARVGTTRLIDNVSLILPTDTQGA | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | Q0RB94 |
Q99811 | PRRX2_HUMAN | Paired-related homeobox protein 2 | Homo | MDSAAAAFALDKPALGPGPPPPPPALGPGDCAQARKNFSVSHLLDLEEVAAAGRLAARPGARAEAREGAAREPSGGSSGSEAAPQDGECPSPGRGSAAKRKKKQRRNRTTFNSSQLQALERVFERTHYPDAFVREELARRVNLSEARVQVWFQNRRAKFRRNERAMLASRSASLLKSYSQEAAIEQPVAPRPTALSPDYLSWTASSPYSTVPPYSPGSSGPATPGVNMANSIASLRLKAKEFSLHHSQVPTVN | May play a role in the scarless healing of cutaneous wounds during the first two trimesters of development. | Q99811 |
Q5HW86 | PYRF_CAMJR | OMP decarboxylase | Campylobacter | MKLCVALDLSTKEECLQLAKELKNLDIWLKVGLRAYLRDGFKFIEELKKVDDFKIFLDLKIHDIPNTMADACEEVSKLGVDMINIHASAGKIAIQEVMTRLSKFSKRPLVLAVSALTSFDEENFFSIYRQKIEEAVINFSKISYENGLDGMVCSVFESKKIKEHTSSNFLTLTPGIRPFGETSDDQKRVANLAMARENLSDYIVVGRPIYKNENPRAVCEKILNKIHRKNISENDIEQNYEVIQQKEWDMCNHFEEWIKTQPDKEHALKEFYAKCGIKY | Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). | Q5HW86 |
Q3AQF1 | AROC_CHLCH | 5-enolpyruvylshikimate-3-phosphate phospholyase | Chlorobium | MIQYVTAGESHGPALSAIVDGMPAGVPLTDEAINHQLARRQQGYGRGGRMKIETDKAEVLSGIRFGKTIGSPIAMVIRNRDWQNWTTTMAQFEQPQEAIPAITVPRPGHADLAGCIKYGFEDIRPVIERSSARETAARVAAGACAKLFLKALGIEIGSIVTAIGSAKEEMPQQELAAMLAHGAEAVATQADQSPVRMLSKSAETAAIAAIDEAKANGDTVGGIVDVFITGVPLGFGSYVQHNRRLDADLAAALLSIQAIKGVEIGTAFDNACKYGSQVHDEFIFSESGELTRPTNRAGGIEGSMSSGQVIHLRAAMKPISSLISPLQSFDIASMEPIPSRFERSDTCAVPAAGVVAEAVVAPVIANALLAKLGGDHFSEIHERLEAYRAYLANRLQRKS | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Q3AQF1 |
Q46WH5 | ENGB_CUPPJ | Probable GTP-binding protein EngB | Cupriavidus | MSLLHQARFFTTVNHLRDLPATAVPEVAFAGRSNAGKSTAINILCNQKRLAFSSRTPGRTQHINYFTVAPVKAPDPIAFLVDLPGYGYAEVSGSAKYHWQGLLSDYVQTRSQLSGLILMMDARRPFTDLDCQMVEWFLPTGKPVHVLLTKADKLTNSENAKALRETRKMLEGYAEQLATPVPLTAQLFSSLKRRGIEEAQRVIAGWLSLPEAQAAAPAEQPAAPGASE | Necessary for normal cell division and for the maintenance of normal septation. | Q46WH5 |
B1HVP3 | LGT_LYSSC | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase | Lysinibacillus | MDLLLLQINPIAFHLGPIPVRWYGLLIVSGIILAYVVGQREAVKRGLPEDFLADLLLWAVPISIICARIYYVSMRWDYYSENPGKIIEIWNGGIAIHGALIGAFVTAYIFTRIKNVSFLRVADIAAPSILIGQIIGRWGNFMNQEAYGGPVSKEFLENLMLPDWIINQMYIEELGTYVHPTFLYESVWNLIGLIILLILRKVNLNRGEIFFSYLIWYSIGRFYIEGMRTDSLYLVGDLRSAQIVSIIGIVVGLGAIIYRRIKVKPAMKYLDNK | Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. | B1HVP3 |
A3N0G0 | PCKA_ACTP2 | Phosphoenolpyruvate carboxykinase (ATP) | Actinobacillus | MLSRIEQELAQLGITNVKEIVRNPSYEQLFEEEMKPELEGFEKGRLTTSGAVAVDTGIFTGRSPKDKYIVYDETSKDNVWWTSDAVKNDNKPMNQATWQSLKELVTHQLSNKRLFVVDAFCGANKDSRVAVRIVTEVAWQAHFVKNMFVRPSEEELLNFVPDFVVMNGSKVTNPNWKEQGLNSENFVAFNLTEKIQLIGGTWYGGEMKKGLFSLMNYWLPLKGIASMHCSANVGAEGDVAVFFGLSGTGKTTLSTDPKRKLIGDDEHGWDDDGVFNYEGGCYAKTINLSEENEPDIYRAIRRDALLENVVVREDGSVDFADGSKTENTRVSYPIHHIDNIVEPVSKAGHAKKVIFLTADAFGVLPPVSKLTPEQTKYYFLSGFTAKLAGTERGITEPTPTFSACFGAAFLSLHPTKYAEVLVKRMEEAGSQAYLVNTGWNGSGKRISIKDTRGIIDAILDGSIEKAETKELPIFNLAIPTALPNVDPAILDPRDTYADKAQWQTKAEDLAGRFVKNFEKYTTNDEGKALVAAGPKL | Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. | A3N0G0 |
Q0TFD0 | ACCD_ECOL5 | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta | Escherichia | MSWIERIKSNITPTRKASIPEGVWTKCDSCGQVLYRAELERNLEVCPKCDHHMRMTARNRLHSLLDEGSLVELGSELEPKDVLKFRDSKKYKDRLASAQKETGEKDALVVMKGTLYGMPVVAAAFEFAFMGGSMGSVVGARFVRAVEQALEDNCPLICFSASGGARMQEALMSLMQMAKTSAALAKMQERGLPYISVLTDPTMGGVSASFAMLGDLNIAEPKALIGFAGPRVIEQTVREKLPPGFQRSEFLIEKGAIDMIIRRPEMRLKLASILAKLMNLPAPNPEAPREGVVVPPVPDQEPEA | Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. | Q0TFD0 |
P26310 | COX6_DICDI | Cytochrome c oxidase polypeptide VI | Dictyostelium | MSTGNESYNLRYPKGFKGYPYNMYKLEGYGTPKGYITLIGVVATLTVSGLFFAKTRSNKREYPTHNKEWRAKTLAYAKETNADPIYQLPKDKI | Component of the cytochrome c oxidase, the last enzyme in 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. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. | P26310 |
B2UGP7 | GLMM_RALPJ | Phosphoglucosamine mutase | Ralstonia | MSRKYFGTDGIRGRVGESPITPDFVLRLGYAAGRVLAHGGEAHGHGRPTVLIGKDTRLSGYMLEAALEAGFTAAGVDVLMSGPLPTPGVAYLTRALRLSAGVVISASHNPYYDNGIKFFSATGDKLPDETELQIEAELEKPMAYAASDALGRARRIEDAAGRYIEFCKSTFPSDLNLFGMKVVLDSAHGAAYHIAPHVFHELGADVVSIGNQPNGRNINDGYGATAPGKLVEATREHGADIGLAFDGDADRLQVVDRNGRLYNGDELLYVMVQARRAAGQTVPGAVGTLMTNLAVELALKAQGVEFVRAKVGDRYVLEELKKNGWLLGGEGSGHLLCLDKHSTGDGIISALQVLAALRRSGQTLDEMLDGVRLFPQKLINVRVEKGFDWKSHAGLQAALKTSEAELDGKGRVLIRPSGTEPVVRVMVEAQDAELANQHAERLAATLQ | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | B2UGP7 |
Q8U3X9 | NIKR_PYRFU | Putative nickel-responsive regulator | Pyrococcus | MGIVRFGVSIPKELLEKFDGIIEEMGYTNRSEAIRDLIRDMVVRHEWQLGDEEVAGTITIVYNHDEADVVRELLDLQHEYLNEIVSSLHVHMDEHNCLEVIVVKGRAKKIKKIADRLLSLKGVKHGKLVMTTTGRDIV | Transcriptional regulator. | Q8U3X9 |
Q83HU9 | YQGF_TROW8 | Putative pre-16S rRNA nuclease | Tropheryma | MVKSVADRFFLGLDFGSTRIGVARNCGSLAVPVGVLPRASCAEILGYISRYSIDEVVIGLPLTLAGKEKQSARLAKEFSRFLVSSGVQVRFFDERFTTVIATQKFYSLGKGVKQIRKCVDAAAATVMLQLFLDMEVKVDPLERKP | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | Q83HU9 |
Q0VQN0 | ACP_ALCBS | Acyl carrier protein | Alcanivorax | MSSIEERVNKIIVEQLGVKPEDVKSEASFVEDLGADSLDTVELVMALEEEFETEIPDEEAEKISTVQSAVDYIKAHS | Carrier of the growing fatty acid chain in fatty acid biosynthesis. | Q0VQN0 |
Q2JK64 | DXS_SYNJB | 1-deoxyxylulose-5-phosphate synthase | unclassified Synechococcus | MHLSDITHPNQLRNLNLSQLRSLARQIRDKHLQTAANSPVGCHLGPGLGVVELTLALYKTLDLDRDKVIWDVGHQAYAHKMLTGRYHNFHTLRQKGGISGYLKRSESRFDHFGAGHASTSISAALGMAIARDRRGDNFKVVAIIGDGALTGGMAYEAINHAGHLPKTNLMVVLNDNGMSISPNVGAIPRYLNRLRLSPPVQFLADSLEEQLKNLPLLGSSLSPEIDRLKETVKLVTAVQNNKAGIIFEELGFTYVGPVDGHNLAELLDAFELAHGISGPVLVHVATVKGKGYPPAEAEQVGYHAQSRFDLATGKPYPPTKPKPPSYSKVFGHALCKLAERDPRIIGITAAMDTGTGLDKLKEKLPDQFVDVGIAEQHAVTLAAGMACEGMRPVVAIYSTFLQRAYDQIIHDVCIQKLPVFFCLDRAGVVGADGPTHQGMYDIAYLRCIPEMVLMAPKDEAELQRMVVTGIQYTQGPIAMRYPRGSGVGVPLAEEGWEPLPIGKAEVLRSGGEVLILAYGSMVHPSLQAAEILKEHGISATVVNARFAKPLDTELILPLAEQSRLVVTVEEGCLMGGFGSAVAEALLDADLAVPLLRLGVPDVWVEHATPEESLAELGLNSAGIAERIRAKFQARVLKGSPAELPTVNS | Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP). | Q2JK64 |
B3QQE0 | ISPH_CHLP8 | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | Chlorobaculum | MKINLDRTSSGFCIGVQGTIHVAEEKLNQSGELYCLGDVVHNEVEVKRLEALGMETIDIPAFEELRDAEVLIRAHGEPPSTYETARRNNLAITDTTCPVVAKLQKTAKMLHQLGYQVIIYGKKIHPEVIGINGQCNDEGVVIKHPDLSDEAEIAPLDLGRKTALISQTTMDVPGFYELKKNLEKLFAEHGHRNPGTKSGEWMAVRDIDITSEKTGGRAMPELVYKDTICRQVSSRNGKLRDFALANDCIVFAAGRKSSNGQVLYSICKDANPHSYFIEDVDEIQPEWFVGENGKPVESVGICGATSTPMWLLEKVANYIGKTFGDDSGNPDA | Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. | B3QQE0 |
A2XFP3 | XXT1_ORYSI | Probable xyloglucan 6-xylosyltransferase 1 | Oryza sativa | MWVAERVVGERRMREIQRFARNAKLTVVCLLLTVVVLRGTVGAGKFGTPQQDLIELRHRFISHPHRALAEHHDALSRGGGSSSSSGRAAQRDDEPDPPPRTLRDPPYTLGPKISDWDEQRAAWHRRHPETPPFVNDVKPRVLLVTGSSPKPCENPVGDHYLLKSIKNKMDYCRVHGLEIFYNMALLDAEMAGFWAKLPLLRALLLAHPEIEFLWWMDSDAMFSDMAFELPWERYGPYNLIMHGWDEMVYDDKNWIGLNTGSFLLRNCQWSLDFLDTWAPMGPKGPVRIEAGKVLTKYLKDRPVFEADDQSAMVYILATEREKWGDKVYLENGYYLHGYWGILVDRYEEMLENYHPGLGDHRWPLVTHFVGCKPCGKFGDYPVERCLKQMERAFNFGDNQILQMYGFTHKSLGSRKVKRIRNETSNPLDVKDELGLLHPAFKAMKTTST | Probable xyloglucan xylosyltransferase involved in the biosynthesis of xyloglucan in roots. | A2XFP3 |
A5ECI7 | CH601_BRASB | Chaperonin-60 1 | unclassified Bradyrhizobium | MAAKDVKFAGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMLREVASKTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDTAVAAVIKDIEKRAKPVASSAEVAQVGTISANGDAAIGKMIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTAELDDVYVLLHEKKLSGLQAMLPVLEAVVQSGRPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISDDLGMKLENVTIKMLGRAKKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEIEVKEKKDRVEDALNATRAAVQEGIVPGGGVALLRAKKAVGRITNPNSDVQAGINIVLKALEAPVRQIAENAGVEGSLVVGKILEEKSETFGFDAQSEDYVDMVAKGIIDPAKVVRTALQDASSVAGLLVTTEAMVAELPKEAAPAMPAGGGMGGMGGMGF | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | A5ECI7 |
Q67UI2 | MUB2_ORYSJ | OsMUB2 | Oryza sativa | MASGGGGGGGMEAVEVRFRLDDGSDIGPSMHDQATTVTALKEFVLARWPQGKEIAPRTVNDVTIINAGQVLENNRTLAESRNLAAESPEGPITMHVVVRRSRPERRVKQPPKARPPERIGCGCTIL | May serve as docking site to facilitate the association of other proteins to the plasma membrane. | Q67UI2 |
A4WGV2 | RFCS1_PYRAR | Clamp loader small subunit 1 | Pyrobaculum | MAELFWFEKYRPRSFDEVVDLEEVKARLREFVRGGNMPHLLFYGPPGTGKTTMALVLARELYGEYWRENTLELNASDERGINVIRERVKEFARTAPVGKAPFKLVILDEADNMTSDAQQALRRIMEMYAQNTRFILLANYVSRIIDPIISRCAVFRFSPMPRSLMAERLRHIAKSEGIELRDDAIDLIYEVSEGDMRKAINLLQVAAATSKVVDANAVASATTMIRPADVVELFNLAFNGDVTKAREKLRELMYVKGIAGIDFIRAFQRELIRMPLDDEVKAEIAELLAEVDYRLTQGSDEELQLLYLLSKLGAIGKRARQTPPPSKRR | Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. | A4WGV2 |
Q823K6 | DCD_CHLCV | Deoxycytidine triphosphate deaminase | Chlamydia | MSIKEDKWIRKMALAHGMIEPFADGQVNVDAETGEKLISYGLSSYGYDLRLSREFKVFTNVYNSLVDPKHFTEDTFISITDDVCIIPPNSFALAHSVEYFRIPRNILTMCIGKSTYARCGLIVNVTPFEPEWEGYVTIEISNTTPLPAKIYANEGIAQVLFFEADEMCEVSYAERKGKYQKQQGITVPFV | Catalyzes the deamination of dCTP to dUTP. | Q823K6 |
Q1CBU1 | BTUB_YERPA | Outer membrane cobalamin translocator | Yersinia | MTIKKYTLLTALSVTAFSGWAQGNNTTDNNDEMVVTANRFPQPKSSVLAPVDVVTRADIDRWQSTNINDVLRRLPGVDIAQDGGMGQRSSLFIRGTNSSHVLVLIDGVRLNQAGITGASDLSQIPISLVQRIEYIRGPRSAVYGSDAIGGVINILTGRDKPGTTLSAGLGSNGYQTYDGSTQQKLGEDTTVTLAGNYTYSKGYDVVAGMPGAGGPRQPDRDGFMGKMLWAGLEHQFNEQFNGFARVYGFDNRSDYDGYTNYSNPLALIDTRKLSSRTYDTGLRYKNGIYASQFIASYNRTKDYNYSPLFGQHDITASLDEAEQYNLQWGNTFQLTNGMISAGADWQEQRTERKSSNQNTTADFTQHNTGIYLTGQQQISDVTLEGAVRSDDNSQFGWHSTWQTSAGWEFIDGYRLIGSYGTAYKAPNLMQLYSAYGGNANLKPEESKQWEGGVEGLTGPLTWRLSAYRNDIDQLIDYSNLTNGYFNINKATIKGVEWTGSFDTGPLSHQVTLEYLDPRNADTHEILVRRAKQQVKYQLDWQVADLDWSVTYQYLGQRYDKDYSTYPEETVELGGVSLWDLAVSYPVTSHLTVRGRIANLFDKDYEMVYGYQTPGREYYFTGSYNF | Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. | Q1CBU1 |
Q6J1H4 | UTF1_MOUSE | Undifferentiated embryonic cell transcription factor 1 | Mus | MLLRPRRLPAFSPPSPASPDAELRSAGDVPVTTSDAFATSGGMAEPGSPKAPVSPDSAQRTPWSARETELLLGTLLQPAMWRSLLLDRRQTLPTYRRVSAALARQQVRRTPAQCRRRYKFLKDKLRDSQGQPSGPFDNQIRQLMGLLGDDGPPRVRRRSTGPGRPQRRGRSSLSALAPAPAPVEQEAELPLAAENDEPAPALRFSSSTTKSAGAHRITSSPPLTSTDTLPPEPGHTFESSPTPTPDHDVETPNEPPGLSQGRASSPQVAPQSLNTALLQTLTHLGDISTVLGPLRDQLSTLNQHVEHLRGSFDQTVSLAVGFILGSAASERGILGDLRQ | Acts as a transcriptional coactivator of ATF2. | Q6J1H4 |
Q8PPE2 | NRDR_XANAC | Transcriptional repressor NrdR | Xanthomonas | MHCPFCQHNDTRVIDSRVSEDGTTIRRRRECEACGERFSTLETIELKLPTVVKSDGGREAFDARKLRTSFDRALQKRPVAEEQIEAAVRAVVHQLRMSGEREVGSLRVGEYVMVELRKLDHVGYVRFASVYRSFQDVADFREEIEKLERELPVGSEQLPLLEAALERAGKPGKR | Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes. | Q8PPE2 |
C0ZJF8 | NAGB_BREBN | Glucosamine-6-phosphate isomerase | Brevibacillus | MKLVIVKDYAELSRKAAEMLVSEVKANPKTVLGLATGGTPVGMYRELIKLSQAQSIDYSQASSFNLDEYVGLSSTHPQSYRSYMEENLFNHINIPAEKTHVPVGNTTDHLAECARYEEAIRLAGGIDIQVLGIGNNGHIGFNEPGSPADSLTRVVQLTDSTIEANARYFDSVEQVPTQAVSMGIKTILGAKKVVLLASGEAKAEAVRLMLEEEPTADVPASLLQLHRDVTVIVDQEAASKLTTSILAGTKPSGS | Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. | C0ZJF8 |
B8CWL4 | SYI_HALOH | Isoleucyl-tRNA synthetase | Halothermothrix | MDYKETINLPRTEFPMRANLSKREPGIEKYWEENNVYEKAIKNREGNKQFILHDGPPYANGDIHIGHALNKILKDIVTRYKTLSGYYSPYVPGWDTHGLPIEHKVTKEMGDKAKDLSVSELRDKCRDYALKYVERQKEQFKRLGVWGEWDKPYLTLNPEYEVKQIEVFGEMAKRGLFYKGKKPVHWCPSCETALAEAEVEYGEHRSPSIYVKFPLKDKVNVGGVELTPGDSYVVIWTTTPWTIPANMAIALHPEFDYVVVKASGEKLVMARELVDRVMEEAEVENYKVVGQAFKGTELENKRCRHPFEDRDSILILGDHVTLEQGTGCVHTAPGHGHDDYLVGLKYDLDIYAPMDNRGVFTEEAERFAGMYYDDVNKEVTKILDEKGLLMNLSFISHQYPHCWRCKGALIFRATDQWFASIEAIKEEALKAIHSVDWYPAWGEERMANMISERTDWCISRQKKWGVPIPVFYCKDCGHSIINDETIEAVKKLFAREGSSGWYKYSAEEILPEGFSCPECGGKSFKKEEDIMDVWFDSGSSHKAVLETRDHLSWPSQLYLEGTDQYRGWFNSSLLTAVATEGKPPYEAVVTNGFVVDDKGNKMSKSIGNVVSPQDVIKRYGADILRLWVASSNFKDDVRVSDRILKQNSEVYRRIRNTFRFILGNINDFNPGQHYVDYNDRAEIDRWIMIKLQDLIKDVTRAYDEYEYHRVYHDVHNFCTIEMSSLYVDIVKDRLYTDGTNSLSRRSAQSTLYDILLVLVKLVAPVLAHTAEEVWQHLDESSKDAESIFLTDWPEVVNEYYDDRLMSKWDKLLEVRKDVAKALELSRENKEIGNSLDARVILVPVDDKQRQLLKDNIDILPDLFIVSQVELQGETGEGFHKGSETGISVSVVKASGEKCARCWKYSEAVGNDEEHPELCERCVEVVRTEV | Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). | B8CWL4 |
Q9WTQ8 | TIM23_MOUSE | Mitochondrial import inner membrane translocase subunit Tim23 | Mus | MEGGGRSSNKSTSGLAGFFGAGGAGYSNADLAGVPLTGMNPLSPYLNVDPRYLVQDTDEFILPTGANKTRGRFELAFFTIGGCCMTGAAFGAMNGLRLGLKETQSMAWSKPRNVQILNMVTRQGALWANTLGSLALLYSAFGVIIEKTRGAEDDLNTVAAGTMTGMLYKCTGGLRGIARGGLAGLTLTSLYALYNNWVHMKGSLLQQSL | Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. | Q9WTQ8 |
B8IT33 | RS13_METNO | 30S ribosomal protein S13 | Methylobacterium | MARIAGVNIPTNKRVVIALQYIHGIGPKKAEEITEKVGIPAERRVNQLTDAEVLQIREAIDRDYIVEGDLRREVAMNIKRLMDLGCYRGLRHRRNLPVRGQRTHTNARTRKGKAKPIAGKKK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. | B8IT33 |
Q1QTN9 | FABV_CHRSD | Enoyl-[acyl-carrier-protein] reductase [NADH] | Chromohalobacter | MIIKPKVRGFICTTTHPLGCERNVAEQIATTRANIPESERDKGPKNVLVIGASSGYGLAARVTAAFGYGASTLGVFFEKPGTEKKPGTAGWYNAAAFDKFAKAEGLYSKAINGDAFSHEAREKAIELIKQDMGQIDLVVYSLASPVRKLPDSGELKRSALKPIGETYTATAIDTNKDAIVEASVEPATEEEIADTVTVMGGEDWELWVDALDKAGVLAPGARSVAFSYIGTEITWPIYWHGALGKAKEDLDRAAGELDARLGQHGGGANVAVLKSVVTQASAAIPVMPLYISMVYKVMKEQGLHEGTIDQLNRLYRERLYSTQGQNGELATDEAGRLRLDDWELRDDVQQACQDLWPQVTTENLFTLTDYAGYKREFLKLFGFERDDVDYEADVDPVAEFDVVQL | Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). | Q1QTN9 |
A1TJ08 | RL4_ACIAC | 50S ribosomal protein L4 | Acidovorax | MQLELLNDQGQAASKIDVPETVFDRQYNEDLIHQIVVAYRANARQGTRAQKDREQVRHSTKKPFKQKGTGNARAGMTSSPLWRGGGRIFPNLPEENFTQKINKKMYRAGMASILSQLAREGRLAVVDSLKVETPKTKVLADKFKAMNLQSVMVISDEVDENLYLASRNLKNVFVVEPRYADPVSLVHYKKVLVTKGAIDKLKEMFA | Forms part of the polypeptide exit tunnel. | A1TJ08 |
Q8N8Y5 | ZFP41_HUMAN | Zinc finger protein 41 homolog | Homo | MEKPAGRKKKTPTPREEADVQKSALREEKVSGDRKPPERPTVPRKPRTEPCLSPEDEEHVFDAFDASFKDDFEGVPVFIPFQRKKPYECSECGRIFKHKTDHIRHQRVHTGEKPFKCAQCGKAFRHSSDVTKHQRTHTGEKPFKCGECGKAFNCGSNLLKHQKTHTGEKPYECTHCGKAFAYSSCLIRHQKRHPRKKP | A putative DNA-binding regulatory protein associated with meiosis in spermatogenesis. | Q8N8Y5 |
Q756Q3 | NPC2_ASHGO | Phosphatidylglycerol/phosphatidylinositol transfer protein | Eremothecium | MRVSVWYGLLHAAAWTRAVSLQVSEDSDEQWTVALRDSRPIPGGSPLSRCDLDEDHLLDVQEIEITPNPPHRGKNLTVEARGDLFGPVEDGAYVTVEVRLGYIKLLSETFDLCKELEENDLGLQCPLEEGEYELSKTVEIPQQVPPGRYHVVARAYTVDDEPITCLTGDVYFPPLMPAERSRMPRLIDPRRMRRLMDPRRKPRIMDEGSGAAA | Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol. | Q756Q3 |
Q42395 | FCP_TRICV | Fucoxanthin-chlorophyll a-c binding protein, chloroplastic | Trieres | MKLAIAALLAGSAAAFAPAQSGKASTALNMAFESELGAQPPLGFFDPLGMLADADQERFDRLRYVEVKHGRIAHVAFLGQIVTRNGIHLSGNIDYAGNSFDSFPNGWAAISGPDAIPQAGLLQIVAFVGILELAVMKDVTGEGEFPGDFRNGALDFGWDTFDEETKLSKRAIELNNGRAAMMGILGLMVHEQLGGSIPIVGEM | The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. Energy is transferred from the carotenoid and chlorophyll C (or B) to chlorophyll A and the photosynthetic reaction centers where it is used to synthesize ATP and reducing power. | Q42395 |
Q04087 | LRS4_YEAST | Loss of rDNA silencing protein 4 | Saccharomyces | MTTLLQLLSNYYKAKLDSERIYNEYVQSQYEFASLDKLNNNKGDPKKVVDETLFLQRQIAQLNKQLQLSFQENEKLLSVQKNQKALYQSKLSSKDAFIDDLKLKLKVEQISVDKHNKERTPSTGRDEQQRNSKAAHTSKPTIHLLSPIVNRDKPNNQTNDRGGNDPDSPTSQRRSRGLRSLLSSGKNTIFDSISKNLDDEINENAHIRNDTTSSKIAGKSPSRLSALQKSPELRKERNNMILKEHILRSKDDQNITSSRKLDNIELSSIGDSTAMTSRSSTVNANDILGNEENDGITKLKRVNKLTSSPVKRDCSTNKKRKLTKQRIATLPNSDEELSNNLNVDEFV | Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Involved in rDNA silencing. | Q04087 |
A9MLY7 | RECR_SALAR | Recombination protein RecR | Salmonella | MQTSPLLTQLMEALRCLPGVGPKSAQRMAFTLLQRDRSGGMRLAQALTRAMAEIGHCADCRTFTEQEVCNICANPRRQENGQICVVESPADIYAIEQTGQFSGRYFVLMGHLSPLDGIGPDDIGLDRLEQRLVSEKISELILATNPTVEGEATANYIAELCAQYGVEASRIAHGVPVGGELEMVDGTTLSHSLAGRHKIIL | May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | A9MLY7 |
Q29429 | IFNT6_SHEEP | Trophoblastin | Ovis | MAFVLSLLMALVLVSYGPGGSLGCYLSRKLMLDARENLRLLDRMNRLSPHSCLQDRKDFGLPQEMVEGDQLQKDQAFSVLYEMLQQSFNVFHTERSSAAWNTTLLEQLCTGLQQQLDHLDTCRGPVMGEKDSELGKMDPIVTVKKYFQGIHDYLQEKGYSDCAWEIVRVEMMRALTSSTTLQKRLTKTGGDLNSP | Paracrine hormone primarily responsible for maternal recognition of pregnancy. Interacts with endometrial receptors, probably type I interferon receptors, and blocks estrogen receptor expression, preventing the estrogen-induced increase in oxytocin receptor expression in the endometrium. This results in the suppression of the pulsatile endometrial release of the luteolytic hormone prostaglandin F2-alpha, hindering the regression of the corpus luteum (luteolysis) and therefore a return to ovarian cyclicity. This, and a possible direct effect of IFN-tau on prostaglandin synthesis, leads in turn to continued ovarian progesterone secretion, which stimulates the secretion by the endometrium of the nutrients required for the growth of the conceptus. In summary, displays particularly high antiviral and antiproliferative potency concurrently with particular weak cytotoxicity, high antiluteolytic activity and immunomodulatory properties. In contrast with other IFNs, IFN-tau is not virally inducible. | Q29429 |
B8B406 | MCM9_ORYSI | Minichromosome maintenance 9 | Oryza sativa | MPPPAEEFAVDDLDEFESRLDSFLNRFHADDLRRILLPDPDGKLHFPLVIDFAELLEFDPEVAHQLYDYPKDVLELFDAAAQRALDKFDAAARRADKRKAGDEPMEKKFVHVRVNTSGSPLECPEASPSIGKVRVKHRGTLLTLKGTVIRSGGVKMIEGERKYQCRKCKCRFTVHPELEAGNRITLPASCKSKSAKGCGGANFQLIEDSITCHDYQEIKIQENIQLLGVGSIPRSMPIILMDDLVDIVKAGDDVVVTGRLSAKWSPDIKDVRSNLDPMLIANFVRRTNELKSDLDIPVEIINKFEEFWAASRATPLKGRNSILKGICPQIYGLFTVKLAVALTLIGGVQHVDASGTKVRGEPHMLLVGDPGTGKSQFLKFAAKLSNRSVITTGLGSTSAGLTVTAVKDGGEWMLEAGALVLADGGLCCIDEFDSMREHDRTTIHEAMEQQTISIAKAGLVTTLNTRTTVFGATNPKGQYDPNESLSVNTTLSGPLLSRFDIVLVLLDTKNKKWDKIVSSHILAENTEEKKGKTSDPEVMWTLSMLRRYIHYVKQHFKPVLTKEAERVISSYYQRQRQSGTRNAARTTVRMLESLIRLAQAHARLMFRNDVTKLDAIAAILCIESSMTTSAIVDTAGNALHSNFTENPDQECILKCDSIAYLSKNIKYLTDEISN | Probable DNA helicase that may play a role in DNA repair during meiosis. | B8B406 |
B3KYH4 | TPA_PELSA | Temporin-1Sa | Pelophylax | FLGTINLSLCEQERDADEEERRDEPNESNVEVEKRFLSGIVGMLGKLFGK | Amphipathic alpha-helical antimicrobial peptide with highly potent activity against Gram-positive bacteria, and potent activity Gram-negative bacteria and fungi (MIC=2-30 uM) . Acts through membranolytic mechanism involving rapid membrane permeabilization and depolarization . Shows a direct extra-cellular antiviral activity probably through degradation of the viral envelope . Also shows a weak indirect antiviral activity by inhibiting virus replication . Also displays anti-trypanosoma and anti-leishmania (prosmastigotes and axenic amastigotes) activity through membranolytic mechanism . Also induces apoptosis in leishmania promastigotes at high peptide concentrations . Shows moderate hemolytic activity (LC(50)=25 uM) . In contrast to many antibiotics, this peptide does not induce bacterial resistance . | B3KYH4 |
Q57RH4 | MODC_SALCH | Molybdenum import ATP-binding protein ModC | Salmonella | MLELNFSQTLGTHCLTLNETLPASGITAIFGVSGAGKTSLINAISGLTRPQKGRIALNGRVLHDAENGICLTPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSMTGQFDKLVSLLGIEALLDRLPGSLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLEDGQVKAFGPLEEVWGSSVMHPWLPKEQQSSILKVSVLEHHPHYAMTALALGDQHLWVNKLNQPLQSTLRIRIQASDVSLVLQPPQQTSIRNVLRAKVANCYDDNGQVEVQLEIGGRTLWARISPWARDELNIKPGLWLYAQVKSVSITA | Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system. | Q57RH4 |
P23011 | RBL_XANFL | Ribulose bisphosphate carboxylase large chain | Xanthobacter | MGADAAIGQIKDAKKRYAAGVLKYAQMGYWDGDYQPKDTDILALFRVTPQDGVDPVEAAAAVAGESSTATWTVVWTDRLTAADMYRAKAYKVEPVPGQPGQYFCWVAYELDLFEEGSIANLTASIIGNVFSFKPLKACRLEDMRLPVAYVKTFRGPPTGIVVERERLDKFGRPLLGATTKPKLGLSGKNYGRVVYEGLKGGLDFVKDDENINSQPFMHWRDRFLYCMEAVNKAQAETGEVKGHYLNITAGTMEEMYRRADFAKELGSVVVMVDLIVGWTAIQSISNWCRENDMLLHMHRAGHGTYTRQKGHGISFRVIAKWLRLAGVDHLHTGTAVGKLEGDPMTVQGYYNVCREDVTRTDYTRGIFFDQDWAGLRKVMPVASGGIHAGQMHQLIDLFGEDVVLQFGGGTIGHPDGIQAGAIANRVALETMILARNEGRDIKNEGPEILVEAAKWCQPLRAALDTWGEVTFNYASTDTSDFVPTASVA | 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. Both reactions occur simultaneously and in competition at the same active site. | P23011 |
Q1AXL8 | ISPE_RUBXD | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Rubrobacter | MRGSLRVRAFAKVNYALEVLGRRADGYHEIRTVLQSVSLWDELEISGPEGRFGLVVEPEGAGVGPERENTVYRAWRLLAGEAGAPPVRVTLRKGIPAGSGLGGGSADAAALLWGANELLGLGLGEADLAALALRVGADVPFCLVGGTALGEGVGERLFPLPAPPEHRLVVAMPPRGASTAEVYGAYGGLGGAAPGGWSGRVVRALRAGDLGALGAAVGNDLTPVTAGLAPEVEKLLAGLREAGALGACMSGTGSAVYGLFREEAAAHEAARRLGGAAFVRVCRPVGRGLAGG | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | Q1AXL8 |
Q8L2F3 | GRPE_MEIRU | HSP-70 cofactor | Meiothermus | MENNEPVVETPEAQNDLPEVERLKGEVEFLKAELEASKNKFLRLYADFENYKKRMVQELEAAQRNGKFDAVRALLGTLDDLERALGFASVKPEDLIPGVRSVLENFTRSLKSLGVEAVPGVGAEFDPRYHEAIGAVEGEEGKVMHVYQQGFKYGDLLVRPARVVVGSGAKPEEAEA | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. | Q8L2F3 |
A5F3E6 | DER_VIBC3 | GTP-binding protein EngA | Vibrio | MVPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGQAKLGEHEFIVIDTGGIDGSEEGVETKMAQQSLAAIDEADVVLFMVDGRAGLTVADEAIAQHLRRIEKPAILVVNKVDGIDADAASAEFWQLGMDQMYQIAAAHGRGVGALIDRVLNPFAEQMESEQAQLEDLTNEEDPEEEQLEYSEEEAEAEYKRLQDLPIKLAIIGRPNVGKSTLTNRILGEERVVVYDMPGTTRDSIYIPMKRDEREYVLIDTAGVRRRKRINETVEKFSVVKTLQAIEDANVVLLVVDARENISDQDLSLLGFALNSGRSIVIAVNKWDGLSFDVKEHVKKELDRRLGFVDFARIHFISALHGTGVGHLFESVQEAYRSATTRVGTSVLTRIMKMATDDHQPPMVRGRRVKLKYAHAGGYNPPIIVIHGNQVNELPDSYKRYLMNYYRKSLEIMGTPIRIQFQNSENPFEGKTNKMTLSQERQRKRLMSMVKNRRK | GTPase that plays an essential role in the late steps of ribosome biogenesis. | A5F3E6 |
Q94JQ6 | CESA6_ARATH | Protein QUILL | Arabidopsis | MNTGGRLIAGSHNRNEFVLINADENARIRSVQELSGQTCQICRDEIELTVDGEPFVACNECAFPVCRPCYEYERREGNQACPQCKTRFKRLKGSPRVEGDEEEDDIDDLDNEFEYGNNGIGFDQVSEGMSISRRNSGFPQSDLDSAPPGSQIPLLTYGDEDVEISSDRHALIVPPSLGGHGNRVHPVSLSDPTVAAHPRPMVPQKDLAVYGYGSVAWKDRMEEWKRKQNEKLQVVRHEGDPDFEDGDDADFPMMDEGRQPLSRKIPIKSSKINPYRMLIVLRLVILGLFFHYRILHPVKDAYALWLISVICEIWFAVSWVLDQFPKWYPIERETYLDRLSLRYEKEGKPSGLSPVDVFVSTVDPLKEPPLITANTVLSILAVDYPVDKVACYVSDDGAAMLTFEALSETAEFARKWVPFCKKYCIEPRAPEWYFCHKMDYLKNKVHPAFVRERRAMKRDYEEFKVKINALVATAQKVPEDGWTMQDGTPWPGNSVRDHPGMIQVFLGSDGVRDVENNELPRLVYVSREKRPGFDHHKKAGAMNSLIRVSGVLSNAPYLLNVDCDHYINNSKALREAMCFMMDPQSGKKICYVQFPQRFDGIDRHDRYSNRNVVFFDINMKGLDGLQGPIYVGTGCVFRRQALYGFDAPKKKKGPRKTCNCWPKWCLLCFGSRKNRKAKTVAADKKKKNREASKQIHALENIEEGRVTKGSNVEQSTEAMQMKLEKKFGQSPVFVASARMENGGMARNASPACLLKEAIQVISCGYEDKTEWGKEIGWIYGSVTEDILTGFKMHSHGWRSVYCTPKLAAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHCPIWYGYGGGLKWLERLSYINSVVYPWTSLPLIVYCSLPAICLLTGKFIVPEISNYASILFMALFSSIAITGILEMQWGKVGIDDWWRNEQFWVIGGVSAHLFALFQGLLKVLAGVDTNFTVTSKAADDGEFSDLYLFKWTSLLIPPMTLLIINVIGVIVGVSDAISNGYDSWGPLFGRLFFALWVIIHLYPFLKGLLGKQDRMPTIIVVWSILLASILTLLWVRVNPFVAKGGPILEICGLDCL | Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the primary cell wall formation. The presence of each protein CESA1 and CESA6 is critical for cell expansion. The hypocotyl elongation is based on a CESA6-dependent cell elongation in dark and a CESA6-independent cell elongation in light. The transition between these two mechanisms requires photosynthesis and PHYB, but not CRY1. The CESA6-dependent cell elongation seems to be independent of gibberellic acid, auxin and ethylene. May be involved in sensitivity to isoxaben. Associates with and moves along cortical microtubules for the process of cellulose deposition. | Q94JQ6 |
Q2W4W1 | ZNUC_MAGSA | Zinc import ATP-binding protein ZnuC | Magnetospirillum | MSLLNLSGVRLSHGGHLVLDRVDLTVDAGRIITVVGPNGAGKSSLLKVALGLLRPDAGTVERGAKVIGYVPQRLDIGRLLPLSVRRFLAMAVAERPPAGRLEETLDLVGAGHVLGRQVVDLSGGEMQRVLLARALLRRPDLLVLDEPVGGVDVAGQAELYDLITGQAREHGVGVLMVSHDLHVVMAATDHVVCLNRHVCCAGHPETVSRHPEYLALFGPRVAASLAIYTHAHDHGHGADGSVLPLAEGGGEPHTHGPGCRHG | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. | Q2W4W1 |
A7HI47 | MURA_ANADF | UDP-N-acetylglucosamine enolpyruvyl transferase | unclassified Anaeromyxobacter | MDKIVIDGGVPLRGSVATSGAKNAALPIIAGALLAEGDHLVRNVPDLADVRTLGRLLVHMGCQAERNAGEKGALWIRVPAAVQPEAPYELVKTMRASVVVLGPLVARWGKARVSLPGGCAIGARPIDQHLKGLSALGAEIRLEHGYVEATAPRGRLRGATFTFDAQTVTGTENVMMAAALAEGETLLRNCAREPEIVDLAAALVRMGARISGAGADEIRIEGVETLRPLDHVVIADRIEAGTFLAAGALPGNDVTVQGCVLEHVEALVEKLRAAGAEVLPVDGGLRVVGDGRPRPVDVRTAPHPGFPTDMQAQMMALLCLADGSSKITETVFENRFMHVQELQRLGAEIAVDGKTAVVKGVPELSGAPVMASDLRASAALVLAGLAAQGTTEVHRVYHLDRGYERIEEKLAPLGARIRREKA | Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. | A7HI47 |
Q55DL0 | DPYS_DICDI | Hydantoinase | Dictyostelium | MLRVDQTGTILIKNGTVVNDDRYFKSDVLVENGIIKEISKNIEPKEGIKVVDATDKLLLPGGIDTHTHFQLPFMGTVSVDDFDIGTQAAVAGGTTFIIDFVIPTRGQSLLEAYDQWKKWADEKVNCDYSLHVAITWWSEQVSREMEILVKERGVNSFKCFMAYKNSFMVTDQEMYHIFKRCKELGAIAQVHAENGDMVFEGQKKMLEMGITGPEGHELSRPEALEAEATNRAIVIADSVCTPVYIVHVQSIGAADVICKHRKEGVRVYGEPIAAGLGVDGSHMWNHDWRHAAAFVMGPPIRPDPRTKGVLMDYLARGDLDCVGTDNCTFCADQKAMGKDDFTKIPNGVNGVEDRMSIVWENGVNTGKLTWCQFVRATSSEAARIFNIYPRKGRIDVGCDGDIVIWDPNQSKTISKDTHHHAVDFNIFEGIKVTGIAVTTIVAGNIVWSDNKLSCVKGSGRFVPRPPFGPVFDGIEQRDKVRNELLRKVDRKPYEDDNTKNSSK | Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate. | Q55DL0 |
Q5QJC9 | BAG5_RAT | Bcl-2-associated athanogene 5 | Rattus | MDMGNQHPSISRLQEIQREVKSIEQQVVGFSGLSDDKNYKRLERILTKQLFEIDSVDTEGKGDIQQARKRAAQDTERLLKELEQNANHPHRIEIKNIFQEAQALVKEKTVPFYSGSNCVTSEFEEAIQDIILRLTHVKTGGKISLRKARYHTLTKICAVQEIIEDCVRKQPSLPLSEDVHPSVAKINSVMCEVNKARGTLIALLMGVDSSETCRHLSCVLSGLMADLDALDVCGRTEIRNYRREVVEDINKLLKYLDLEEEADNTHAFDLGQNHSIIKIENVLKRMREMKNELLQAQSPPELYLRSKTELQGLIGQLDEVSLEKNPCIREARRRAVIEVQTLITYLDLKEALEKRKLFPCEETPPHKAVWNVLGNLSEIQGEVLSFGGNRTDKNYIRLEELLTKQLLTLDAVDPLGEEKCKAARKQAVKLAQNILSYLDMKSDEWEY | May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN. | Q5QJC9 |
Q8X6X7 | NUDC_ECO57 | NADH pyrophosphatase | Escherichia | MDRIIEKLDHGWWVVSHEQKLWLPKGELPYGEAANFDLVGQRALQIGEWQGEPVWLIQQQRRYDMGSVRQVIDLDVGLFQLAGRGVQLAEFYRSHKYCGYCGHEMYPSKTEWAMLCSHCRERYYPQIAPCIIVAIRRDDSILLAQHTRHRNGVHTVLAGFVEVGETLEQAVAREVMEESGIKVKHLRYVTSQPWPFPQSLMTAFMAEYDSGDIVIDPKELLEANWYRYDDLPLLPPPGTVARRLIEDTVAMCRAEYE | mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates. | Q8X6X7 |
Q0BYD8 | RPOA_HYPNA | Transcriptase subunit alpha | Hyphomonas | MTTVNDRNWKVLIRPNRPVVQAGYDAKRKAKLVVEPLERGYGTTLGNALRRVLLSSLQGAAIIGVQIDGVVHEFSAIPGVREDVTTIVLNLKQVAIFMESDTPKRMVLRAKGPGEVKAGQIETPGDVKILNPDLVICTLDGGSEVRMEFTVATGKGYVAAEAHRPEDAPIGYIPIDAIYSPVRRVGYQVEDTREGTVLDYDKLTLDIETDGSLSPEDSVAYAARILQDQLQLFINFEEPTLETGGAADETDLGFNPVLLKKVDELELSVRSANCLKNDNIVYIGDLIQKSEAEMLRTPNFGRKSLNEIKEVLAGMGLHLGMEVPDWPPEDIEGLAKKYDDHI | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q0BYD8 |
Q3K3U8 | KAD_STRA1 | Adenylate monophosphate kinase | Streptococcus | MNLLIMGLPGAGKGTQAAKIVEEFGVAHISTGDMFRAAMANQTEMGRLAKSYIDKGELVPDEVTNGIVKERLAEDDIAEKGFLLDGYPRTIEQAHALDATLEELGLRLDGVINIKVDPSCLIERLSGRIINRKTGETFHKVFNPPVDYKEEDYYQREDDKPETVKRRLDVNIAQGESILEHYRKLGLVTDIEGNQEITEVFADVEKALLELK | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | Q3K3U8 |
A8FRM9 | TRMN6_SHESH | tRNA m6A37 methyltransferase | Shewanella | MAFTFKQFHIDDFGCGMPVSTDAVILGAWAPLSDAQNILDIGAGSGLLSLMATQRSNAKVTSIELDDTAVNACQKNFEASPWTSRLTVKHSSVQEFSKQHQESEESLFDHIICNPPYFKGGTQSQNRLRAQARHTDTLDFCALLEAIGSLLAPNGTASLILPSQSMSEFGLVLADSSLEFSQVTDISDSQRKTPHRHLFTLCHKSTDASAKPNEGATEHFCIKELDGSYTEEMKLLITGFYLKY | Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC). | A8FRM9 |
D1C4U5 | FTSH3_SPHTD | ATP-dependent zinc metalloprotease FtsH 3 | Sphaerobacter | MNPRPVRPGGSLQQSLLALGSLSVAVGLAVWQQRTLGRGRSDSVTAVERPETTFSDVAGLIEAKEELAEIVTFLRDPERFRRMGARMPRGVLLAGPPGTGKTLLARAVAGEAGVPFFAMSASQFVEVYVGVGAKRVRDLFAAARKASPAIVFIDEIDAIGRRRGDSQSHQEYEQTLNQVLVELDGFHPRQAVVVIAATNRSDILDPALLRPGRFDRRVELSLPDRAERAAILRVHAQDKPLAPDVDLDALAARTVGLSGADLENTLNEAALLALRRGGDEITQADLEEAVDRVIAGPSRRSRALSARERETIAVHEAGHALVAHQLASADAPRRVTILGRGQMGGATVLAPDEDRRLWTRGQFLDRLAVLLGGYAAEEYRYGEVTTGSSGDLSQASALAQAMVTTYGMGKSLRGRAFDANGPVSDETSRAIDEEVSALVSEALELASRTIANAAHLLDALVAALLAEETLDEARLAAILGPRPARPAMN | Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. | D1C4U5 |
Q9I273 | SSTT_PSEAE | Na(+)/serine-threonine symporter | Pseudomonas | MTYPERPLLHLLTRTSLVGQIIVGLIAGLLLASFFPAAALKVGFIGKVFVSALKAVAPVLVFVLVMASIANHKQGQQTHIRPILLLYLVGTFSAAVVAVIASFAFPSSLVLASHPGEMSPPGGIAEVLQSLLLSVVDNPVNALISANFIGILAWAIGLGIAFRHASDTTRNLLSELSNGVSLIVKVVIRFAPLGIFGLVASTFAESGVEALKGYAHLLVVLLGCMLFVAFVVNPLIVFLKIRRNPYPLVLTCLRESGMTAFFTRSSAANIPVNLQLCERLGLHEDTYSVSIPLGATINMAGAAITITVLTLAAVHTLGIAVDVPTAILLSVVASICACGASGVAGGSLLLIPLACSLFGIPSEVAMQVVAVGFIIAILQDSAETALNSSTDVLFTAAACEAEERKASAA | Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system). | Q9I273 |
A5V9Q2 | TRMD_RHIWR | tRNA [GM37] methyltransferase | Rhizorhabdus | MTFAATILTLYPEMFPGPLGVSLAGRALAEGKWSCDPVQIRDFATDRHRSVDDTPAGGGAGMVMRADVLARAVDHALETRPDSPLLAMTPRGAPLTQARVRQLAAGPGVTILCGRFEGIDERLFEARPIEPVSIGDYILSGGEMGALVLLDACIRLLPGVMGAPDSGDEESFESGLLEYPHYTRPAEWEGRTIPEVLRSGDHARIEAWRNAMAETDTRLRRPDLWERHEGARAQSPSGARRQKKER | Specifically methylates guanosine-37 in various tRNAs. | A5V9Q2 |
Q52665 | BZTC_RHOCB | Glutamate/glutamine/aspartate/asparagine transport system permease protein BztC | Rhodobacter | MSDTSFVRTEMLAPRPAPVSQVGAIKWMRENLFSGPLNTALTVFGLLATVWLVQAAAPWLLHGVWNANSLTECRAIIAERWGPEATGACWAVIRVRWNQFLFGFYPVDQYWRLFVTFAGLFLALAPVLFDALPRKLIWGTLLYPLAAFWLLWGGPIWGPVSVLAGFAILGLLFTALAPKLGVPVSAGIGLVVAALFWLYAAAPIEAALQSALPLALPEVDSDQFGGFLLALVIGVTAIVVSLPLGILLALGRQSDMLIVKSLSVGIIEFVRGVPLITLLFTASLLLQYFLPPGTNFDLILRVVILVTLFAAAYIAEVIRGGLAALPRGQYEAADALGLDYWQAQRLIIMPQALKISIPGIVSSFIGLFKDTTLVAFVGLFDPLKGISNVVRSDMAWKGTYWEPYIFVALIFFLFNFSMSRYSMYLERKLKRDHR | Part of a binding-protein-dependent transport system for glutamate, glutamine, aspartate and asparagine. Probably responsible for the translocation of the substrate across the membrane. | Q52665 |
Q9ERI2 | RB27A_MOUSE | Ras-related protein Rab-27A | Mus | MSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTVGIDFREKRVVYRANGPDGAVGRGQRIHLQLWDTAGQERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAYCENPDIVLCGNKSDLEDQRAVKEEEARELAEKYGIPYFETSAANGTNISHAIEMLLDLIMKRMERCVDKSWIPEGVVRSNGHTSADQLSEEKEKGLCGC | Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion. Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. | Q9ERI2 |
O29164 | ACDE1_ARCFU | ACDS complex carbon monoxide dehydrogenase subunit epsilon 1 | Archaeoglobus | MMEMAVAKEEKFPTAKRFDIADIQVSREATAVKPKVVANMIKRAKRPLLVTGGQLLKDEKLVEFAVKFAEKGIPIAATAGSSKPLIERGIKPVSKTYTLHQITQFLQDEEFQGFDGNGNYDTVIFLGFLPYYLSRMLSSLKHFSKITTIAIDEFYQPHAKFSFTNLTKDRELYYSMLQEVLDNL | Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation. | O29164 |
Q6GDE0 | CAPA_STAAR | Capsular polysaccharide biosynthesis protein CapA | Staphylococcus | MKEKFDLVKLLNILKKNIKLLLILPAICLVVSAALTFFVMPDKYTASTQILVNMKKSSSDLAFQNVQSSLQSVNTYTEIIKSPRILDKVSREFDGQYSTAELNSFLKVTNQTNSQIITVSVTTGNKSESDKIVNRISKVFAHDMPKIMSVDNVTILSSAHDNAVKVSPIVSVNLVISIIVGIVLAILIIFLKELLDKRIKTEEDVESQLGLPILGSIQKF | Required for the biosynthesis of type 1 capsular polysaccharide. | Q6GDE0 |
P06642 | HBE2_BOVIN | Hemoglobin epsilon-2 chain | Bos | MVHFTTEENVAVASLWAKVNVEVVGGESLARLLIVCPWTQRFFDSFGNLYSESAIMGNPKVKVYGRKVLNSFGNAIKHMDDLKGTFADLSELHCDKLHVDPENFRLLGNMILIVLATHFSKEFTPQMQAAWQKLTNAVANALTHKYH | Hemoglobin epsilon chain is a beta-type chain found in early embryos. | P06642 |
Q9PP04 | AMPA_CAMJE | Leucyl aminopeptidase | Campylobacter | MKFELNDKKLDAIKADFELVFIQDKNLKIFNKEKDFFKLNNYKGEGALLDLNNKKLYLELKSLAYEDIRLSLCTAYKTLEKLNIKSVKLPSIIGDCVVRSFASLVEGVLFGAYKFDKYKSEKKTSTLEKFIISNEELNGKKFNKDEAKIGLERGEILANATNFTKNIVNEIPEIYTPLKMAEDAQNLAKENKNIICKIYDEKFLAKEKMNAFLAVNHASVHPPRLIHLSYKAKNAKKRVVFVGKGLTYDSGGLSLKPADFMLTMKADKSGAAAAMGIIKAVAELALDLEVHCILGATENMIGGNAYKPDDVLISREGVSIEVRNTDAEGRLVLADCLSFAQDLKPDLLIDMATLTGACVVGLGEFTSAIMGNNEELQNDFYLSSKKSGEYTTILHFNPHLRELIKSNIADVSNTASSRYGGAITAGLFLDKFIRKEYKDKWLHLDIAGPAYTEKSWGYSSFGAGGAGVRMCVNYLIQILRKAK | Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. | Q9PP04 |
B1GYL7 | ENO_ENDTX | 2-phosphoglycerate dehydratase | Endomicrobium | MAKIVKIAGREIIDSRGNPTVEVDVRLGDGTLGRAAVPSGASTGSREALELRDGDKKRFGGKGVLKAVSNVNDIIAPKLTGLEITKQQDIDDIMIKLDGTDFKSSLGANAVLGVSLACAKAGSNSNKLPVYEYVREIYNVKSDKYVLPVPLMNIINGGEHADNNVDLQEFMIAPVSAPTFREALRMGCEVFHGLKKVLNEKGYATGVGDEGGFAPNLKSNAQALEVICEAVKVAGYEVGRDIVFALDVAASELYENNKYTLEGEVKEKVKTSKDMIAFYGDLLKEYPIISIEDGLSESDWDGWKILTEKLKSRLQLVGDDLFVTNTKIFKDGIDKGIANSILIKVNQIGSLSETVAAVQMAYKAGYTAVMSHRSGETEDSIIADLAVALNTGQIKTGSASRTDRMCKYNQLLRIEEELGSKSAYLGKSAFSSIK | Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. | B1GYL7 |
K4CJJ1 | NCED2_SOLLC | Nine-cis-epoxycarotenoid dioxygenase 2 | Solanum subgen. Lycopersicon | MTSTIANYRVSHSFSPSTSYSLDFTLPSKSISMKNHTTTKTKIHSALLTLPKQNNTPKNQPQFQTSHWNFFQKAAAKALDIVESALVSRELQNPLPKTADPRVQIAGNFAPVPEQSVRHNLPVTGTIPDCINGVYVRNGANPLFEPVAGHHLFDGDGMVHAVTVENGSVSYSCRFTETERLVQERELGHPVFPKAIGELHGHSGIARLLLFYARGVFGLVDHSHGTGVANAGLVFFNNRLLAMSEDDVPYHVQVLPSGDLQTVGRYNFDDQLKSTMIAHPKIDPVSGELFALSYDVVQKPYLKSFKFSPDGEKSPDVEIPLDVPTMMHDFAITENYVVIPDQQVVFKLQEMIKGGSPVIYDKNKKSRFGILPKNAENSENIIWVESAETFCFHLWNAWEEPETDEVIVIGSCMTPPDSIFNECNENLKSVLSEIRLNLKTGESTRRQLLSPSDQVNLEAGMVNRNKLGRKTQFAYLAIAEPWPKVSGFAKVDLSTGEIKKHIYGDKRYGGEPLFLPRNVNSEKEDDGYILAFCHDEKTWKSELQIVNAMTLELEATVKLPSRVPYGFHGTFISSKDLQNQV | Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid (ABA) biosynthesis from carotenoids. | K4CJJ1 |
Q2T1P5 | ACEK_BURTA | Isocitrate dehydrogenase kinase/phosphatase | pseudomallei group | MNHFPKLLSSQIGFDVAQTILENFDRHYRIFREAAVEAKDLFERSDWHGLQRLARERITSYDDRVRECVELLEDEYDAENIDHDVWPQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRAYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGSEGLAATLERIVTNFQLNPPFEDLERDIACIMQAIHDEFGAFDEAVNFQIHVLSSLFYRNKTAYIVGRIINGDRVLPFAVPIRHARAGVLALDTVLLRRDQLKIIFSFSHSYFLVDMNVPSAYVQFLRSIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKMIKDHFPPPKETTREQIMDKYLLVKRHDRLGRMADTLEYSSVALPLARLDDALVRELEKEVPSLIEYEGDSLVIKHLYIERRMVPLNLYLQNGSDAEIEHGVREYGNAVKELIQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNDEDEMSGEPWYTVGPHDIFPETYAPFLLGDPRVREHFLAHHADFFDPQLWQDSKDRLLRGELPDFFAYEPALRFCLRYPERFAPGDAAEDGKRAAA | Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Q2T1P5 |
Q9SNC6 | PUB13_ARATH | RING-type E3 ubiquitin transferase PUB13 | Arabidopsis | MEEEKASAAQSLIDVVNEIAAISDYRITVKKLCYNLARRLKLLVPMFEEIRESNEPISEDTLKTLMNLKEAMCSAKDYLKFCSQGSKIYLVMEREQVTSKLMEVSVKLEQSLSQIPYEELDISDEVREQVELVLSQFRRAKGRVDVSDDELYEDLQSLCNKSSDVDAYQPVLERVAKKLHLMEIPDLAQESVALHEMVASSGGDVGENIEEMAMVLKMIKDFVQTEDDNGEEQKVGVNSRSNGQTSTAASQKIPVIPDDFRCPISLEMMRDPVIVSSGQTYERTCIEKWIEGGHSTCPKTQQALTSTTLTPNYVLRSLIAQWCEANDIEPPKPPSSLRPRKVSSFSSPAEANKIEDLMWRLAYGNPEDQRSAAGEIRLLAKRNADNRVAIAEAGAIPLLVGLLSTPDSRIQEHSVTALLNLSICENNKGAIVSAGAIPGIVQVLKKGSMEARENAAATLFSLSVIDENKVTIGALGAIPPLVVLLNEGTQRGKKDAATALFNLCIYQGNKGKAIRAGVIPTLTRLLTEPGSGMVDEALAILAILSSHPEGKAIIGSSDAVPSLVEFIRTGSPRNRENAAAVLVHLCSGDPQHLVEAQKLGLMGPLIDLAGNGTDRGKRKAAQLLERISRLAEQQKETAVSQPEEEAEPTHPESTTEAADT | Functions as an E3 ubiquitin ligase. | Q9SNC6 |
Q48L73 | MINC_PSE14 | Probable septum site-determining protein MinC | Pseudomonas | MSQIESQNPEPVFQLKGSMLAITVMELARTNLEALDRQLAAKVAQAPNFFSNTPLILALDKLAPNEGPVDLPGLVRICRQHGLRTLAIRANRIEDIAAAIAVDLPVLPPSGARERVIDPIEVEAPKKIPEKPPEPLIKPTRVITAPVRGGQQIYAQGGDLVVVAPVSPGAELLADGNIHVYGPMRGRALAGIKGDTKARIFCQQLSAELISIAGQYKVSEDLRRDPLWGSPVQVSLSGDVLNIIRL | Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. | Q48L73 |
Q12ZU6 | RL22_METBU | 50S ribosomal protein L22 | Methanococcoides | MARIKYTTELDAETSAKAMGSELHISPKKSRELCKAIKGMRTNAARQYLEDVVILKQAVPFGRHNDSLGHRKGPMAAGRYPVKVASEMLKLLKNAESNAEYKGLNPEHMFIAHTAMNRGRVIHGMRPRARGRASPENTETVNLEMIISEVR | The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | Q12ZU6 |
B3DRN8 | PAFA_BIFLD | Pup-conjugating enzyme | Bifidobacterium | MPQLRDSGTRSLHATEPVPSAEMDGFCRIFGVETEYGVAVTGAERPVDAGQVAMTMFQPIVSRSRSTNTYLTNGSRLYLDVGSHPEYATAEARDPREALAQDLAGEHVMRNLALKAQRKLRESYGAHATIHVFKNNVDSAGHAFGCHENYLVRRFVPLETIEHQLLPFLITRQLYTGAGRMTPDGFQITQRADFLDEAVSSATTRSRPMVNTRDEPHADPDSFRRLHVIIGDSNRSQWSTWMKLAVTHLVLCAIEDAFRHGTPSGFEHCAFADPAAANRTVSRFLDDPHAELTLESGESVSALGLQRRYYAAVKAFIETHVDALASSLPATTIDTIMGEWSRVLDALERGAYDALADRVDWAAKKRLFDALKRRRPDVTFAQMEQLELDYHDIANGRLYGSLVARNQMRELLTGDNVEYAVHNPPTDTRAALRGRFVDAALNVGAQFSADWTHLTLTAPERREAILLDPFEAEPTLGFEQLMEALN | Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine. | B3DRN8 |
Q489T8 | RL9_COLP3 | 50S ribosomal protein L9 | Colwellia | MEVILLDKIAKLGGLGDKVSVKSGYARNYLLPQGKAVFASEANVEHFEARRADIEAKLADVLATAEARAAKVVALAEVTIASKSGDEGKLFGSIGTRDIADAITEAGVEITKAEVRLPLGAIRETGEFEIAIHLHHDVDTSIKVVVIAEA | Binds to the 23S rRNA. | Q489T8 |
Q6B8U6 | PSAA_GRATL | PsaA | Agarophyton tenuistipitatum | MTISSQEQETKKVQVTVDKNPVATSFEKWAKPGHFSRTLAKGPKTTTWIWNLHADAHDFDSHTSSLEEVSRKIFSAHFGQLAIIFLWLSGMYFHGAKFSNYIAWLSNPTAIKPSAQIVWPIVGQEILNGDVGGGFQGVQITSGFFQIWRASGITTEFELYATAIGGLFMACLMLFAGWFHYHKAAPKLEWFQNVESMMNHHLAGLLGLGCLGWAGHQIHISIPINKLLDSGVSPQELPLPHEFLVNRELVSQLYPSFSKGIIPFFTLNWNEYSDFLTFKGGLNPITGGLWLTDTAHHHLALAVLFLVAGHMYRTNWGIGHSMKEILEAHKGPFTGEGHKGIYEILTTSWHAQLAINLAMMGSLSIIVAHHMYAMPPYPYIATDYPTQLSLFTHHMWIGGFCIVGAGAHASIFMVRDYNPAQNYNNVLDRVIRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMRALGRSQDMFSDTAIQLQPIFAQWIQNIHSLAPSNTSPNALATASYAFGGDVIAVNNKIAMMPINLGTADFMVHHIHAFTIHVTVLILVKGFLFSRNSRLIPDKSSLGFRFPCDGPGRGGTCQVSGWDHVFLGLFWMYNSLSIAIFHFSWKMQSDVWGSVTPAGTVSHITGGNFAQSAITINGWLRDFLWAQASQVIQSYGSALSAYGLIFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKVKVAPSIQPRALSITQGRAVGVAHYLLGGIGTTWAFFLARIISVG | PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6. | Q6B8U6 |
Q8XCJ6 | G6PD_ECO57 | Glucose-6-phosphate 1-dehydrogenase | Escherichia | MAVTQTAQVCDLVIFGAKGDLARRKLLPSLYQLEKAGQLNPDTRIIGVGRADWDKAAYTKVVREALETFMKETIDEGLWDTLSARLDFCNLDVNDTAAFSRLGAMLDQKNRITINYFAMPPSTFGAICKGLGEAKLNAKPARVVMEKPLGTSLATSQEINDQVGEYFEECQVYRIDHYLGKETVLNLLALRFANSLFVNNWDNRTIDHVEITVAEEVGIEGRWGYFDKAGQMRDMIQNHLLQILCMIAMSPPSDLSADSIRDEKVKVLKSLRRIDRSNVREKTVRGQYTAGFAQGKKVPGYLEEEGANKSSNTETFVAIRVDIDNWRWAGVPFYLRTGKRLPTKCSEVVVYFKTPELNLFKESWQDLPQNKLTIRLQPDEGVDIQVLNKVPGLDHKHNLQITKLDLSYSETFNQTHLADAYERLLLETMRGIQALFVRRDEVEEAWKWVDSITEAWAMDNDAPKPYQAGTWGPVASVAMITRDGRSWNEFE | Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone. | Q8XCJ6 |
B9M6F7 | KAD_GEODF | Adenylate monophosphate kinase | Geotalea | MNLILLGPPGAGKGTQAKLLIKKYRIPQISTGDILRAAVKDMTPMGGKAKSFMDAGALVPDEVVVGIIQERLNLADCSNGFILDGFPRTVAQADALAKVLSGLGRSIDHVISIVVDNEELLERVTGRRTCRNCGKGFHVSFDPPKSSGICDECSGELYQRDDDREDTMRKRLEVYWQQTSPLVEYYKNKSLLRSVEGVGSMEEIQQKIVSILQG | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | B9M6F7 |
Q7VHX2 | TGT_HELHP | tRNA-guanine transglycosylase | Helicobacter | MQVTLQAQDGGARALSLKLAHSEVQTPVFMPVGTQGCVKALDSRDMSEILNAQIILVNTYHMYLRIGIERLKNFGGIARFAHFDRSYLSDSGGFQAFSLNKNAKVTNEGVAFKSHIDGSKHFFSPEYVLDIQYALNSDIMMVLDDLVGLPSSEERIADSIARTSDWAQKSLIYHQSQKARGLGLNNNLFAIIQGGVNEHFRTLCAKQLVDMGDFDGFAIGGLAVGETSEQMYKTISFTTPLMPVNKPRYLMGVGTPENIIESIALGVDMFDCVMPTRNARNATLFTHFGKINIKAAIFSNDQSPIDELCDCYTCQHFTRAYLCHLFRSQEMTYYRLASLHNLHYYLNLMREAREAILQGTFSAYRSSFYALREMEIPNNEY | Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). | Q7VHX2 |
Q6C101 | CD123_YARLI | Cell division cycle protein 123 | Yarrowia | MIINDKKDQETKVDDTTTLTLTREHLLNCQFSAWYKLYKSITPKTRIIKPLPEDFVNYLSEDGVILPDEEKTSYGSDSGVFEEYSDDEDELDSYVSKLDDFHPKVQAVIDEFGAVAPKLNWSSPQDAIWISPSNSTRCVTVNDVYLLLKSSDYIAHDLTMLDKLGGIPKDFSFELVLRKWININPALEFRCFVKDRELIAVTQRDQNYYEFLIKLKERFLGEIELFFYEHIKDTFPDSSFVFDVYIPEPYDKVWLMDFNVFYPTTDSLIEWSTLVNLDATSPSFDLDLLLIDKELRNASFACQRHSQNKVPMDIVNASMDTEAMVEMLRSQQREMDRLDGDQGGEASATGDTTGDSVANETTAANTTSQDS | Regulates the cell cycle in a nutrient dependent manner. | Q6C101 |
Q485R8 | PY2CR_COLP3 | Proline ketimine reductase | Colwellia | MKIISAEQVHQNLNFEELIPLLKQSFSRPFSMPQRQVYSLAPEQSENHDAFALLPSWNEEVIGNKAFTYFPDNAKKHDLPGLFSKIMLFKRQTGEPLALVDGTSVTYWRTAAISALASQLLSRKNSQHLMLFGTGNLASYLVKAHLTVRDIKQVTLWGRNAKKVSKLIADFSILYPAVTFKTSVDVNAEVASADIICCATGAKTPLFDGNSVSAGCHIDCLGNHMTDARECDTTTILRARVFVDSLTNTLNEAGELLIPMAEDAFNKDEIVGELADMCKTPSMLRQSSDEITLFKSVGTAISDLVAAHSVVEKLAD | Catalyzes the reduction of Delta(1)-pyrroline-2-carboxylate (Pyr2C) to L-proline, using preferentially NADPH over NADH as the electron donor. Together with LhpH, is involved in a metabolic pathway that converts trans-3-hydroxy-L-proline (t3LHyp) to L-proline. To a much lesser extent, can also reduce Delta(1)-piperideine-2-carboxylate (Pip2C) to L-pipecolate in vitro; however, this activity has likely no physiological significance in vivo since C.psychrerythraea probably possesses no ability to metabolize D-lysine via the L-pipecolate pathway. Does not show ornithine cyclodeaminase (OCD) activity. | Q485R8 |
B8CXL9 | RS20_HALOH | 30S ribosomal protein S20 | Halothermothrix | MPIIKSAKKRVRITEKRTAYNREWKEKIKQAIKEFEKVVEEGNVEEAEAKLREASKILDKSAGKGIIHKNKAARKKSQLTRQFNKIA | Binds directly to 16S ribosomal RNA. | B8CXL9 |
Q9V675 | CP6G2_DROME | CYPVIG2 | Sophophora | MELVLLILVASLIGIAFLALQQHYSYWRRMGVREIRPKWIVGNLMGLLNMRMSPAEFISQLYNHPDAENEPFVGIHVFHKPALLLRDPEMVRNILVKDFAGFSNRYSSSDPKGDPLGSQNIFFLKNPAWKEVRLKLSPFFTGNRLKQMFPLIEEVGASLDAHLRQQPLHNERMRCFDLEAKELCALYTTDVIATVAYGVSANSFTDPKCEFRRHGRSVFEFNLLRAAEFTLVFFLPHLVPFVRFKVVPAEATRFLRKTINYVMSEREKSGQKRNDLIDILIEFRRSTQLAKASGIKDQFVFEGDILVAQAVLFFTAGFESSSSTMAFAMYELAKDTDVQQRLREEIKDALVESGGQVTLKMIESLEFMQMILLEVLRMYPPLPFLDRECTSGRDYSLAPFHKKFVVPKGMPVYIPCYALHMDPQYFPQPRKFLPERFSPENRKLHTPYTYMPFGLGPHGCIGERFGYLQAKVGLVNLLRNHMITTSERTPHRMQLDPKAIITQAKGGIHLRLVRDALGV | May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. | Q9V675 |
A7F8R0 | NAGS_SCLS1 | N-acetylglutamate synthase | Sclerotinia | MPLSLSSRVREELAKETCEKLSTQHQAKKKAKAIDRDFFLSVLGSSATKREARSYIQNFKPPNTAPTKSKIQESTQQNSTENGANLGSIYTATRAVAESPKFVQQPVLPKPAPEGPLLHVALVKIRAPQLLDDETLSGIGKTLSRLSRLGLVSTVVVDGDDGSDTFLRISNCEWRNMVKEQAARVVAAIDASGTEARLVDNVIGIAEDGSNFEQRPYLKGRVHVTLRELLMTPLRRGVLPIIPSIGHTDITQTVVSATANDVVLALTREFAGIWSSESPDEHPNVVKERLQALRSEVSLDRLILVDPLGGIPASDRKNGYHVFLNMEQEYELAKQDLINRGGMHSVAPQKPTLPEASANFTVGDPILLSSFTENKPGELDDSPPPQNGSPAKHDPRMKFHLENLELVRSTLSLLPPSSSALITTPHEAANSEKQPEFKAAGVGTRRQRNPLIHNLLTDKPAFSSSLPVGRLGPMDKNEPISSSTKFAPTTFAKHGMPVTIFPDPKTTPWQPPIAGVPQISLTDPQIDLPRLVHLIEDSFNKKLDVQHYLRRVNNRIAGVIIAGEYEGGALLTWELPPGVPDGSEESRKRMVPYLDKFAVLKKSQGSGGVADVVFKSMVRDCFPGGDNPVNKWYFERSRATLKLSDTNWTMFFTTPEENMDHQTFKDYEAVCKFFGRENVGGYYQQGKRGIYVLDSE | N-acetylglutamate synthase involved in arginine biosynthesis. | A7F8R0 |
Q988B9 | PDLA_RHILO | 4-pyridoxolactonase | Mesorhizobium | MSDTKVYLLDGGSLVLDGYHVFWNRGPGGEVRFPVYSILIEHAEGRFLIDTGYDYDHVMKVLPFEKPIQEKHQTIPGALGLLGLEPRDIDVVVNSHFHFDHCGGNKYFPHAKKICHRSEVPQACNPQPFEHLGYSDLSFSAEAAEARGATAQLLEGTTRANSTFEGIDGDVDLARGVKLISTPGHSIGHYSLLVEFPRRKPILFTIDAAYTQKSLETLCQAAFHIDPVAGVNSMRKVKKLAEDHGAELMYSHDMDNFKTYRTGTQFYG | Involved in the degradation of pyridoxine or pyridoxamine (free, phosphate-unbound, forms of vitamin B6). Hydrolyzes 4-pyridoxolactone to 4-pyridoxic acid. Has lower activity toward N-hexanoyl-D,L-homoserine lactone, but is not active toward 5-pyridoxolactone and gamma-butyrolactone. | Q988B9 |
O93426 | SLA_CRODU | Snaclec convulxin subunit alpha | Crotalus | MGRFIFVSFGLLVLFLSLSGTGAGLHCPSDWYYYDQHCYRIFNEEMNWEDAEWFCTKQAKGAHLVSIKSAKEADFVAWMVTQNIEESFSHVSIGLRVQNKEKQCSTKWSDGSSVSYDNLLDLYITKCSLLKKETGFRKWFVASCIGKIPFVCKFPPQC | Snake venom lectin that activates platelets by binding to the platelet collagen receptor glycoprotein VI (GP6) . The indirect activation of integrin alpha-IIb/beta-3 (ITGA2B/ITGB3) also induced by the toxin is upstream the cytoskeletal translocation of GPIb, FcRgamma (FCER1G) and 14-3-3zeta (YWHAZ). | O93426 |
P17752 | TPH1_HUMAN | Tryptophan 5-monooxygenase 1 | Homo | MIEDNKENKDHSLERGRASLIFSLKNEVGGLIKALKIFQEKHVNLLHIESRKSKRRNSEFEIFVDCDINREQLNDIFHLLKSHTNVLSVNLPDNFTLKEDGMETVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKTWGTVFQELNKLYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTIKRPFGVKYNPYTRSIQILKDTKSITSAMNELQHDLDVVSDALAKVSRKPSI | Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis. | P17752 |
Q5FUE6 | PXPA_GLUOX | 5-oxoprolinase (ATP-hydrolyzing) subunit A | Gluconobacter | MTAKTIDLNADLGESFGHYTMGNDSAMLDIVTSANVACGFHGGDPEVMAETFRIAREKGVSVGSHPGFPDLWGFGRRVMPFTPAQIERIVAYQIGAAQALATYSGHRMTYMKTHGALGNLTERDPAVAEAIVNAVKAVDANLPIMAIALSHLERIGRERGLTVFSEIFADRAYTEDGHLVSRKEPGAVLHDADFAAARAVRMVQNGAIETISGKMLPTRIDTICVHGDNAESVEVARKVRAGFEAAGIAVRALT | Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. | Q5FUE6 |
Q3AF82 | REX_CARHZ | Redox-sensing transcriptional repressor Rex | Carboxydothermus | MKGFKIPEATISRLSVYSRYLENLYRKGITTVSSADIAQGVGVTSAQVRKDLAYFGEFGTRGVGYNVKELLDHTLKILGLNNTWNMVVVGAGNLGSALCAYRGFRERGFYIVGVFDNDLTKIGKKINEYEVLPIDKLEEVVRENNVEIGIIAVPAAYAQDVATRLVKAGVKGILNFAPTVLNVPDKVIVRSVDLTVNLEVLTFNIRRD | Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. | Q3AF82 |
B4KCL9 | ENOPH_DROMO | 2,3-diketo-5-methylthio-1-phosphopentane phosphatase | Drosophila | MALTDLSAKVVLVDIEGTTTSITFVHDVLFPYAKANAGQYLSETWETDDTKQIVEELTQLPQYTEYASTLETRPEINAAHIADFSRYLIEKDLKVTPLKTLQGHIWAKGYASGELKGHVYEDVAVAFQAWSDAGLRIAVYSSGSVAAQKLIFQHSIAGDLLPLLSAHFDTNVGHKQQTESYTRIAESLGVEPQHVLFLTDVPEEASAARDAGMQTVLLARPGNAPLTAEHTSAFPVVANFVALQSLKQP | Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). | B4KCL9 |
Q1CSB9 | RL19_HELPH | 50S ribosomal protein L19 | Helicobacter | MKNRYIQQFEDAQLKDKTMPAFKAGDTLRLGITIKEGEKTRTQYFEGVCIAIRGNGVDKTFCVRKIGANNIGVEKIFPFYSESLASVEVLRVGRVRRAKLYYLRDRRGKAARIKEVRH | This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. | Q1CSB9 |
Q8LGA1 | CCD41_ARATH | G1/S-specific cyclin-D4-1 | Arabidopsis | MAEENLELSLLCTESNVDDEGMIVDETPIEISIPQMGFSQSESEEIIMEMVEKEKQHLPSDDYIKRLRSGDLDLNVGRRDALNWIWKACEVHQFGPLCFCLAMNYLDRFLSVHDLPSGKGWILQLLAVACLSLAAKIEETEVPMLIDLQVGDPQFVFEAKSVQRMELLVLNKLKWRLRAITPCSYIRYFLRKMSKCDQEPSNTLISRSLQVIASTTKGIDFLEFRPSEVAAAVALSVSGELQRVHFDNSSFSPLFSLLQKERVKKIGEMIESDGSDLCSQTPNGVLEVSACCFSFKTHDSSSSYTHLS | May activate cell cycle in the root apical meristem (RAM) and promote embryonic root (radicle) protrusion. | Q8LGA1 |
Q8D2N4 | TYSY_WIGBR | Thymidylate synthase | Wigglesworthia | MKEYLDLLNLILKNGYPKIDRTKTGTLSMFGYQIRINLNEGFPLLTTKYCHFKSIVYELLWFLRGDTNISFLKKNNISIWNKWADKNGNLGPIYGKQWRAWEDKKNNTIDQIEIALNKLKKEPSSRRILVSSWNVGELDLMSIPPCHVLFQLYVINNKLSCQVYQRSCDIFLGLPFNIGSYALLTHIFANQCDLLVEDLIWTGGDIHLYKNHLNQAKLQLTRSPLPLPKIFIKKKPKNLFNYAFNDFLLIDYNHHPKIKAPISI | Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. | Q8D2N4 |
C3MEK8 | LSPA_SINFN | Signal peptidase II | Sinorhizobium | MSERNTLFSRPLPIALFILVALVADQAIKYLVEAFLPFQEAVPVVPMLALYRTYNYGVAFSMLSGMEGWFIVGMRLAVVAFVLWLWRRTPKDRFFAHLGYAMIIAGALGNLVDRLLFGYVIDYILFHTATWSFAVFNLADSFITVGAGAIILDELLQTKKTRSLKL | This protein specifically catalyzes the removal of signal peptides from prolipoproteins. | C3MEK8 |
P86043 | PA21B_STRCA | Phosphatidylcholine 2-acylhydrolase 1B | Struthio | AVWQFREMIKCTIPPSDDLLDF | PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | P86043 |
Q9RJ47 | MOAA_STRCO | Molybdenum cofactor biosynthesis protein A | Streptomyces albidoflavus group | MLRRSASREGAHVLIDTYGRVATDLRVSLTDRCNLRCTYCMPEEGLQWLAKPDLLTDDEIVRLIDIAVTSLGIEEVRFTGGEPLLRPGLVGIVERVAALEPRPQMSLTTNGIGLRRTATALKAAGLDRVNVSLDTLRPDVFKTLTRRDRHKDVLEGLAAAREAGLTPVKVNSVLMPGLNDDEAPDLLAWAVEHDYELRFIEQMPLDAQHGWKREGMVTAGDILTSLRTRFELTAEGSEERGSAPAERWLVDGGPHRVGVIASVTRPFCSACDRTRLTADGQVRTCLFATEETDLRAALRSDAPDEEIARIWRLAMWGKKAGAGLDDPTFVQPDRPMSAIGG | Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate. | Q9RJ47 |
Q2LVE4 | LPXC_SYNAS | UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase | Syntrophus | MYFQRTLKSDLSCQSVGLHSGRKVNMRIRPASSDEGIILVRTDTRYRQMIRVCLENVTDTTLATTIGSSGAAISTVEHILSALSGMGVDNAIIEVDAPEIPIMDGSALPFVNMLKLVGIRTQEKLKKYLVVKKPVSVSEGESFAMLAPSSSFEITYKIEFDHPLIKEQSYHLKLSDETYEKEICSSRTFGFLKDVEYLQAKGLALGGSLKNAVILDEKRIINKEGLRSHNEFVKHKILDAIGDLSLIGMPIVGHFIAYKSGHKLNSMLVKALLEQQENWTTASFLNCQDAHGQNTREKFSIRDIPARKILGAIHA | Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. | Q2LVE4 |
B9IY25 | NAMA_BACCQ | NADPH dehydrogenase | Bacillus cereus group | MNYKLFSPYTIKDVTLKNRIVMSPMCMYSSKNEDGQITNFHLIHYGTRAAGQVGLVMIEATAVLPEGRISNKDLGIWDDSLIEGLHKATTFIHDNGAKAAIQLAHAGRKAELETDALAPSAIPFNETMKMPIEMSKHQIKDTVLAFQQAAVRSKQAGFDVIEIHGAHGYLINEFLSPLTNKRTDEYGGSPENRYRFLREIIESINEVWNGPLFVRISANDYHPDGLTVQDYVQYTKWMKEQGVDLIDCSSGAVVPARIDVYPGYQVQYAKHIKEHANIATGAVGLITTGAQAEQILNNNEADLIFIGRELLRNPYFPRIAANELGFELEEPYQYERAPGKISTNK | Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes. | B9IY25 |
A6UZF6 | COQ7_PSEA7 | 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase | Pseudomonas | MSADRHYSPIDRFLLQADSALRTLLPFSGQPARPSPAIVEPDGELSEEDTRHIAGLMRINHTGEVCAQALYQGQSLTARLPEVREAMEEAAEEEIDHLAWCEQRIRQLGSRPSVLNPIFYGLSFGVGAAAGLVSDRVSLGFVAATEDQVCKHLDEHLAQIPQEDRKSRAILEQMRVDEEQHSSNALAAGGLRFPAPVKLGMSLLAKVMTKSTYRI | Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis. | A6UZF6 |
Q726Y4 | CHED_DESVH | Probable chemoreceptor glutamine deamidase CheD | Desulfovibrio | MRDAVRAKTNRRSVAGMPAELMDLDLRHLHLRIGEGILAARPALIATVLGSCVSVTFHHPSTETGGIFHAMLPTVLGAADGARTPCKYVDAAIETLLGQFARRGIAANDLVVKLFGGAFTMNPEEKQRLRCIVDVGGRNVEVARATLQRFGIEPQSEHILGDRGRKLFFHSGTGEVWVRLLRRTEPPLPSALVCRDDLT | Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis. | Q726Y4 |
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