ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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O14793 | MQKLQLCVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACTWRQNTKSSRIEAIKIQILSKLRLETAPNISKDVIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVETPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQK... | Function: Acts specifically as a negative regulator of skeletal muscle growth.
PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a late... |
P37020 | MPTTYVPINQPIGDGEDVIDTNRFTNIPETQNFDQFVTIDKIAEENRPLSVDSDREFLNSKYRHYREVIWDRAKTFITLSSTAIVIGCIAGFLQVFTETLVNWKTGHCQRNWLLNKSFCCNGVVNEVTSTSNLLLKRQEFECEAQGLWIAWKGHVSPFIIFMLLSVLFALISTLLVKYVAPMATGSGISEIKVWVSGFEYNKEFLGFLTLVIKSVALPLAISSGLSVGKEGPSVHYATCCGYLLTKWLLRDTLTYSSQYEYITAASGAGVAVAFGAPIGGVLFGLEEIASANRFNSSTLWKSYYVALVAITTLKYIDPFR... | Function: Anion/proton exchange transporter involved in iron and copper cation homeostasis. Involved in intracellular iron metabolism during growth on fermentable and non fermentable carbon sources. Required for proper copper-loading and maturation of multicopper oxidase FET3. Important for adjusting intracellular comp... |
Q93LK9 | MKPYGKIPDNSIKSLQDLMQLLKKSKDFITLEIASNNSSIVISYFRTLIDVNIFHEEVLTYIKEKSFNSLQDIHSVLPFENSKITNQIEDIQDSILNGYILIQYDTDKLNCLLVNVSKKEKRDITKAEIEYNIVGPQIAFVEDLDVNLNLVRRKLPTPYLQMKELKVGSLSNTTVAIVFIEGIVNDQNLQEIIKRVSQIKTDHVLDSTYLMQLIADNPNSIFPQFLNTERPDRVAAVLAEGKIALFVDGSPYAITLPTTLIDFFSTTEDYTMPWIIASFFRLLRLFAFIFSVLTTPLYVSILTYHYELIPKELLETLIIS... | Function: Required for the germination response to inosine. Has no role in L-alanine germination.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56786
Sequence Length: 499
Subcellular Location: Membrane
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Q93LK8 | MKQIPIEYQVSPYMVFFLIITIQMGVGMLGFERISAKLVGNDAWISTLLFGISVNVMIWIIYQILNQGNGDIIAINQNVLGKWIGGLLNFIFLSYIVLLGATTLHTYIEVVHVWMFPSISSWVIAGAFLGLCYYIVTGGFRVVAGIGFFGIVIPSILIFTFFYPLQYADFRNLFPIAQHSFLEIMKGMKGNMFSFFGFEMLLLYYPFIKKARTSQKYAHYANLVTTIVYTYLMILTLAFFSEKQLANAIWAYLSMIKIIQFPFIERFEYIIVSVWAFFILPNVSFTLWGVSRGIKEALGIKQKYVLPVIILFIFILSFFL... | Function: Required for the germination response to inosine. Has no role in L-alanine germination.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41556
Sequence Length: 360
Subcellular Location: Membrane
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Q93LK7 | MKRWILFLILSVFLIGCAKTKIVDDIDLVQVAAYDTEAEGKLKGTFAISAYKGGGEGETKIYSASGQTGREVLARASEKSSGPLELGQLRVIIFNEKIIEKGMQEILETLNRNPSVGNAIYLAITNVKGESLLKGNYSKEKEIASYLSSLLEQNMNNGTQPKTNFFMFLNQLDDDARDSYLPMISKKGNVLELNGIALFKRCKMVDKVNPKDLFVFKLLTDNFKQGTYQFKLPGSSNTYATIENIKARTKYKMEGNSKHPFVNAHIQVKAEIQEFTKTKNLDNPKEIKKLEKIMGKEIEKKATTLIKRFIKKDTDPIGLR... | Function: Required for the germination response to inosine. Has no role in L-alanine germination.
Location Topology: Lipid-anchor
Sequence Mass (Da): 40665
Sequence Length: 359
Subcellular Location: Membrane
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P39620 | MKPKKNQYQQMQAFDNMQGYQPQFGANPYPQQGQGSQMQTMGMQPMMPMQQGQQGQQGQQGFGFPGQQQGGGFQIPSGPTPSGPGQSVPGMLPVEESYIENILRLNRGKTATIYMTFENSKEWGSKIFRGVIEAAGRDHIIISDPKSGTRYLLLTIYLDYITFDEEIAYTYPYSMASYSPR | Function: Essential for the localization of CwlJ in the spore coat and for spore germination triggered by calcium and dipicolinic acid (DPA). Its assembly into the spore coat is dependent on the coat morphogenetic proteins CotE and SpoIVA.
PTM: Three N-terminal lysines form epsilon-(gamma-glutamyl)lysine isopeptide bon... |
Q8GUE4 | MALQMIAPFLSSFLPNPRHSLAAHGLTHQKCVSKHISCSTTTPTYSTTVPRRSGNYKPSIWDYDFVQSLGSGYKVEAHGTRVKKLKEVVKHLLKETDSSLAQIELIDKLRRLGLRWLFKNEIKQVLYTISSDNTSIEMRKDLHAVSTRFRLLRQHGYKVSTDVFNDFKDEKGCFKPSLSMDIKGMLSLYEASHLAFQGETVLDEARAFVSTHLMDIKENIDPILHKKVEHALDMPLHWRLEKLEARWYMDIYMREEGMNSSLLELAMLHFNIVQTTFQTNLKSLSRWWKDLGLGEQLSFTRDRLVECFFWAAAMTPEPQF... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Monoterpene synthase that catalyzes the formation of geraniol from geranyl diphosphate.
Catalytic Activity: (2E)-geranyl diphosphate + H2O = (2E)-geraniol + diphosphate
Sequence Mass (Da): 69081
Sequence Length: 603
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXX... |
Q6USK1 | MSCARITVTLPYRSAKTSIQRGITHYPALIRPRFSACTPLASAMPLSSTPLINGDNSQRKNTRQHMEESSSKRREYLLEETTRKLQRNDTESVEKLKLIDNIQQLGIGYYFEDAINAVLRSPFSTGEEDLFTAALRFRLLRHNGIEISPEIFLKFKDERGKFDESDTLGLLSLYEASNLGVAGEEILEEAMEFAEARLRRSLSEPAAPLHGEVAQALDVPRHLRMARLEARRFIEQYGKQSDHDGDLLELAILDYNQVQAQHQSELTEIIRWWKELGLVDKLSFGRDRPLECFLWTVGLLPEPKYSSVRIELAKAISILL... | Cofactor: Binds 3 Mn(2+) ions per subunit.
Function: Monoterpene synthase that catalyzes the formation of geraniol from geranyl diphosphate.
Catalytic Activity: (2E)-geranyl diphosphate + H2O = (2E)-geraniol + diphosphate
Sequence Mass (Da): 64933
Sequence Length: 567
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif... |
E8W6C7 | MTSQASAPKIPQLWVPLPSGIHPSWREIDQGSAAWLDRFGLYSDHAQRERLTRISVGEITGRGGPDGRLAALQWTADFLMWLFAFDDEYCDEGPAAASPDATLLIITKLQRIVEVPWAAPADDNYSAALLELRLRLDDLTTPVQTARWAASFRAYLQGQIWMAANSTYGRIPTLSDHLAVRLDSSGVKIFSTLSEIIHGYDLPAADYDRHDVRGFVEVFAAIIGWSNDLVSYHKERRRSQDSYGNVVDLIAHERQCSVEEAVSETATMHTRAMALYLRLRDQILRDAEPELRKWITDCDSWIRADYDWSLTTHRYVNPDD... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the sesquiterpene (+)-(1(10)E,4E,6S,7R)-germacradien-6-ol via a putative 1,10-cyclization, which could require the abstraction of the pyrophosphate from FPP to yield the (E,E)-germacradienyl cati... |
Q0UP11 | MASAALIDSDMEPTLQPILDQKTLRWIFVGGKGGVGKTTTSCSLAIQLAKHRKSVLLISTDPAHNLSDAFNQKFGKDARLINGFDNLSAMEIDPNGSIQDLLAGGGESGEDAMAGLGGMGNMMQDLAFSIPGVDEAMSFAEVLKQVKSMSYEVIIFDTAPTGHTLRFLQFPTVMEKALSKVSQLSRQFGPMLNSFLGGGGRLPNGQNIDELVEKMEALRGTISEVNGQFKDADLTTFVCVCIPEFLSLYETERMIQELNSYEIDTHSIVVNQLLFPKQDNPCEQCNARRKMQKKYLEQIEELYDEFNVVKMPLLVEEVRG... | Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored ... |
B2VVF0 | MASAALIDADMAPTLQSILDQKTLRWIFVGGKGGVGKTTTSCSLAIQLAKHRKSVLLISTDPAHNLSDAFNQKFGKDARLVNGFDNLSAMEIDPNGSIQDLLASGAEEGQDPMAGLGGMGSMMQDLAFSIPGVDEAMSFAEVLKQVKSMSYEVIIFDTAPTGHTLRFLQFPTVMEKALSKVSQLSRQFGPMLNSFLGASGRLPNGQNMDELIEKMENLRETIGEVNGQFKDADLTTFVCVCIPEFLSLYETERMIQELNSYEIDTHSIVVNQLLFPKQDNPCEQCNARRKMQKKYLDQIEELYDEFNVVKMPLLVEEVRG... | Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored ... |
Q9P7F8 | MSFDPLPGTLENLLEQTSLKWIFVGGKGGVGKTTTSCSLAIQMSKVRSSVLLISTDPAHNLSDAFGTKFGKDARKVPGFDNLSAMEIDPNLSIQEMTEQADQQNPNNPLSGMMQDLAFTIPGIDEALAFAEILKQIKSMEFDCVIFDTAPTGHTLRFLNFPTVLEKALGKLGGLSSRFGPMINQMGSIMGVNANEQDLFGKMESMRANISEVNKQFKNPDLTTFVCVCISEFLSLYETERMIQELTSYEIDTHNIVVNQLLLDPNTTCPQCMARRKMQQKYLAQIEELYEDFHVVKVPQVPAEVRGTEALKSFSEMLVKP... | Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored ... |
A7EHP6 | MSTAVINTDDDQLEPTLQSILDQKSLRWIFVGGKGGVGKTTTSCSLAIQLAKVRRSVLLISTDPAHNLSDAFSQKFGKEARLINGFENLSAMEIDPNGSIQELMGQAEEGEGPAAGMGGMMQDLAFAIPGIDEAMSFAEVLKQVKSLSYETIIFDTAPTGHTLRFLQFPTVLEKALAKVSQLSTQFGPMLNGLLGANGSLPNGQNLGEMMEKLEGLRETISEVNGQFKDENLTTFVCVCIPEFLSLYETERMIQELSSYHIDTHCIVVNQLLFPKKGSDCDQCNARRKMQKKYLEQIEELYDEFNVVKMPLLVEEVRGKE... | Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored ... |
C4JZ54 | MSSAVVPADDILEPTLQNILDQKSLRWIFVGGKGGVGKTTTSCSLAIQLAKVRKSVLLISTDPAHNLSDAFGQKFGKEARLIDGFDNLSAMEIDPSASMQDLMAAGGDQAEDMGFGLGGMMQDLAFSIPGVDEAMSFAEVLKQVKSLSYEVIVFDTAPTGHTLRFLQFPTVLEKGLAKLSQLSSQFGPMLNSVLGARGGLPGGQNLDDVLSKMESLRETISEVNTQFKNADLTTFVCVCIAEFLSLYETERMIQELTSYHIDTHAIVVNQLLFPGKDSTCDQCKARRKMQKKYLNEIEELYEDFNVVRMPLLVEEVRGKE... | Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored ... |
Q0IIZ2 | MAAPADDEFEDAPDVEPLEPTLSNVIDQRSLRWIFVGGKGGVGKTTCSCSLAVQLSRVRESVLIISTDPAHNISDAFDQKFSKVPTKVRGYDNLFAMEIDPSLGVAELPDEIFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCSIDTHNIIVNQLVFPEPEKPCRMCEARHKIQSKYLDQMEDLYEDFHIAKLPLLPHEVR... | Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1/WRB and CAMLG/GET2, ... |
Q84L08 | MSSSRFDSNKQLTTSSLVIGYALCSSLLAVINKLAITYFNYPGLLTALQYLTCTVAVYLLGKSGLINHDPFTWDTAKKFLPAAIVFYLAIFTNTNLLRHANVDTFIVFRSLTPLLVAIADTVFRSQPLPSRLTFLSLVVILAGAVGYVATDSSFTLTAYSWALAYLVTITTEMVYIKHMVSNIKLNIWGLVLYNNLLSLMIAPVFWFLTGEFTEVFAALSENRGNLFEPYAFSSVAASCVFGFLISYFGFAARNAISATAFTVTGVVNKFLTVVINVLIWDKHATPVGLVCLLFTICGGVGYQQSVKLDKPIEKVSEKDS... | Function: Acts as the major nucleotide-sugar transporter for the import of GDP-Fucose into the Golgi lumen. Transports GDP-Fucose in a strict counter-exchange mode. Is required for proper plant growth and development . Acts also as a GDP-mannose transporter that may be involved in the import of GDP-mannose from the cyt... |
P92916 | MDAQDIESRHPLIGARPRRRALRSLSILLAAALLLGLVLFYANGTGSGTAVDPVRVDNEFPWTNDMLAWQRCGFHFRTVRNYMNDPSGPMYYKGWYHLFYQHNKDFAYWGNITWGHAVSRDLINWQHLPVAVGPDHWYDISGVWTGSIIVVSEDRVVMLFTGGTKSFDQSINLAEAADPSDPLLLKWIKYDNNPILWPPPGIVRDDFRDPNPIWYNASESTYHIVVGSKNDSLQHTGIALVYLTKDFKKFDLLPTVLHSVDKVGMWECVEVYPVATTGPLLHKAIDNFDVDRVLDRSTVKHVLKASMNDEWHDYYAIGTF... | Function: Involved in the synthesis of fructan of the inulin neoseries. Catalyzes a self-transfer between identical oligosaccharides of the 1-kestose series.
PTM: Might be processed in two N-terminal and C-terminal proteolytic fragments.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: [1-bet... |
I3L273 | MKSFSRILFLVFLLAGLRSKAAPSAPLPLGCGFPDMAHPSETSPLKGASENSKRDRLNPEFPGTPYPEPSKLPHTVSLETFPLDFTEPLNPDLRETPHPESPETPKADSLTTSISESLDMPKTNLSKMAHPESSETPTPGPTEMPHPGSPETPKPNFSKTSRPEFPETPNTDLMQTTPQESPEILQLNATEVSQAELPETSNTNPTKTPDPKSPEKHDLNSTETPNSEFLQALHPDPSKTPHPESHVTHNPSPTEISQTEFPTTYYQNATDVPRTSDPQISTSLYPETPVPFKDDATALNELSLNPKPGTPAAIQPDSPK... | Function: Required for proper function of the olfactory system. May be involved in establishing the acuity of olfactory sensory signaling (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 56104
Sequence Length: 518
Subcellular Location: Golgi apparatus membrane
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J3KML8 | MQPFSPIFFHLLFLLNGLSSRAAPSPGQPVVADLQGMLQPSGMPTGTLENLTRDQPTPGSSASHPPEHSETPPSASPHISTKILRETPSPSPFLSLETPIPDQLTSVAESQGTSQMSPSRATLGKPSETPKPDPTGISPSDSPETPKPNPSNTSPPESPESVYTDPTPTLHHESPEISKRDTPKLSPGEESKIPSPRPTQFLSSKSLETYDPSATRHLNSALEPTTHPDPTESPQSVFLTTHNSNPTVVPQTQFPTSPSQNVTETARTSDLEPSSSLPTQPTTFREEATTPSEPGLSPSPEAPAVTRVATPGLSTSDSPG... | Function: Required for proper function of the olfactory system. May be involved in establishing the acuity of olfactory sensory signaling.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 53786
Sequence Length: 504
Subcellular Location: Golgi apparatus membrane
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Q5YKI7 | MKEEDSSFKLCVPGIVALQSPPNKAFRSTDTVGFLESELKKLLGMQQESRLWKLGSQEGRELLTRPEITVVEGEGYEVQRRLRHLPSPISVAQCLLLEEKGEMGNWPPE | Function: May be involved in spermatogenesis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12309
Sequence Length: 109
Subcellular Location: Cytoplasm
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Q6K1E7 | MAAPARTPRSRILGCSSMLRFLRNLVGSKGGSKSTNKPLTRSQPSSSWEQDVVSPMMGHQGGRGRKEPRAKVHSAASSNGKREPPPRVLSAAPSNPRHDAFELGTGDSGSQTLTSKDVPKLRAQGVEVTSVPLRGTWEVLEQLPEKKGEEEEPVGEVSGASDREHFGQALETEQGCLQWVPGPLALTPGAFIKEEEDEHCPIEFGDLKPSSCKVGSTPWNYLLGLYKQLQKSAMAKAQRPAAPQLALKDGLPHEEKGEREEAVDESCPKWCAPRASSDESCPKWCAPRASTYQSPLQKKFRSTDTVGFVESELKKILSVQ... | Function: Induces mitochondrial fragmentation, possibly by promoting DNM1L-dependent fission and may play a role in mitochondrial morphogenesis during spermatogenesis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40505
Sequence Length: 370
Domain: The N-terminal domain is required for targeting to... |
Q5J2D6 | MAAQARTPRSRILGCSSMLRFLRSLVGSKGSSKSSNRPLNRSQPSSSPEQDVVSPTMGHQGGCGRKETRPRVLSATSSNGKREPRPRVLSAAPSNQRLRDASGLGTGDTGSQTLTSKDVLKLRAQGVEVTSVPTRGTWEVLEHLPEKKGEEGEPAGEVSGASDRAHFGQALEAEQGCLQWVSGPMVLPPEAFIKEEEDEHCLIDFGDLRLSSCKVGSTPWNYLLGLYKQLQKSAMTKAQRPDADAPQFALKDSSPTEERGEREEAVDESSLKWCAPRASSDDSNLKWCAPRNSTYQSPLQKTFRSTDTVGFVESELKKIL... | Function: Induces mitochondrial fragmentation, possibly by promoting DNM1L-dependent fission and may play a role in mitochondrial morphogenesis during spermatogenesis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40854
Sequence Length: 373
Domain: The N-terminal domain is required for targeting to... |
E4PMA5 | MLLKNAVQLICYPDRIGNNLKDLYTVVDTHLSEAIGGLHILPFFPSNADGGFSPLTHKEVDPKVGTWDDIEAFTAKYDLCVDLTVNHISDESPEFTDFIANGFDSEYADLFVHVDKFGEISPDDMAKIHIRKEKEPFREVTLSDGTKTRVWCTFTEQQIDLNYESDLAYQLMESYIGFLTSKGVNLLRLDAFGYTTKRIGTSCFLVEPEVYQILDWVNQVALKHGAECLPEVHDHTSYQYAISRRNMHPYGFALPPLLLYSLLDANSTYLKNWLRMCPRNMVTVLDTHDGICIPDVEGVLPDEKIKVLIDNIDARSADPI... | Function: Catalyzes the reversible phosphorolysis of 2-O-alpha-D-glucosylglycerol with retention of the anomeric configuration, forming alpha-D-glucose 1-phosphate and glycerol. Has most likely a catabolic role, either regulating the intracellular levels of glucosylglycerol, which acts as a compatible solute, or degrad... |
Q8ECL7 | MHNIHRRHFLKAAGAVTAGLVTANIALNANASSVAPKPSSGKSVIGLIAPKMEVVRVGFIGVGERGFSHVEQFCHLEGVELKAICDTHQAVVDRAVEHIVKQKRPKPAVYTGNDLSYRELLNRDDIDIVIISTPWEWHAPMAIDTMESGKHAFVEVPLALTVEECWQIIDTAERTQKNCMMMENVNYGREELMVLNMVRQGLFGELLHGEAAYIHELRWQMKEINHKTGSWRTYWHTKRNGNLYPTHGLGPVSQYMNINRGDRFDYLTSMSSPALGRALYAKREFPADHERNQLKYINGDMSTSLIKTVKGRTIMVQHDT... | Cofactor: Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
Function: Glycosidase that has specific alpha-N-acetylgalactosaminidase activity.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: Cleavage of non-reduc... |
Q01S58 | MDKTSRRDLLKLASLAGIGAGLARSQGSSKSMAGVSFKPNGTVRIGVIGTGGRGGSLIENFSAVEGVQITALCDTVKDKVLKQQAWLDKAGKASHPIALFHSDDHAFENLVKRDDVDLVVVSTPWVWHTRMAVAAMKQGKHVAVEVPAARTIDECWELVNTSEATQRHCIQLENCCYGYNEMMVLNMVRAGLFGELTHGGAAYNHDLRSILFSAEGEGEWRRFEHLNRDGNLYPTHGLGPVAHYMDVNRGDRFDTLVSMSSISASLQQYRKEKIPAGDPRQKEVYKEGDFNVSLIRTVKGRVIELEHNVSSPQPYDRINL... | Cofactor: Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
Function: Glycosidase.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 48656
Sequence Length: 438
EC: 3.2.1.-
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Q9RK81 | MSQTPAVSRRLLLGSAAATGALATGIGSAAPVAAAEQAPRRRPGQKSMIGVPFAAHPTVRVAVIGLGNRGGGMITGWAAVPGCTVTAVCDIRADRAERAADRLESKGNPRPAEYGGSADSYARMLRRDDIDLVYIATPWEFHYEHGRAALLSGRHAVVELPVATELRQLWDLVDTSERTRRHLLLSENCNYGRNELAMLKAAHDGLFGDLTNGHGGYLHDLRELLFSDTYYTDSWRRLWHTRSTASFYPMHGLAPIAAAMDVNRGDRMTTLRATTTAPKGLADYRARFVPRDHPSWKETYINGDLVTCMIETAKGRTVRA... | Cofactor: Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
Function: Glycosidase (By similarity). Has no alpha-N-acetylgalactosaminidase activity.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 51800
Sequence ... |
B2FLK4 | MFAMKRREFIAASAAVAASSLLPQTPAWARGRKVRLAMIGTGMRGLVLLKELVRRDDVEVVALCDIEPIMLGRAMDMVAKAGKPAPKTYGQDRDTHAWKRLLEQKGIDGVIIATPWEYHAPMAIAAMQAGVAVGCEVVAGITLQDHWDVLKTQLSTGTPYMLLENVCYRRDVMAALQMVRQGLFGELVHLQAGYQHDLRGVKFNSGDPNQPYDSGVEFGPKGWSEARWRTEHSVERNGELYPSHGIGPCAMYTGINRGNRFTHINAFATKARGLHEYTVAKSGGTTHPSTKVKFKLGDIVTTTLACENGETILLQHDTSL... | Cofactor: Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
Function: Glycosidase.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 50486
Sequence Length: 454
EC: 3.2.1.-
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Q50HM6 | MNDAAPQNPGQDEAKGTGEKDNGGSMSPRSALRTTAGVAGAGLGLSALGTGTASASVPEAAQTAVPAAESDESAAPKRQGRTMAGVPFERRSTVRVGIIGLGNRGGSMIDLFLAVPGVRVVALCDTVRDKAASAAAKVVKAGQPAPAVYTKDEHDYEQLCARGDVDFVYVATPWDFHFEMAKTAMLNGKHVGVECPVAMRLDELWKLVDLSERTRRHCMQLENCAYGKNEMRVLRMAHAGLFGDLLHGAGAYNHDLRGLMFDPDYYEGPWRRLWHTRLRGDLYPNHGFGPVANYLDINRGDRAVSITSMGTPALGLAQYR... | Cofactor: Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
Function: Glycosidase.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 54036
Sequence Length: 494
EC: 3.2.1.-
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A4Q8G1 | MENTRRNFLKKVTAAGIGAAGLAVTDQAMAAVNQPGEAAQQKKKPAGKSDGMLRFGFIGTGSRCQEHINNVLGIQGNKIVAICDIQKGPLEKTLKHIAKFNVPEPKVYTGGEREFEKMLNNEEFDCVIIASPWEWHVPMAVAAMKAGVPYVGVEVSAANTVEECWDLVNVSEATGSHLNILENVCYRRDVMAALRMVREGLFGEMIHGTCGYQHDLRDVKFNDGIHYTYQEGGELRMGPTAYAEAQWRTQHSVTRNGDIYPTHGIGPVANCLNINRGNRFLSLTSMATQSRGLHNFVVDKGGANHPYAKIHFNLGDIVTS... | Cofactor: Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
Function: Glycosidase that has specific alpha-N-acetylgalactosaminidase activity.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: Cleavage of non-reduc... |
E4Q361 | MSFPKGFLWGAATASYQIEGAWNEDGKGESIWDRFTHQKGNILYGHNGDVACDHYHRHEEDVSLMKELGIKAYRFSTAWARIFPDGFGNINQKGLEFYDKLINELVENGIEPVVTLYHWDLPQKLQDIGGWANPEIVNYYFEYAMLIINRYKDKVKKWITFNEPYCIAFLGHWHGIHAPGIKNFKVAMDVVHNIMLSHFKVVKAVKENNIDVEIGITLNLTPVYLQTERLGYKVSEIEREMVNLSSQLDNELFLDPVLKGSYPQKLLDYLVQKDLLDSQKVNNMQQEVKENFIFPDFLGINYYTRSVRLYDENSGWIFPI... | Function: Has high beta-D-glucosidase, exoglucanase, beta-D-xylosidase, beta-D-galactosidase, and transgalactosylation activities in vitro. Has a very broad substrate specificity with the highest activity with p-nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Active with pNP-beta-D-glucopyranoside (pNPGlu),... |
Q6DB24 | MKPSVILYKKVADDLRARLDQHFTVTELDAFPALDHPALATAEGIIGSGGKVDKDFLQHAPRLRAASTISVGYDTFNVDALNEKGVILMHTPTVLTETVADTVLALMLASARRVVEVVERVKAGEWKGGVGSDWFGTDVHHKTIGILGMGRIGLAVAQRAHFGFSMPVLYNARRHHAEAEERFNARHCDLDTLLAESDFLCITLPLTAETHHLIGREQLAKMKPSAILINIGRGAVVDEDALTEALVKGTIQAAGLDVFVKEPLPVDSPLLDLPNVVALPHIGSATHETRYDMAACAVDNLIAALSGQVKENCVNPQVLK | Function: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively.
Catalytic Activity: glycolate + NADP(+) = glyoxylate + H(+) + NADPH
Sequence Mass (Da): 34549
Sequence Length: 320
Subcellular Location: Cytoplasm
EC: 1.1.1.79
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Q99JY3 | MEVQCGGAGFIPESSRSSHELGNQDQGIPQLRIVLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVSTWDGKELVVVDTPGIFDTEVPDADTQREITRYVALTSPGPHALLLVVPLGRYTVEEHKATQKILDMFGKQARRFMILLLTRKDDLEDTDIHEYLEKAPKFFQEVMHEFQNRYCLFNNRASGAEKEEQKMQLLTLVQSMVRENGGRCFTNKMYESAECVIQKETLRMQELYREELEREKARIRREYEEQIKDLRDELEREIRRARMEREFKEREAIFTKNQQNARKEVENTSMILELIIKAWEIASF... | Function: During thymocyte development, may play a role in the regulation of apoptosis.
PTM: Phosphorylated at very low levels in resting splenocytes. Rapidly and transiently phosphorylated in response to splenocyte activation. Phosphorylation is increased in cells undergoing apoptosis.
Sequence Mass (Da): 38044
Sequen... |
Q96F15 | MGGFQRGKYGTMAEGRSEDNLSATPPALRIILVGKTGCGKSATGNSILGQPVFESKLRAQSVTRTCQVKTGTWNGRKVLVVDTPSIFESQADTQELYKNIGDCYLLSAPGPHVLLLVIQLGRFTAQDTVAIRKVKEVFGTGAMRHVVILFTHKEDLGGQALDDYVANTDNCSLKDLVRECERRYCAFNNWGSVEEQRQQQAELLAVIERLGREREGSFHSNDLFLDAQLLQRTGAGACQEDYRQYQAKVEWQVEKHKQELRENESNWAYKALLRVKHLMLLHYEIFVFLLLCSILFFIIFLFIFHYI | Function: Plays a role in T lymphocyte development and the optimal generation of CD4/CD8 double-positive thymocytes (By similarity). Inhibitor of GSK3A, possibly by sequestering GSK3A in cytoplasmic vesicles and impairing its translocation to the nucleus. Consequently, impairs GSK3A-dependent transcriptional program an... |
Q8BWF2 | MEHLQKSTYGTIVQGPEAHCVQESSCLRILLVGKSGCGKSATGNSILRRPAFQSRLRGQSVTRTSQAETGTWEGRSILVVDTPPIFESKAQNQDMDKDIGDCYLLCAPGPHVLLLVTQLGRFTAEDAMAVRMVKEVFGVGVMRHMIVLFTRKEDLEEKSLEEFVTHTDNRSLRSLTQECGRRYCAFNNRASGEEQQGQLAELMALVRRLEQECEGSFHSNDLFLHAEALLREGYSVHQEAYRCYLAKVRQEVEKQRRELEEQEGSWIAKMICTVKSCWSSHTAACALLIVLGLTLLTTFINLCISRCK | Function: Plays a role in T lymphocyte development and the optimal generation of CD4/CD8 double-positive thymocytes . Inhibitor of GSK3A. May act by sequestering GSK3A in cytoplasmic vesicles and impairing its translocation to the nucleus. Consequently, impairs GSK3A-dependent transcriptional program and regulation of ... |
Q8K3L6 | MEDHGFEELSTRTHDLNVRRLTKGNINFLLSTGQETYSVEDSGLLRILLVGKSGCGKSATGNSILRRPAFESRLRGQSVTRTSQAEMGTWEGRSFLVVDTPPIFESKIQNQDMDKDIGNCYLMCAPGPHVLLLVTQLGRYTVEDAMAVRMVKQIFGVGVMRYMIVLFTHKEDLADESLEEFVTHTGNLDLHRLVQECGRRYCAFNNKASGEEQQGQLAELMALVRRLEQEHEGSFHSNDLFVYTQVFLRGGYSEHQEPYKFYLTKVRQEVEKQKRELEEQEGSWMAKMLCRVTSCLDWHIAVSVLLIVLGLTLLITLINM... | Function: Required for mitochondrial integrity and T-cell survival. May contribute to T-cell quiescence.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 37266
Sequence Length: 326
Subcellular Location: Lysosome membrane
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G5ECR8 | MSRWKVVILCLLSFMFEIGHASFQCNPKTYDGAFLNIVCVCNATFCDEIEPIGEIAEGKAIVYRSSLDGDRLKRMSMKMKEKLRKNESVNVTITIDASERFQNIFGFGGAFTDSAGDQFVSLSETLQNYIVDSYFGKNGLEYNIGRVPIASCDFSTHEYSYDDVHDDFELKHFALPDEDLKLKIPFIKKAIEKTEGNIQLFASPWSAPGWMKVTGRMRGGGAMRNDKRVYQAYADYFFKFFEAYSSHAITFWGLTIQNEPSTGADMAWRWQTMNYTAETMRDFLKKYLGPKLKENKLTETLKVMVLDDGRGLLPGWADTI... | Catalytic Activity: a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-glucose
Sequence Mass (Da): 59088
Sequence Length: 522
Pathway: Lipid metabolism; sphingolipid metabolism.
EC: 3.2.1.45
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Q9UB00 | MILNISVSLLIFLAFYGFSSDAKSLPCSEVKKEYGIVCRCNATYCDTIEPLGTVTSGKAVVYTTSRNGKRMNRSELKHTTSSTAKTKVYVNTTQSFQPVMGFGAAFTDAAGINMKMLPQTMQDQIIQQYFSDDGLGYVFGRVPMASTDFSTHEYSYDDVKFDFDLKNFNLTVEDLQYKIPFIKKAMTASGGKLKLFATPWSSPGWMKTSGRMVGAGELLGDQNGKYYQTWAQYFVKFFEAYHAQGIDFWSLTPQNEPTTGIDPLWKWQTLFFDASMERNFIKKLLGPALASSPVTKNLKIMINDDQRINLPHWPNVILTD... | Catalytic Activity: a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-glucose
Sequence Mass (Da): 58247
Sequence Length: 519
Pathway: Lipid metabolism; sphingolipid metabolism.
EC: 3.2.1.45
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Q9Y223 | MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGT... | Function: Regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. Plays an essential role in early development (By similarity). Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metast... |
I7FJX8 | MIELDRLDLGGGRRLVITSEPDAAVPQVRDADGHWRRAGPGDGVAEAMLDALNQNPGTTKHGNFTLLSWASQTARGERPITVDQTNESVIVGDAAVVKWATHLQEGPHPAPARIKALRGNGFRGMPMPWGLVTWQTADHPETLVVTVDEYLPDAVDGWTWAVALVTDAAQDRAAVPALVDAVTAVGCVVAELHAAQADTARPATAADARSWREAALETVETAATLGTSVSGELLRARREDVEAVVGTLGDLAGIPVLAGHGDLHVGQVLRAGGRYVVTDFDGNPVLPAEARVKPVPAALDVAGMAQSLAHVAIVACKYTE... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the ATP-dependent phosphorylation of D-glucosamine (GlcN) to D-glucosamine 6-phosphate. May be involved in the phosphorylation of acquired extracellular GlcN derived from the hydrolysis of chitosan, i.e., in the incorporation of exogenous GlcN into the bact... |
A0A1H7TQR5 | MTPNWSELVAAADPALVLPSGERRAEVAVPGPLRLDALLDLGEGHAVGVVRSADAARWTVPLVRDGAGGVRRSRPGDGTAEHLVAALARRGATPDAAFVLEAFTGAAPVTGERGIIVDQTNESVIVGECAVVKWAVRLPAEGEPGSPAAQRIAALARGGFTEMPRPWGLLTLAEGAQPVLLASVVAYLPGALDGWDWAVDDVRRLARGELTMDQALLPAAQLGTLTARMHAALAARGRTPATAADVAAWGVRMREELDEAVASVPGAEGERLKAWAPRIADVYAELDALAGTPLIDVHGDFHVGQILRADGRYAVVDFDG... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the ATP-dependent phosphorylation of D-glucosamine (GlcN) to D-glucosamine 6-phosphate. May be involved in the phosphorylation of acquired extracellular GlcN derived from the hydrolysis of chitosan, i.e., in the incorporation of exogenous GlcN into the bact... |
O07563 | MLRGTYLFGYAFFFTVGIIHISTGSLTPFLLEAFNKTTDDISVIIFFQFTGFLSGVLIAPLMIKKYSHFRTLTLALTIMLVALSIFFLTKDWYYIIVMAFLLGYGAGTLETTVGSFVIANFESNAEKMSKLEVLFGLGALSFPLLINSFIDINNWFLPYYCIFTFLFVLFVGWLIFLSKNREYAKNANQQVTFPDGGAFQYFIGDRKKSKQLGFFVFFAFLYAGIETNFANFLPSIMINQDNEQISLISVSFFWVGIIIGRILIGFVSRRLDFSKYLLFSCSCLIVLLIAFSYISNPILQLSGTFLIGLSIAGIFPIALT... | Function: Can transport glucose, mannose, 2-deoxyglucose and methyl alpha-glucoside, but not galactose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44910
Sequence Length: 401
Subcellular Location: Cell membrane
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A0A0H2VG78 | MKANKYLIFILGALGGLLYGYDNGVISGALLFIHKDIPLNSTTEGIVVSSMLIGAIVGAGSSGPLADKLGRRRLVMLIAIVFIIGALILAASTNLALLIIGRLIIGLAVGGSMSTVPVYLSEMAPTEYRGSLGSLNQLMITIGILAAYLVNYAFADIEGWRWMLGLAVVPSVILLVGIYFMPESPRWLLENRNEEAARQVMKITYDDSEIDKELKEMKEINAISESTWTVIKSPWLGRILIVGCIFAIFQQFIGINAVIFYSSSIFAKAGLGEAASILGSVGIGTINVLVTIVAIFVVDKIDRKKLLVGGNIGMIASLLI... | Function: Transporter highly specific for glucose uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48375
Sequence Length: 446
Subcellular Location: Cell membrane
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Q89YS5 | MPATEKASAPHWSFLSSDVISIMKSNPSTLLLPLAALSLASCANPQKEETKRPNIIFMMTDDHTTQAMSCYGGNLIQTPNMDRIANEGIRFDNCYAVNALSGPSRACILTGKFSHENGFTDNASTFNGDQQTFPKLLQQAGYQTAMIGKWHLISEPQGFDHWSILSGQHEQGDYYDPDFWEDGKHIVEKGYATDIITDKAINFLENRDKNKPFCMMYHQKAPHRNWMPAPRHLGIFNNTIFPEPANLFDDYEGRGKAAREQDMSIEHTLTNDWDLKLLTREEMLKDTTNRLYSVYKRMPSEVQDKWDSAYAQRIAEYRKG... | Function: Exosulfatase involved in the degradation of the glycosaminoglycan (GAG) heparan sulfate (HS). Catalyzes the hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units . GAG-specific sulfatases play a key role in the persistence of the major human gut symbiont B.thetaiotaomicron in the ho... |
Q97UZ1 | MKRKYPYSLAKGLTSTQIAVIVAVIVIVIIIGVVAGFVLTKGPSTTAVTTTVTSTFTTTTTIPSTTTSTPSNTVVFYTWWGGGDGGEALSQIIPAVKQYAGLQMQTYSIPGAGGTNAKYAILALIQAGKPPAAFQVHYGPEMISYVEAAPNGIHTFVNMTPYLIQWGLLNNAVYAVLQAGAYNGTLLSVPINVHRGAVLYVNTQLLREYNLPFPYNFSTLVYDTVQLANHGVSPWIIPGGDGGWDQFNVWEDIFLYLAGPQLYNELIYGTLNFSNPTVQKLINETNYWFLNFTSYNYPGWQSMSWEQAFALIAQGKVAFQ... | Function: Part of the ABC transporter complex GlcSTUV involved in glucose uptake (Probable). Binds glucose. Can also bind galactose and mannose .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61128
Sequence Length: 554
Subcellular Location: Cell membrane
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Q9VQC4 | MAKRQTWEQMRQIFVQAVNAVHPEKVFADFQKFDLRPQIGENATDISIKLNGERQDISGKTCHIVGFGKAVLGMANKVQQDLGATSAGGVLSVPVNTLKQFQQPVAPGLVVHEGAANNLPDENALKAAREIKQLAEKMTAQDILFVFISGGGSALLPLPRSPLTLEDKRSIADKLMKRGASIQEINAVRIACSDIKGGRLARLAGQAGLLVTFVLSDIIGDPLELIACGPTIQPEAAASPSDILKKHHVWEELSPEIRRVFEQPEEQKNTSLPEHKVFVVGSNVIATSTAAHEAERLGYIPCVLSCAVQGDVAQVAGDYQ... | Catalytic Activity: (R)-glycerate + ATP = (2R)-3-phosphoglycerate + ADP + H(+)
Sequence Mass (Da): 52792
Sequence Length: 487
Subcellular Location: Cytoplasm
EC: 2.7.1.31
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Q8IVS8 | MAAALQVLPRLARAPLHPLLWRGSVARLASSMALAEQARQLFESAVGAVLPGPMLHRALSLDPGGRQLKVRDRNFQLRQNLYLVGFGKAVLGMAAAAEELLGQHLVQGVISVPKGIRAAMERAGKQEMLLKPHSRVQVFEGAEDNLPDRDALRAALAIQQLAEGLTADDLLLVLISGGGSALLPAPIPPVTLEEKQTLTRLLAARGATIQELNTIRKALSQLKGGGLAQAAYPAQVVSLILSDVVGDPVEVIASGPTVASSHNVQDCLHILNRYGLRAALPRSVKTVLSRADSDPHGPHTCGHVLNVIIGSNVLALAEAQ... | Catalytic Activity: (R)-glycerate + ATP = (2R)-3-phosphoglycerate + ADP + H(+)
Sequence Mass (Da): 55253
Sequence Length: 523
Subcellular Location: Cytoplasm
EC: 2.7.1.31
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Q6MAS9 | MHIIHIASELAPLAKVGGLADVVLGLCRELSWKGHDVDIIIPKYDCMDSEQIRDLTVDYFELPSFYNGEWFFNTVWMGWVENLKVYFIEPHHPRFFFNRGCFYGCEDDLERFLYFSRTALEFLYKKSILPDIIHLHDWQTAVIAPLYKDMYQKLGYTKPKILFTIHNMEYQGKCAAHDLNYIGLDGNRYQQHSFMQDNLYPHLINLLKGGIVYSDFVTTVSPNYAKEVLTPKEGRGLEATLVEYQHKFKGILNGIDYSYWNPEIDRFLPAHYSLREMPKNKKDRNTVDKKGFIKKILREKLYLAEEHRPIIGCITRLVPQ... | Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Mass (Da): 58201
Sequence Length: 500
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
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Q6CZK3 | MRVLHVCSELFPLLKTGGLADVAGALPGAQIAAGMDVRVILPAFPDLKKGIANLQVVRELDTFAGHVTLLFGHFNGVGIYLIDVPELYERAGSPYHDPALYAYADNYLRFALLGWMGCEMACGLDHYWRPDIVHAHDWHAGLTCAYLAARNRPAKSVFTVHNLAYQGLFAAGHMANLHLPSDFFQVYGLEFYGQISYLKAGLFYADHITTVSPTYAHEITLPAYGYGMEGLLKTREEEGRLSGILNGVDETIWNPTHDPLLTNHYSREALANKAENKRHLQTAMGLKVDDKAPVFAIVSRLTSQKGLDIALSAIPDLLEQ... | Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Mass (Da): 52541
Sequence Length: 479
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
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A9BG68 | MKIAYVSYEVSPFAKAGGLADVAGALPKYIKNAGEDIYVVMPFHKNIENNYDISKFEVVKTGLIPDSHTHKSPFSVYKSYLEGSSVVIYFIKTDSLYDSKNIYDEENIFLKTSYFCDSALKTIKECEPDTNVININDWHTSLIPVYLKTHYLQDNILKKIATILTIHNIGYQGLFNPEVLNQAGLPNYLFNMNALEYYGKVNVLKGGILFSNIINTVSPTYAKEIQSEEYGYGLEGILKVRSEDLFGILNGIDYSIYDPLKDPHIFHPIESYEDKLKNKTSLQEYLGLTKDENITLISFIGRLFEQKGIDLISKIMDLLL... | Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Mass (Da): 55456
Sequence Length: 483
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
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A1VL96 | MKVLHAAAEVYPLVKTGGLADVLGALPEALIGAGADVRLVLPGLPAILAGVEQQQVVHEIGAVFGAGRVTLRLGRLAHNGVPAYVIDAPYLYQRPGNPYLAPDGGEWPDNLQRFGLLGWVAAHLAAGELDPGWTPDVLHAHDWHAAMACAYAACHPATRAATVYTIHNLAYQGLFDEDDFHLLGLPSRLMVPVGLEFHGQLSFMKAGLKYAHRITTVSPTYAHEIATEAFGCGLDGVIRARGADVSGILNGVDGAVWNPASDPLIAAPYSADMLDGKALCKAALQRELGLAVDAGAPVFAVVSRLTSQKGLDLLLDALPA... | Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Mass (Da): 51711
Sequence Length: 494
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
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Q7VBP0 | MRVLFAAAECAPMVKVGGMGDVVASLPSALAKLGHDVRLIIPGYSKLWGLLDISKDPIYTAQTMGAEFSVYETKHPTSNLPIYLVGHPVFDPERIYGGEDEDWRFTFFASATAEFAWNVWKPQVLHCHDWHTGMIPVWMHQDPEISTVFTIHNLKYQGPWRWKLERMTWCPWYMSGDHTMAAAMLFADRVNAVSPTYSREIRTSEYGESLEGLLNYISGKLRGILNGIDLDEWDPATDKALPANFSSGKMSTRKKNKEALQRQMGLEVNNDKYLLGMVGRLVDQKGVDLLLQVSRRLLAYTDSQIVVLGTGDQILESALW... | Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Mass (Da): 56943
Sequence Length: 501
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
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O84874 | MDPFFLNTQHVELLVSGKQSSPQDLLGIVSESLNQDRIVLFRPGAETVFVELRGKIQQAESHHSGIFSLPVMKGISPQDYRVYHQNGLLAHDPYAFPLLWGEIDSFLFHEGTHQRIYERMGAIPCEIDGVPGVRFIVWAPHAQRVSVIGDFNGWHGLVNPLHKVSDQGVWELFVPGLTAGACYKWEMVTESGQVLIKSDPYGKFFGPPPWSVSVVIDDSYEWTDSEWLEERIKKTEGPMNIYEVHVGSWRWQEGQPLNYKELADQLALYCKQMHYTHVELLPVTEHPLNESWGYQTTGYYAPTSRYGSFEDLQYFIDTMH... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q0TQ16 | MRNCKELKHEKNGNVTEKIGKNKGKSKKVSKDESLLSFDLFLEGKEHSAYKFMGAHFVTENRKRGVRFTTWAPRSSKIYVIGDFNNWELKEEYSMKKINERGIWSLFLPKLEEGIKYKFAVVNECGNNTVYKADPYAFKSELRPNTASVLTKIKSFRWGDKRWLNKREKEGLDNKPMNIYELHLGSWKRKDGEFMTYEEISEVLVEYVKEMGYTHVEFMPINEHPLDASWGYQGVGYYSVTSRYGDLNGLKALINKLHKNNIGVLLDWVPSHFCKDEHGLFMFDGSPTYEYGAWWKANNEGWGTCNFDLGRPEVKSFLFS... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q8NR40 | MTVDPASHITIPEADLARLRHCNHHDPHGFYGWHETEAGSVIRTRQVGATQVNLLIDDTSHVMTPIGDDIFAIDLGHRERADYRLEVTWPDQEPQVKADPYYFLPTVGEMDIYLFSEGRHERLWEILGANIKTYQTALGTVRGTAFTVWAPNAIGCAVVGGFNGWNASQHPMRSMGGSGLWELFIPGIEEGEVYKFAVQTREGQRRDKADPMARRAELAPATGSIVASSEYQWQDSEWLRERSQTDLASKPMSVYEVHLGSWRWGKNYEDLATELVDYVADLGYTHVEFLPVAEHPFGGSWGYQVTGYYAPTSRWGTPDQ... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q6A8Q7 | MAHDEFGGLTGWDLEGFHSGGDTEVWKRLGSHVVTIDDDERGPITGTRFAVWAPNAQAVEVISDFNWWTGDRMRLIPGSGVWGTFVEGVDEGTLYKFRIQDQWGTWHEKVDPMARYSEQAPQNASIVTETHYEWNDDEWIARREASRAHAEPMSVYEVHLGGWRHGLSYRELADQLVSYVTWQGYTHVEFMPLAEHPFAPSWGYQVTGYFSPTSRYGSPDDLRYLIDKLHQAGIGVIMDWVPGHFPKDDWALGRFDGTALYEHADPRQGEHKDWGTYIFNYGRNEVKSFLVSSALYWISEFHADGLRVDAVASMLYLDYS... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
P32775 | MYNIPDNVKGAVEFDPWLKPFADVLSERRYLADKWLYDITHATPDGSYQSLSKFARDSYKSYGLHANPETKEITYKEWAPNAERAFLVGDFNNWDTTSHELKNKDEFGNFTITLHPLPNGDFAIPHDSKIKVMFILPDGSKIFRLPAWITRATQPSKETSKQFGPAYEGRFWNPENPYKFVHPRPKFSESVDSLRIYEAHVGISSPEPKITTYKEFTEKVLPRIKYLGYDAIQLMAIMEHAYYASFGYQVTNFFAASSRFGTPEELKELIDTAHSMGILVLLDVVHSHASKNVEDGLNMFDGSDHQYFHSISSGRGEHPL... | Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 81116
Sequence Length: 704
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q9KRB5 | MAGVLGMILAGGEGSRLKPLTETRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYIHMKKGWNLSGITDRFIDIIPAQMRDGKRWYEGTADAIYQNLRFVEIVAPDQVCIFGSDHIYKMDIRQMLDFHRRMEAELTVSALRMPISQASQFGVIEVDENGKMVGFEEKPSNPKSIPGEPEWALVSMGNYIFEAETLSKELREDAENNQSSHDFGKDIIPKMFPRGKVYVYDFTTNKIKGEKESTYWRDVGTIESYWSAHMDLLDKDPEFSLYNRSWPLHTYYPPLPPATFVDVKDKKVKITDSLISGGSYI... | Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glu... |
Q9KLP4 | MQDTLAVILAGGMGSRLSPLTDDRAKPAVPFGGKYRIIDFTLTNCLHSGLRRILVLTQYKSHSLHKHLRNGWSIFNPELGEFITVVPPQMRKGGKWYEGTADALFHNMWLLARSDAKYVVVLSGDHIYRMDYAAMLEEHISKNATLTIACMQVPRHEASAFGVMAIDDDSRITCFVEKPADPPCIPNRPDHSLASMGIYIFNMDVLKKALTEDAEIEQSSHDFGKDVIPKLIATGSVFAYSFCSGKGRVARDCYWRDVGTIDSFYDANMDLLQPVPPMNLYQKNWAIRTYEQQYPPARTVSSATGNEGIFINSIIANGVI... | Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glu... |
Q2RS49 | MDQITEFQLDINRALKETLALVLAGGRGSRLRDLTNRESKPAVPFGGKYRIIDFPLSNCMNSGIRRMCVITQYRAHTLIHHIQRGWGFLRAEIGEFVELWPAQQQTDKESWYLGTADAVHQNLDLIRMHDPRFVLILAGDHIYKQDYSKLLAHHIARGSDCTVACVDVPREEATGYGCVEVDNDDNIVHFLEKPANPPGIPGRPDRAFASMGIYIFNADFLYEILESDALNEASQHDFGRDIIPSQVGKARIVAHRFSQSCVYSVGRREPYWRDVGTVDAYWSANIDLVSVTPALDLYDADWPIWTYQMQRPPAKFVFDT... | Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glu... |
B7K5U7 | MKKVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPLSNCINSEILKIYVLTQFNSASLNRHLTRTYNFTGFSDGFVEVLAAQQTAENPKWFQGTADAVRQYLWAFQEWDIDEYLILSGDHLYRMDYRDFIQRHRETGADITLSVVPIDEERASSFGLMKIDDHGRVVDFSEKPKGDELKQMQVDTTVLGLTPEQAKESPYIASMGIYVFKKEVLAQLLEENPDQTDFGKEIIPFSAKDYNLQAYLFKGYWEDIGTIKAFYEANLALNRQPSPRFSFYNEEYPIYTRSRYLPPTKALNCTITESMVSEGCILKDC... | Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glu... |
Q21M27 | MLDPNSRYVSRLTRDTVALVLAGGRGSRLHELTDWRAKPALHFGGKFRIIDFPLSNCVNSGIRRIGILTQYKAHSLIRHVIRGWSSFKKEFGEYVEILPASQRYSPNWYQGTADAIYQNLDILQAEAPKYILVLSGDHVYQMDYGAIIAHHVETGADLTVSCIEVPIEEAAGSFGVMTVDDDNRIIRFDEKPQRPTELANKPGYTLASMGNYVFNTEFLFDQLRKDAADPDSEHDFGKNIIPNIIAEKLVSAYRFRDHDTNETAYWRDVGTLDSFWEANMELVSPNPSLNLYNHDWPIWTYQTQLPPAKFVFDDDSRRGY... | Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glu... |
A6TF50 | MTSLAAGKPAPLGASYDGKGVNFALFSAHAERVELCVFDEQGNEQRFDLPARSGDIWHGWLAAAGPGLRYGYRVHGPWDPAQGHRFNPAKLLIDPSAHRVEGDLPDDERLHGGMWQPDRRDSAAVAPKSQVVDLRYDWRGDKPPRTPWGETVIYEAHVKGLTLLNPQLPEAIRGTYKALGHPAMIAYFKSLGISALELLPVAQFASEPRLQRMGLSNYWGYNPLAWFALDPRYASDPDRALDEFRDAVKALHAAGIEVILDIVLNHSAEIDLEGPTVSLRGIDNRSYYWVREDSDYHNWTGCGNTLNLSHPGVVEWARQC... | Function: Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin.
Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches with degrees of polymerization of three or four glucose residues in limit... |
Q8YDC6 | MQAIIDAEQSFKFPVLVGDIGGTNARFSILVDSNAEPKEFPVLQTADYATIDEAIQHAILDQTAIQPRSVILAVAGPVDGDEIDLTNCDWVVRPKKMIADLGFEDVTVLNDFEAQALAVVSLEGHHMEQIGGKPEEAVATRVVLGPGTGLGVAGLVCTRHAWVPVPGEGGHIDIGPRTERDYQIFPHIERIEGRVTGEQILSGRGLRNLYLGICAADKITPTLETPVDITSAGLDGSNPQAAETLDLFATYLGRLAGDLALIFMAHGGVYLSGGIPVRILSALKAGSFRAAFEDKAPNKAIMRDIPVRVITYQLAALTGL... | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 36919
Sequence Length: 343
Subcellular Location: Cytoplasm
EC: 2.7.1.2
|
Q62HW8 | MSTGAQTKAAAASQHADGPRLLADVGGTNARFALETGPGEITQIRVYPGAEYPTLTDAIRKYLKDAKIGRVNHAAIAIANPVDGDQVRMTNHNWSFSIEATRRALGFDTLLVVNDFTALAMALPGLTDAQRVQIGGGTRRQNSVIGLMGPGTGLGVSGLIPADDRWIALGSEGGHATFAPMDEREDLVLQYARRKYPHVSFERVCAGPGMEIIYRALAARDKKRIAANVDTADIVERAHAGDALALEAVECFCAILGTFAGNLAVTLGALGGIYIGGGVVPKLGELFMRSPFRARFEAKGRFEAYLANIPTYLITAEYPA... | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 68376
Sequence Length: 641
Subcellular Location: Membrane
|
Q9A6N3 | MDGNHSGGLGLVGDIGGTNARFALVEFDGQDPRLIEPTAYRGEDYGTAEDAIEEYLRKVGVKHPDQAVVAVAGPIDHGQVHMTNLDWRISEDGLRRAGGFRNAKLINDFTAQALAAPRVGPKDLRQIGELPTSGEGDLAILGPGTGFGVAGLVRRHGQEIPLATEGGHVAFAPVDDVEIEVLRALTRRLDGGRVSVERILSGPGMEDLHVDLAAAEGRGVEALTAKQITERAVEGCADSLATVNRFCAILGSTAGDIALTLGARGGVFIAGGIAPRIIDILEKSPFRERFDSKGRLSGFTRSIPTHVILHPHTALIGAAV... | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 34714
Sequence Length: 331
Subcellular Location: Cytoplasm
EC: 2.7.1.2
|
Q1QZ16 | MTRPALIGDIGGTNARFALVTPGAFDLHDIRTLPCAHYPSLSDAIRAYLKEVGAEMPTEACLAFACPVHDDEVRMTNNAWRFSKRQVAEEFGFTLFKVINDFTAQALGVPHVADDELVALGDGEAAPGCTRLIFGPGTGLGMAGLFPGQHDWIPLPTEGGHISFAPTDQHERDLLAYFQARYGRVSVERILCGQGLLDLYRAHAQLAKQVARYNTPAEVTGAARAGDPLARNALERFLKILGDVSGDAALMLGARGGVYLCGGILPRLLDWLPHSHFRDAFADKGRMHAYTAHIPVWVVTAPWNGLLGACEALHNEEVT | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 34536
Sequence Length: 319
Subcellular Location: Cytoplasm
EC: 2.7.1.2
|
Q7P1R6 | MSTGLPEAWPRLLGDVGGSNARFALETAPGVIEDILTLSNERYPTLEDALRDYLAQVGARRVAHAAIGIANPLNGDLVRMTNCHWSFSIEATRRALGLSTLLLLNDFTALALALPRLPRRELAQVGGGAPRPDAPLALIGPGTGLGVSALVPHAGGWRALAGEGGHTSFAPANEREIGIWRYASARFGHVSHERLLSGSGLSLLHRALCALDGAEEAGLAPAEVSARGLSGADARCREALEIFCALLGSAAGNLALTLGARGGVYIGGGIVPRLSGFFEQSPFRRRFEDKGRMSAYLADIPVYLITSAYPALPGVAAHLA... | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 36267
Sequence Length: 348
Subcellular Location: Cytoplasm
EC: 2.7.1.2
|
Q47XU3 | MKNSQDTQVINLVADIGGTNIRLAITDKDNNINEIKTYQCKDFPHLSNVIYHYLKENGLLNSQVNACLAIACPVDTDSISMTNLPWKFSQKQLKEELKLHSLTLINDYTAIAMAIPLLSDKQKVKIGHGEAENKQPIAVCGPGTGLGVANLVNINNHWYCLGGEGGHTDFAPVDELDVKIFQQLKTTKKRLSYEQLLSGYGLEQIYQALVIINNQEATNAEQSKLSAKEISTQAIAGTCPICQQALSQFCKILGSFSGNLALTTGSFGGVYIAGGIVPRFIDYLKNSEFRARFETKGRMSHLNEQIPTYIITESQPGLLG... | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 36201
Sequence Length: 330
Subcellular Location: Cytoplasm
EC: 2.7.1.2
|
P21908 | MEIVAIDIGGTHARFSIAEVSNGRVLSLGEETTFKTAEHASLQLAWERFGEKLGRPLPRAAAIAWAGPVHGEVLKLTNNPWVLRPATLNEKLDIDTHVLINDFGAVAHAVAHMDSSYLDHICGPDEALPSDGVITILGPGTGLGVAHLLRTEGRYFVIETEGGHIDFAPLDRLEDKILARLRERFRRVSIERIISGPGLGNIYEALAAIEGVPFSLLDDIKLWQMALEGKDNLAEAALDRFCLSLGAIAGDLALAQGATSVVIGGGVGLRIASHLPESGFRQRFVSKGRFERVMSKIPVKLITYPQPGLLGAAAAYANKY... | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 34897
Sequence Length: 324
Subcellular Location: Cytoplasm
EC: 2.7.1.2
|
Q89DN1 | MSRKYFGTDGIRGRANGLITPELALKVGQAAGLAFQRGDHRHRVVIGKDTRLSGYMIEYAMVAGFTSVGMDVLLVGPMPTPAVAMLTKSMRADLGVMISASHNLFEDNGIKLFGPQGFKLSDDVEKQIEQLLDEPIDKRLAQSASLGRARRIDGVHDRYIEFAKRTLPRDLSLDGLRVVVDCANGAAYKVVPEALWELGADVVPIGVEPDGFNINKDCGSTSPEALSKKVREMRADIGIALDGDADRVILVDERGHVVDGDQLLAVIAQSWKEDGRLSRPGIVATVMSNLGLERFLKGQGLDLVRTPVGDRYVLEQMLSG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Mass (Da): 48276
Sequence Length: 447
EC: 5.4.2.10
|
C0ZIM8 | MGKYFGTDGVRGVANTQLTPELAFKIGRVGGYVLTRHKQEGKPKVVIGRDTRISGQMLENALLAGLLSVGAEVVRLGVISTSGVAYLTRALGADAGVMISASHNPFPDNGIKFFGSNGFKLSDEVEAEVEQYLDAAEDTMPRPTGEQIGTVLEFLEGGQKYLSHLKSTVSERFDGLKVVLDCANGAVSSLAARLFADVDAEVITIGANPNGININDQCGSTHPERLVEEVLKHKADLGLSFDGDADRCIAVDNNGEIIDGDYIMAICARALKAKGKLNNNTVVTTVMANMGFFKGMEECSINTTKTAVGDRYVVEEMLRG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Mass (Da): 47996
Sequence Length: 448
EC: 5.4.2.10
|
Q8Y5E6 | MGKYFGTDGVRGVANSELTPELAFRLGRMGGYVLTRHVGEHPRVLVARDTRISGEMLESALIAGLVSVGIEVMRLGVISTPGVAYLTKAQGASASVMISASHNPVDDNGIKFFGSDGFKLSDDQEEEIEQLLDTAEDTLPRPSGEGLGTVSDYFEGKQKYIQYLKQTIENDFNGYHIALDCANGATSGLATHLFADLDADISSMGASPNGLNINDGVGSTHPEALAAFVLDKKADVGLAFDGDGDRVIAIDEIGQIVDGDKIMFICAKYLREQGLLNNNTIVSTVMSNLGFYKGLKELEIEDVQTAVGDRYVVEAMREGN... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Mass (Da): 48488
Sequence Length: 450
EC: 5.4.2.10
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C4XU39 | MDNKLFGTDGLRGRVNAYPMTPDVVMRLALSAGLHFRNGSRRHKVLIGKDTRRSGYIYEYALSSGFCAAGMDVFLTGPLPTPAISFLTRDMRADVGVVISASHNPACDNGIKFFDHMGFKLPDAVEAEIAARVEGYAQDWRLPDPDHVGRAFKLEDSPGRYNVFLKNSIPLDVNFEGLKIVLDCAHGAAYRVTPQVFEELGAKVIKIGVDPDGSNINQRVGSLFPQQVARMVAEAEADIGIALDGDADRVIVADEKGRILDGDQIMAICALDLMERGALPGNLLVATVMSNMALEVFMKDHGGRLLRTPVGDRYVVEAMR... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Mass (Da): 48501
Sequence Length: 450
EC: 5.4.2.10
|
Q027B2 | MAKDLFGTDGIRGVAGQYPLDRDTVYAFGVALGKDAALHAAKPEILIGADTRESGTWIAELVAGGLASQGAQVRYAGVITTPGVAYLTRTGSFVAGVMISASHNPYDDNGLKVFGHSGFKLPDDEELLIEQEIFRLREAPVAPQPLSLTVEEPLVRQYLKYLSGISSVRLDGVRVAIDCGNGASYRLAPELFQGLGADVVTICCEPNGRNINLNCGALHLEALQQAVVAHRAHFGVAFDGDADRAIFVSSSGQVVNGDAVLLACGRALKAAGKLAGNTVVSTVMSNLGLERAFDAAGIRMVRTPVGDKYVLEEMVRLGAA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Mass (Da): 47468
Sequence Length: 446
EC: 5.4.2.10
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A9G862 | MPKHTKKDPREGAPSATGEPQKQAAGRKLFGTDGVRGVANQPPMTPEMALRLGRAIAFVASHGKSRQVRVVIGKDTRLSGYMLETAIASGVCAMGGRVMLSGPIPTPAVAQLTQSMRADAGVVISASHNPYQDNGIKIFGPDGYKLPDTAEEEIERLMESHELDEARVVGAAIGSAVKLDDARGRYVVFCKNTFPTALSLDGVKIVVDAAHGAAYRVAPSVFTELGANVTALGVKPNGRNINRETGALHPEHVKAEVLKRGAAIGIALDGDADRVIMVDERGEVVDGDAIMALCALRMLRTGKLPRNTIVTTVMSNLGLE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Mass (Da): 51042
Sequence Length: 480
EC: 5.4.2.10
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O26273 | MCGIVACILKDGSAAPVLLECVRRLEYRGYDSVGIATSDPMIRIKKDSGKIDEVDAELDLADLPGTMGIAHVRWATHGLPTAENAHPHTDCSGEIAVVHNGIIENYLEVKEELESEGHIFRSETDTEVIPHLIEKYMDEGMDLEAATATALRKLRGAYAIAAVSSREPGRIVGARKESPLIVGVGEGEYFLASDVPAILNHTSRVIYLDDGEMVILDGDLRVTDMEGNTVEKEVHSIDWSADMAEKGGYDHFMLKEIHEEPSAVRDTLTEWDEVLGVVEEIGEVERICFVACGTSYHASLVGKYLFESLLGIPTDVILAS... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 63995
Sequence Length: 590
Subcellular Location: Cytoplasm
... |
O68956 | MCGIVGYVGHRPARDIVVDALRRMEYRGYDSAGIALIDGNGGLTVRRRAGRLANLEATLAETDSNDGDGLGGSTGLGHTRWATHGRPTDRNAHPHRDAAGKIAVVHNGIIENFAPLRAELEAAGVEFASDTDTEVAVHLVARQYTQGDTAGDFPASVLAVLQRLEGHFTLVFASADDPGTIVAARRSTPLVLGIGDGEMFVGSDVAAFIEHTRDAVELGQDQAVVLTADGYRITDFAGNDHLEAGRDFREFHIDWDLNAAEKGGYDYFMLKEIAEQPSAVADTLLGHFDKNRIVLDEQRLSDQELREIDKVFIVACGTAY... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 67903
Sequence Length: 628
Subcellular Location: Cytoplasm
... |
Q9K1P9 | MCGIVGAIRAHHNVVDFLTDGLKRLEYRGYDSSGIAVNTDGKIKRVRRVGRVQLMEDAAREKGISGGIGIGHTRWATHGGVTEPNAHPHISGGMIAVVHNGIIENFESERKRLEGLGYRFESQTDTEVIAHSINHEYAQNGGRLFEAVQEAVKRFHGAYAIAVIAQDKPDELVVARMGCPLLVALGDDETFIASDVSAVIAFTRRVAYLEDGDIALLASDGIKRLTDKNGLPAERKVKVSELSLASLELGLYSHFMQKEIHEQPRAIADTAEVFLDGGFIPENFGKDAKSVFESIRSVKILACGTSYYAALTAKYWLESI... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 66619
Sequence Length: 612
Subcellular Location: Cytoplasm
... |
Q6CYJ9 | MCGIVGAVAQRDVAEILLEGLRRLEYRGYDSAGLAVVDSEGHVARLRRLGKVQVLSQAAEEHELHGGTGIAHTRWATHGEPSEENAHPHISEHITIVHNGIIENHEPLRELMIGRGYRFVSETDTEVVAHLVHFEQKQNGGTLVEVVKRVIPQLRGAYGMVVLDNRDSSVLVAARSGSPLVIGRGVGENFIASDQLALLPVTRRFMFLEEGDVAEITRRDVRVFDKSGQLATREEIESKVSYDAGDKGAYRHYMQKEIYEQPMAIKNTLEGRFSHGEINLSELGPKADELLAKVEHVQIIACGTSYNSGMVSRYWFEALA... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 67000
Sequence Length: 610
Subcellular Location: Cytoplasm
... |
Q9HT25 | MCGIVGAIAERNITPILIEGLKRLEYRGYDSAGVAVFDNEGRLQRCRRVGKVASLEEGLAGTPLLGRLGIAHTRWATHGAPTEGNAHPHFSSDEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSIGDLTLALKDAVKELHGAYGLAVISAAQPDRIVAARSGSPLVIGLGLGENFLASDQLALRQVTDRFIYLEEGDIAEIRRDSVRLWDVQGNDVQRETVQYHEGAEAADKGEYRHFMLKEIHEQPSVVQRTLEGRLGQNQVLVESFGPQAAELFAKVRNVQIVACGTSYHAGMVARYWLESLT... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 66295
Sequence Length: 611
Subcellular Location: Cytoplasm
... |
A4XIS1 | MSKKSTFIILAAGEGKRMKSKYSKVVQKIMGKPMILYIIDEIEKNFEDGRIVVVVGNKKEDVYKVLEGRNVRFAYQEKQLGTAHAVMCAMSEISDDSEDVFVLYGDVPFIKADTLKKLSQKRKEEAAALCLLTAIFENPYGYGRIIADENGNVLKIVEERDATEEQRKIKKINPGFYCFEKQELVNVLSKIDNKNSQNEYYLTDAIEILNRSGKKVVKVTVEDNFEVMGINSRYELFVAEQELKLRINKEHLSKGVQIIDIYSTYIHPDAQIGKDTVIYPGTFILGKTSIGEDCVIGPQSYIVDSKIGNNCHILFSVIEN... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q9PPA2 | MKTSILILAAGLGTRIKSQKPKVLQELCQKSMILHILKKAFALSDDVSVVLSHQKERVEKEILEYFPKTQILEQDLQNYPGTAGALSGFEPKNERVLILCGDMPLVEQTSLEALLGNNAKLNLAVFKARDPKSYGRVVIKNDSVEKIVEFKDANTQEKEINTCNAGVYVIDSRLLKELLPLIDNNNAAKEYYLTDIVKLAKEKDVMIKAVFVDEDEFMGINDKFELSIAENFMQKKIKKYWMQQGVIFHLPQSTFIGADVEFVGECEVYENVRIEGKSKIINSIIKSSSVIENSIVENSDVGPLAHLRPNCELKNTHIGN... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
A0R3C7 | MTASTEAAVVVLAAGAGTRMRSDTPKVLHTLAGRGMLAHVLHTVSEIDARHLVAVLGHDRERIAPEVARLSEELGRAIDVAVQDQQLGTGHAVNCGLTALPHDFAGMVVVTSGDVPLLDTATLTGLITSHGSGDAAATVLTTTLPDPTGYGRILRTQDHEIIGIVEQADATESQRTICEVNTGVYAFDIADLRSALTRLRSDNAQHELYLTDVVEILRQDHRTVRALHVDDSALVTGVNDRVQLSDLGKVLNRRIVAAHQRAGVTIIDPGSTWIDIDVQIGQDTVVHPGTQLLGATRVGSHCVIGPDTTLTHVTVGDGAS... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q1DCI1 | MSVLAAVVLCAGKGTRMKSEKAKVLHPILGRPLCAYPLKRALELGATSVVPVVGHQAEAVEKAVRGLFPDAPLRFALQREQRGTADAVRSAEEALKGYSGRVLILYGDVPLLRRETLEALLAAHDQAGGKLAMVTTTLEDPTGYGRVIRDGGKVTRIVEHKDCTPEQRAVRECNAGIYSVDADFLWKALAEIKPQNAQGEYYLTDLVEMAAKRGPVGSVEADATETAGVNDRVELAARARVLQQRINEAHMRAGVSLQDPATAYIEEGVTVGPDTEIGPSVTLAAGTVVGKGCTIGQGSVLHASTVADGTVIKPYSVLEE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q67JC8 | MSDITAVLLAAGHGTRMKSDLIKVMHPLAGKPMIGHIVDNVRRAGLEDIVVVVGYQQERIREYLGDRVRYAVQSEQLGTGHAVLQAAGLIDETEGGHVLVMYGDNPFIGPELIERLIRAHVEADAAASLLTAELADPGALGRILRDPATGAFLGSVEYKDATPEQRRIREIWTGVAVFRRAGFTALLNRLDRNNAQGEYYLPQVWEILLQRGEKVQALLLASEEDALAPNDRVELARAEARLRRQINERHMRNGVTIINPDATYIDEDVEIGRDTVIWPFTFIHGKTVIGPHCKIGPMTTIVSSTVAEGCVVEQSVVEES... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q2JII9 | MAERELSVAILAAGKGTRMRSQLPKVLHKLGSLSLIERLLRTVLTLKPHRCLVVVGYEQEQVRQALREYPVEFVEQAQQLGTGHAVQQLLPVLGGFQGDLLVINGDVPLLRAETLQALVERHRQVNPEVTLLSAQVADPYGYGRVFCDAQQRVLELVEERDCTPAQRQNRRINSGVYCFHWPALAQVLPHLNRNNAQQEYYLTDAVKRVGKAIALDVADPQEIVGVNDRRQLAQAYQILQDRLKEAWMEAGVTFVDPDSSSLEETVELAPDVVIEPQTHLRGVCRIGPGTRLGPGSWIESSEIGSGCHILYSVVSHSRIG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
P25462 | MAQAVVPAMQCRVGVKAAAGRVWSAGRTRTGRGGASPGFKVMAVSTGSTGVVPRLEQLLNMDTTPYTDKVIAEYIWVGGSGIDIRSKSRTISKPVEDPSELPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRGGNNVLVICDTYTPQGEPLPTNKRHRAAQIFSDPKVGEQVPWFGIEQEYTLLQKDVNWPLGWPVGGFPGPQGPYYCAVGADKSFGRDISDAHYKACLYAGINISGTNGEVMPGQWEYQVGPSVGIEAGDHIWISRYILERITEQAGVVLTLDPKPIQGDWNGAGCHTNYSTKTMREDGGFEEIKRA... | Function: The light-modulated chloroplast enzyme, encoded by a nuclear gene and expressed primarily in leaves, is responsible for the reassimilation of the ammonia generated by photorespiration.
Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 46017
Sequence Leng... |
O29313 | MVRRLRGDCMEEVERAKAVLKENNVRQVLCAFADVRGYLQMFSIPAREFVDGSAFENGIGFDGSSVRGFRTIEKSDMVWMPDASSLKIIPWIDDPIQKSAIMFGNVYEAWGTEIADCDPRGYVAKRYEDMLKSEGMSAIFGPEIEFFLFEGVDFTRLSWDMWVSPNGGAGDSWGPPRIMPISSELESGYMIRPKEGYFRPPPEDTTVEYRNELVYYLEQLGIDIEYHHHEVATAGQVELDFKPKQLVDVGDAFYLYKFAAKNIAAMHGLYATFMPKPLYLDNASGMHTHQSLWKGEPFSGEAVFADPDDEYMLSQKARYY... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Beta-glutamate is a much poorer substrate than alpha-glutamate.
Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP ... |
P34497 | MTHLNFETRMPLGTAVIDQFLGLRPHPTKIQATYVWIDGTGENLRSKTRTFDKLPKRIEDYPIWNYDGSSTGQAKGRDSDRYLRPVAAYPDPFLGGGNKLVMCDTLDHQMQPTATSHRQACAEIMHEIRDTRPWFGMEQEYLIVDRDEHPLGWPKHGFPDPQGKYYCSVGADRAFGREVVETHYRACLHAGLNIFGTNAEVTPGQWEFQIGTCEGIDMGDQLWMSRYILHRVAEQFGVCVSLDPKPKVTMGDWNGAGCHTNFSTAEMRAPGGIAAIEAAMTGLKRTHLEAMKVYDPHGGEDNLRRLTGRHETSSADKFSW... | Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 41284
Sequence Length: 367
Subcellular Location: Cytoplasm
EC: 6.3.1.2
|
Q8HZM5 | MATSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKGVEELPEWNFDGSSTFQSEGSNSDMYLVPAAMFRDPFRKDPNKLVFCEVFKYNRKPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADKAYGRDIVEAHYRACLYAGIKIAGTNAEVMPAQWEFQIGPCEGIDMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEESIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRG... | Function: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (By similarity). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of th... |
P16580 | MATSASSHLSKAIKHMYMKLPQGEKVQAMYIWIDGTGEHLRCKTRTLDHEPKSLEDLPEWNFDGSSTFQAEGSNSDMYLRPAAMFRDPFRKDPNKLVLCEVFKYNRQSADTNLRHTCRRIMDMVSNQHPWFGMEQEYTLLGTDGHPFGWPSNCFPGPQGPYYCGVGADKAYGRDIVEAHYRACLYAGVKIGGTNAEVMPAQWEFQVGPCEGIEMGDHLWIARFILHRVCEDFGVIVSFDPKPIPGNWNGAGCHTNFSTKNMREDGGLKHIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSSIHEFSAGVANRG... | Function: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine . When expressed in liver, it may be involved in detoxifying intramitochondrially generated ammonia . Also acts as glutamate decarboxylase by catalyzing the production of 4-aminobutanoate (gamma-aminobutyric... |
Q12613 | MATEAAVVSNPNTLAKYLKLDQKGSIMAEYIWIDADGETRSKSRTLKEKEYTPEDLPMWNFDGSSTGQAPGDNSDVYLKPVAVFPDPFRGSPNILVLSECWNADGTPNKYNYRHECAKLMEAHAAHEPWFGLEQEYTLLDLSNRPFGWPANGFPAPQGPYYCGVGTGKVVQRDIVDAHYKACLYSGVKISGTNAEVMPAQWEFQVGPCVGIEMGDHLWLARFLLARIAEEFGAKVSVDPKPIPGDWNGAGLHSNFSTKEMRVEGGMKHIEAAIKKLEGRHKEHIAVYGEGNEKRLTGRHETGAIDQFSYGVANRGASIRI... | Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 39963
Sequence Length: 360
Subcellular Location: Cytoplasm
EC: 6.3.1.2
|
P04773 | MATSASSHLNKGIKQMYMSLPQGEKVQAMYIWVDGTGEGLRCKTRTLDCEPKCVEELPEWNFDGSSTFQSESSNSDMYLSPVAMFRDPFRKEPNKLVFCEVFKYNQKPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLLGTDGHPFGWPSDGFPGPQGLYYCGVGADKAYRRDIMEAHYRACLYAGVKITGTYAEVKHAQWEFQIGPCEGIRMGDHLWVARFILHRVCKDFGVIATFDSKPIPGNWNGAGCHTNFSTKTMREENGLKHIKEAIEKLSKRHRYHIRAYDPKGGLDNARRLTGFHKTSNINDFSAGVADRS... | Function: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (By similarity). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of th... |
P11600 | KAQEPWFGIEQEYTLLNSVTKWPLGWPKGGYPAGQGPYYCSVGAGRSIGRDIPEVHYRCCLHAGIQISGVNGEVLPSQWEYQVGPVEGIAMGDQMWMSRYLMYRVAELFNVEVTFDPKPIPGDWNGSGGHVNFSNRQPESPPAGKQSRSSAKKLGKRHRWHIAAYGEGNERRLTGKHETSSMNDFSWGVANRGCSIRVGRMVPVEKCGYYEDRRPSSNLDPYVVTRLLVETTLL | Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 26224
Sequence Length: 234
Subcellular Location: Cytoplasm
EC: 6.3.1.2
|
Q2N784 | MTDPKVPRQRRIIDRRKLAAAVEALAEQQGEKARPAVLKVLREALEKGRDELSQRLLDRPSAGHQITAGHAFLVDQLVRVIFDHVTTHLYPVANRSSSERIAVLAVGGYGRAEMAPQSDVDIAFLHPSRRTPWCEQVTEAMLYFLWDLGFKVGQSSRTPEDMVRMAREDLTIRTALLEARFVWGDRELYDEARKRFWSEVVNGTERQFVAEKLAERDARHERMGGTRYVVEPNVKEGKGGLRDLQTLYWIGKYIHRARGAAELVDAGLLTETEYHGFRRAEGFLLAVRCHLHEITGRPEDRLTFDFQKQIAERMRFAERR... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
Q5FPT6 | MKETSFWGETPSLSFADDTDKPLSDRTASPPCDPASSLQTALDTAAAQGQTTRENVLSILRRHLGSGNATVRREFEKRRMSGIDAARALARQADDMVCALAELAAQKHESPGETLCLCATGGYGAGLLAPFSDIDILFLIPGDPTPAMTARIEFILYALWDLGLRVGHATRSIAECVRDADSDLTIRTALLDLRFLHGERGLARDLRCALGADLQNDRLCEFVMGKIAEREQRHRRFGDNPYMVEPNIKEGRGGLRDLQTLNWMGRAALGCAVSTPDRSGQPAEAPQTPSFASFGLLTDRESLRARRSWDFLWTVRLHLH... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
P43919 | MLFSPTLSSLLTPSAVKIERENLKQFELENFSCYSIFELIENRCDFYDALLIQLWQEIGLSEQQGISLIAVGGYGRREMFPLSDLDFLILVEQTPSHEIEEKITQFIQFLWDCGFEVGNSVRTLEQCELEGKQDITIATNLLEARFLTGNRPHFDVLNELVKRADFWSKEDFFNAKVQEQIERYQRYHNTAYNLEPDIKFSPGGLRDLHLLYWVALRHSGALTLEAILQSGFIYPQEYQQLQESRAFLFKVRFALHLILKRYDNRLLFDRQIKVSELLGFRGEGNPAVEKMMKCFFQALHRISLISNLLIQHYRENVLSS... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
Q31G41 | MATTTDKQVSPTSPSFVYNLDHEDRNTSLKSGRAVLTDFNEQQFVKFDKGCSIETLLKERTSFIDQLLKKIWEHFFSKDECEQLTLVAVGGYGRGELQPYSDIDLLILGENFIELQPKIVEFITYLWDIGFEVGHAVRNLEDCIEAGREDVTTATNLLEARWLAGNYEQFLSLQNLFNLKSFWPSHEFFQAKLEEQEKRHKRYNDTLYQLEPNIKESPGGLRDIQTILWVAKRHFGASSLQELMQHNFISLQEYKEIQAAYLYLNRIRFALHRLKKRHEDRLLFDHQQQLAELLNHDDRPEHNDSIKAVEAFMKPYYQNA... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
Q5QXT0 | MANVQEDKDFHGRWPDRTLQPCLKDYKALLESYQNWSAARFVTADIDELVHHRATFFDQLISQLWQQFQLEDEPASILAVGGYGRETLHPGSDIDLLILVGPENAEAEAKLSEKLGQFVTFLWDLHLDIGHSVRTIEDCFAQSENDITIATNLIESRYLSGAESLYNEFHQQLLNDFPWSSRDFYQAKLDEQKQRHQQYHSTSYNLEPNIKSSPGGLRDIQTVGWIAKRHFRTHSDENLVEYGYMTADEFVELRDCMNWLWRIRFALHLEAGKREDRLLFDFQPGVAVRLGYGNDGKASVETMMKDYFKVVLRVSELNQM... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
P41393 | MSNSLSNTVPPDLSAQPENPGEWPKSDFNCATIKALIDAFQRWLGEAFDSGIAAERLIEARTEFIDQLLQRLWVEYGFGSINDIALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGERLALLWDIKLEVGHSVRTLEECLLEGLSDLSVATNLIESRLLIGDVALFLELQKHIFSDGFWPSEKFFAAKVEEQNDRHQRYHGTSYNLEPDVKSSPGGLRDIHTLQWIARRHFGATSLDEMVGFGFLTEAERNELNECLHQLWRIRFALHLELNRYDNRLLFDRQFSVARRLRYEGESNQPIEHMMKDFFRVTRRV... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
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