ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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O14793 | MQKLQLCVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACTWRQNTKSSRIEAIKIQILSKLRLETAPNISKDVIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVETPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS | 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 latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase.
Sequence Mass (Da): 42750
Sequence Length: 375
Subcellular Location: Secreted
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P37020 | MPTTYVPINQPIGDGEDVIDTNRFTNIPETQNFDQFVTIDKIAEENRPLSVDSDREFLNSKYRHYREVIWDRAKTFITLSSTAIVIGCIAGFLQVFTETLVNWKTGHCQRNWLLNKSFCCNGVVNEVTSTSNLLLKRQEFECEAQGLWIAWKGHVSPFIIFMLLSVLFALISTLLVKYVAPMATGSGISEIKVWVSGFEYNKEFLGFLTLVIKSVALPLAISSGLSVGKEGPSVHYATCCGYLLTKWLLRDTLTYSSQYEYITAASGAGVAVAFGAPIGGVLFGLEEIASANRFNSSTLWKSYYVALVAITTLKYIDPFRNGRVILFNVTYDRDWKVQEIPIFIALGIFGGLYGKYISKWNINFIHFRKMYLSSWPVQEVLFLATLTALISYFNEFLKLDMTESMGILFHECVKNDNTSTFSHRLCQLDENTHAFEFLKIFTSLCFATVIRALLVVVSYGARVPAGIFVPSMAVGATFGRAVSLLVERFISGPSVITPGAYAFLGAAATLSGITNLTLTVVVIMFELTGAFMYIIPLMIVVAITRIILSTSGISGGIADQMIMVNGFPYLEDEQDEEEEETLEKYTAEQLMSSKLITINETIYLSELESLLYDSASEYSVHGFPITKDEDKFEKEKRCIGYVLKRHLASKIMMQSVNSTKAQTTLVYFNKSNEELGHRENCIGFKDIMNESPISVKKAVPVTLLFRMFKELGCKTIIVEESGILKGLVTAKDILRFKRIKYREVHGAKFTYNEALDRRCWSVIHFIIKRFTTNRNGNVI | 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 compartment pH to more alkaline pH under iron limitation. May also transport chloride ions through the plasma membrane.
PTM: Proteolytically processed in the secretory pathway by protease KEX2 within the first extracellular loop. However, both the N- and C-terminal products of the cleavage reaction are required for assembly of a functional channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87592
Sequence Length: 779
Subcellular Location: Golgi apparatus membrane
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Q93LK9 | MKPYGKIPDNSIKSLQDLMQLLKKSKDFITLEIASNNSSIVISYFRTLIDVNIFHEEVLTYIKEKSFNSLQDIHSVLPFENSKITNQIEDIQDSILNGYILIQYDTDKLNCLLVNVSKKEKRDITKAEIEYNIVGPQIAFVEDLDVNLNLVRRKLPTPYLQMKELKVGSLSNTTVAIVFIEGIVNDQNLQEIIKRVSQIKTDHVLDSTYLMQLIADNPNSIFPQFLNTERPDRVAAVLAEGKIALFVDGSPYAITLPTTLIDFFSTTEDYTMPWIIASFFRLLRLFAFIFSVLTTPLYVSILTYHYELIPKELLETLIISRSKVPFPPLIEALFLEITIELLREAGARLPTKVGLTVGIVGGIVIGQASVEASLTSNVLIIIVALSALSSFTAPIYRIGNTIRVIRFPFIISAHLLGLLGIVLTSSLLLARLLRTESLRRPYLFPFYPTRPTDWKDSIIRMPISAMFRRPIFSRSKQRFRFNPEEVEKNKILSRNDFDD | 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 | MKQIPIEYQVSPYMVFFLIITIQMGVGMLGFERISAKLVGNDAWISTLLFGISVNVMIWIIYQILNQGNGDIIAINQNVLGKWIGGLLNFIFLSYIVLLGATTLHTYIEVVHVWMFPSISSWVIAGAFLGLCYYIVTGGFRVVAGIGFFGIVIPSILIFTFFYPLQYADFRNLFPIAQHSFLEIMKGMKGNMFSFFGFEMLLLYYPFIKKARTSQKYAHYANLVTTIVYTYLMILTLAFFSEKQLANAIWAYLSMIKIIQFPFIERFEYIIVSVWAFFILPNVSFTLWGVSRGIKEALGIKQKYVLPVIILFIFILSFFLNNRNKINLLNTWTGQIGFVYIYVYLPVLWLIQTAKIKLRR | 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 | MKRWILFLILSVFLIGCAKTKIVDDIDLVQVAAYDTEAEGKLKGTFAISAYKGGGEGETKIYSASGQTGREVLARASEKSSGPLELGQLRVIIFNEKIIEKGMQEILETLNRNPSVGNAIYLAITNVKGESLLKGNYSKEKEIASYLSSLLEQNMNNGTQPKTNFFMFLNQLDDDARDSYLPMISKKGNVLELNGIALFKRCKMVDKVNPKDLFVFKLLTDNFKQGTYQFKLPGSSNTYATIENIKARTKYKMEGNSKHPFVNAHIQVKAEIQEFTKTKNLDNPKEIKKLEKIMGKEIEKKATTLIKRFIKKDTDPIGLRKLGRTHVRKWNSQEWEESYKHLRFRVTADVKVTQSGVTE | 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 bonds with glutamines of other spore coat proteins.
Sequence Mass (Da): 20276
Sequence Length: 181
Subcellular Location: Spore coat
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Q8GUE4 | MALQMIAPFLSSFLPNPRHSLAAHGLTHQKCVSKHISCSTTTPTYSTTVPRRSGNYKPSIWDYDFVQSLGSGYKVEAHGTRVKKLKEVVKHLLKETDSSLAQIELIDKLRRLGLRWLFKNEIKQVLYTISSDNTSIEMRKDLHAVSTRFRLLRQHGYKVSTDVFNDFKDEKGCFKPSLSMDIKGMLSLYEASHLAFQGETVLDEARAFVSTHLMDIKENIDPILHKKVEHALDMPLHWRLEKLEARWYMDIYMREEGMNSSLLELAMLHFNIVQTTFQTNLKSLSRWWKDLGLGEQLSFTRDRLVECFFWAAAMTPEPQFGRCQEVVAKVAQLIIIIDDIYDVYGTVDELELFTNAIDRWDLEAMEQLPEYMKTCFLALYNSINEIGYDILKEEGRNVIPYLRNTWTELCKAFLVEAKWYSSGYTPTLEEYLQTSWISIGSLPMQTYVFALLGKNLAPESSDFAEKISDILRLGGMMIRLPDDLGTSTDELKRGDVPKSIQCYMHEAGVTEDVARDHIMGLFQETWKKLNEYLVESSLPHAFIDHAMNLGRVSYCTYKHGDGFSDGFGDPGSQEKKMFMSLFAEPLQVDEAKGISFYVDGGSA | 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 (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Plastid
EC: 3.1.7.11
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Q6USK1 | MSCARITVTLPYRSAKTSIQRGITHYPALIRPRFSACTPLASAMPLSSTPLINGDNSQRKNTRQHMEESSSKRREYLLEETTRKLQRNDTESVEKLKLIDNIQQLGIGYYFEDAINAVLRSPFSTGEEDLFTAALRFRLLRHNGIEISPEIFLKFKDERGKFDESDTLGLLSLYEASNLGVAGEEILEEAMEFAEARLRRSLSEPAAPLHGEVAQALDVPRHLRMARLEARRFIEQYGKQSDHDGDLLELAILDYNQVQAQHQSELTEIIRWWKELGLVDKLSFGRDRPLECFLWTVGLLPEPKYSSVRIELAKAISILLVIDDIFDTYGEMDDLILFTDAIRRWDLEAMEGLPEYMKICYMALYNTTNEVCYKVLRDTGRIVLLNLKSTWIDMIEGFMEEAKWFNGGSAPKLEEYIENGVSTAGAYMAFAHIFFLIGEGVTHQNSQLFTQKPYPKVFSAAGRILRLWDDLGTAKEEQERGDLASCVQLFMKEKSLTEEEARSRILEEIKGLWRDLNGELVYNKNLPLSIIKVALNMARASQVVYKHDQDTYFSSVDNYVDALFFTQ | 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 is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Plastid
EC: 3.1.7.11
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E8W6C7 | MTSQASAPKIPQLWVPLPSGIHPSWREIDQGSAAWLDRFGLYSDHAQRERLTRISVGEITGRGGPDGRLAALQWTADFLMWLFAFDDEYCDEGPAAASPDATLLIITKLQRIVEVPWAAPADDNYSAALLELRLRLDDLTTPVQTARWAASFRAYLQGQIWMAANSTYGRIPTLSDHLAVRLDSSGVKIFSTLSEIIHGYDLPAADYDRHDVRGFVEVFAAIIGWSNDLVSYHKERRRSQDSYGNVVDLIAHERQCSVEEAVSETATMHTRAMALYLRLRDQILRDAEPELRKWITDCDSWIRADYDWSLTTHRYVNPDDPADLPVGSAEAPFRAREADQPLPIASVSWWWTLLKD | 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 cation. The only accepted substrate is farnesyl diphosphate (FPP).
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = (+)-(1(10)E,4E,6S,7R)-germacradien-6-ol + diphosphate
Sequence Mass (Da): 40241
Sequence Length: 356
Domain: The Asp-Asp-Xaa-Xaa-Xaa-Asp (DDXXXD) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 4.2.3.166
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Q0UP11 | MASAALIDSDMEPTLQPILDQKTLRWIFVGGKGGVGKTTTSCSLAIQLAKHRKSVLLISTDPAHNLSDAFNQKFGKDARLINGFDNLSAMEIDPNGSIQDLLAGGGESGEDAMAGLGGMGNMMQDLAFSIPGVDEAMSFAEVLKQVKSMSYEVIIFDTAPTGHTLRFLQFPTVMEKALSKVSQLSRQFGPMLNSFLGGGGRLPNGQNIDELVEKMEALRGTISEVNGQFKDADLTTFVCVCIPEFLSLYETERMIQELNSYEIDTHSIVVNQLLFPKQDNPCEQCNARRKMQKKYLEQIEELYDEFNVVKMPLLVEEVRGKEKLEK | 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 protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
Sequence Mass (Da): 36029
Sequence Length: 326
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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B2VVF0 | MASAALIDADMAPTLQSILDQKTLRWIFVGGKGGVGKTTTSCSLAIQLAKHRKSVLLISTDPAHNLSDAFNQKFGKDARLVNGFDNLSAMEIDPNGSIQDLLASGAEEGQDPMAGLGGMGSMMQDLAFSIPGVDEAMSFAEVLKQVKSMSYEVIIFDTAPTGHTLRFLQFPTVMEKALSKVSQLSRQFGPMLNSFLGASGRLPNGQNMDELIEKMENLRETIGEVNGQFKDADLTTFVCVCIPEFLSLYETERMIQELNSYEIDTHSIVVNQLLFPKQDNPCEQCNARRKMQKKYLDQIEELYDEFNVVKMPLLVEEVRGKEKLEKFSEMLVKPFVPPQ | 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 protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
Sequence Mass (Da): 37663
Sequence Length: 339
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q9P7F8 | MSFDPLPGTLENLLEQTSLKWIFVGGKGGVGKTTTSCSLAIQMSKVRSSVLLISTDPAHNLSDAFGTKFGKDARKVPGFDNLSAMEIDPNLSIQEMTEQADQQNPNNPLSGMMQDLAFTIPGIDEALAFAEILKQIKSMEFDCVIFDTAPTGHTLRFLNFPTVLEKALGKLGGLSSRFGPMINQMGSIMGVNANEQDLFGKMESMRANISEVNKQFKNPDLTTFVCVCISEFLSLYETERMIQELTSYEIDTHNIVVNQLLLDPNTTCPQCMARRKMQQKYLAQIEELYEDFHVVKVPQVPAEVRGTEALKSFSEMLVKPYVYPTSGKE | 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 protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
Sequence Mass (Da): 36548
Sequence Length: 329
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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A7EHP6 | MSTAVINTDDDQLEPTLQSILDQKSLRWIFVGGKGGVGKTTTSCSLAIQLAKVRRSVLLISTDPAHNLSDAFSQKFGKEARLINGFENLSAMEIDPNGSIQELMGQAEEGEGPAAGMGGMMQDLAFAIPGIDEAMSFAEVLKQVKSLSYETIIFDTAPTGHTLRFLQFPTVLEKALAKVSQLSTQFGPMLNGLLGANGSLPNGQNLGEMMEKLEGLRETISEVNGQFKDENLTTFVCVCIPEFLSLYETERMIQELSSYHIDTHCIVVNQLLFPKKGSDCDQCNARRKMQKKYLEQIEELYDEFNVVKMPLLVEEVRGKERLEKFSEMLITPYVPPAGGL | 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 protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
Sequence Mass (Da): 37544
Sequence Length: 340
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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C4JZ54 | MSSAVVPADDILEPTLQNILDQKSLRWIFVGGKGGVGKTTTSCSLAIQLAKVRKSVLLISTDPAHNLSDAFGQKFGKEARLIDGFDNLSAMEIDPSASMQDLMAAGGDQAEDMGFGLGGMMQDLAFSIPGVDEAMSFAEVLKQVKSLSYEVIVFDTAPTGHTLRFLQFPTVLEKGLAKLSQLSSQFGPMLNSVLGARGGLPGGQNLDDVLSKMESLRETISEVNTQFKNADLTTFVCVCIAEFLSLYETERMIQELTSYHIDTHAIVVNQLLFPGKDSTCDQCKARRKMQKKYLNEIEELYEDFNVVRMPLLVEEVRGKEKLERFSDMLVHPYQPPQE | 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 protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
Sequence Mass (Da): 37303
Sequence Length: 338
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q0IIZ2 | MAAPADDEFEDAPDVEPLEPTLSNVIDQRSLRWIFVGGKGGVGKTTCSCSLAVQLSRVRESVLIISTDPAHNISDAFDQKFSKVPTKVRGYDNLFAMEIDPSLGVAELPDEIFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCSIDTHNIIVNQLVFPEPEKPCRMCEARHKIQSKYLDQMEDLYEDFHIAKLPLLPHEVRGAENVNTFSKLLLEPYKPPSGK | 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, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-CAMLG receptor, and returning it to the cytosol to initiate a new round of targeting.
Sequence Mass (Da): 38331
Sequence Length: 342
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q84L08 | MSSSRFDSNKQLTTSSLVIGYALCSSLLAVINKLAITYFNYPGLLTALQYLTCTVAVYLLGKSGLINHDPFTWDTAKKFLPAAIVFYLAIFTNTNLLRHANVDTFIVFRSLTPLLVAIADTVFRSQPLPSRLTFLSLVVILAGAVGYVATDSSFTLTAYSWALAYLVTITTEMVYIKHMVSNIKLNIWGLVLYNNLLSLMIAPVFWFLTGEFTEVFAALSENRGNLFEPYAFSSVAASCVFGFLISYFGFAARNAISATAFTVTGVVNKFLTVVINVLIWDKHATPVGLVCLLFTICGGVGYQQSVKLDKPIEKVSEKDSEKGEEDEELTQLVPGKLASVV | 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 cytoplasm into the Golgi lumen .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37386
Sequence Length: 341
Subcellular Location: Golgi apparatus membrane
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P92916 | MDAQDIESRHPLIGARPRRRALRSLSILLAAALLLGLVLFYANGTGSGTAVDPVRVDNEFPWTNDMLAWQRCGFHFRTVRNYMNDPSGPMYYKGWYHLFYQHNKDFAYWGNITWGHAVSRDLINWQHLPVAVGPDHWYDISGVWTGSIIVVSEDRVVMLFTGGTKSFDQSINLAEAADPSDPLLLKWIKYDNNPILWPPPGIVRDDFRDPNPIWYNASESTYHIVVGSKNDSLQHTGIALVYLTKDFKKFDLLPTVLHSVDKVGMWECVEVYPVATTGPLLHKAIDNFDVDRVLDRSTVKHVLKASMNDEWHDYYAIGTFDPIGNKWTPDDETVDVGIGLRYDWGKFYASRTFFDPLKQRRIIWGYIGEVDSQKADIAKGWASLQGIPRSVLYDVKTGTNVLTWPIEEMEGLRMARKDFSGIKIKKGSTVELSDFGDAFQIDIEAEFTISKEALEATIEADVGYNCSSSGGAAIRGTLGPFGLLVLANQDLTENTATYFYVSKGIDGSLITHFCQDETRSSKANDIVKRVVGGTVPVLDGETFAVRILVDHSVIESFAMGGRTSATSRAYPTEAINSAARVFLFNNATGVDVIAESVKIWQMNSTYNDFYHF | 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-beta-D-fructofuranosyl-(2->1)-]m+1 alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 alpha-D-glucopyranoside = [1-beta-D-fructofuranosyl-(2->1)-]m alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0, n >= 0).
Sequence Mass (Da): 68631
Sequence Length: 612
Subcellular Location: Vacuole membrane
EC: 2.4.1.100
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I3L273 | MKSFSRILFLVFLLAGLRSKAAPSAPLPLGCGFPDMAHPSETSPLKGASENSKRDRLNPEFPGTPYPEPSKLPHTVSLETFPLDFTEPLNPDLRETPHPESPETPKADSLTTSISESLDMPKTNLSKMAHPESSETPTPGPTEMPHPGSPETPKPNFSKTSRPEFPETPNTDLMQTTPQESPEILQLNATEVSQAELPETSNTNPTKTPDPKSPEKHDLNSTETPNSEFLQALHPDPSKTPHPESHVTHNPSPTEISQTEFPTTYYQNATDVPRTSDPQISTSLYPETPVPFKDDATALNELSLNPKPGTPAAIQPDSPKLPTSDSPGMVELKAPQNSGPKESNVPPPSARIAGPPALPGRPSQLAPATLRAPQRHSRGEGVNTIIVVERVKETGVTLVGRPRGAAGGALCLFFAGTALLIGIFVLLWCLYRRAARQRPFAHHRLPDDGDEPVLHLDAPKDPYDLYFYAPDTWVPSHIATKQPPPTPPLPPKLPPPPRGGRPQRLEALSPATLPNNFV | 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 | MQPFSPIFFHLLFLLNGLSSRAAPSPGQPVVADLQGMLQPSGMPTGTLENLTRDQPTPGSSASHPPEHSETPPSASPHISTKILRETPSPSPFLSLETPIPDQLTSVAESQGTSQMSPSRATLGKPSETPKPDPTGISPSDSPETPKPNPSNTSPPESPESVYTDPTPTLHHESPEISKRDTPKLSPGEESKIPSPRPTQFLSSKSLETYDPSATRHLNSALEPTTHPDPTESPQSVFLTTHNSNPTVVPQTQFPTSPSQNVTETARTSDLEPSSSLPTQPTTFREEATTPSEPGLSPSPEAPAVTRVATPGLSTSDSPGTKELHVPQNSDPKGPDIPLPSARIAGPPAPLEHPNQVAPAPQRHSRGDTVNTIIVVERVKETGVTLVSRPRGSVGGALCLFFAGTGLLIGIFLLLWCLYRRASRHRSFAHHRLRDSGDEPVLHLDAPKDPLDLYFYAPDAWVPSHIATQPPPSTPPLPPKLPPPPRGPQRLEALSPAALSPNFF | 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 | MAAPARTPRSRILGCSSMLRFLRNLVGSKGGSKSTNKPLTRSQPSSSWEQDVVSPMMGHQGGRGRKEPRAKVHSAASSNGKREPPPRVLSAAPSNPRHDAFELGTGDSGSQTLTSKDVPKLRAQGVEVTSVPLRGTWEVLEQLPEKKGEEEEPVGEVSGASDREHFGQALETEQGCLQWVPGPLALTPGAFIKEEEDEHCPIEFGDLKPSSCKVGSTPWNYLLGLYKQLQKSAMAKAQRPAAPQLALKDGLPHEEKGEREEAVDESCPKWCAPRASSDESCPKWCAPRASTYQSPLQKKFRSTDTVGFVESELKKILSVQREARLWKVGNPEGRELLTQPDITLEEAGMVDGQHLLLEEMDEMGNWPPPD | 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 the mitochondrion.
Subcellular Location: Cytoplasm
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Q5J2D6 | MAAQARTPRSRILGCSSMLRFLRSLVGSKGSSKSSNRPLNRSQPSSSPEQDVVSPTMGHQGGCGRKETRPRVLSATSSNGKREPRPRVLSAAPSNQRLRDASGLGTGDTGSQTLTSKDVLKLRAQGVEVTSVPTRGTWEVLEHLPEKKGEEGEPAGEVSGASDRAHFGQALEAEQGCLQWVSGPMVLPPEAFIKEEEDEHCLIDFGDLRLSSCKVGSTPWNYLLGLYKQLQKSAMTKAQRPDADAPQFALKDSSPTEERGEREEAVDESSLKWCAPRASSDDSNLKWCAPRNSTYQSPLQKTFRSTDTVGFVESELKKILAVQREARLWKVGNPEGRELLTQPDITLEEAGMVDGQHLLLEEMDEMGNWPPPE | 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 the mitochondrion.
Subcellular Location: Cytoplasm
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E4PMA5 | MLLKNAVQLICYPDRIGNNLKDLYTVVDTHLSEAIGGLHILPFFPSNADGGFSPLTHKEVDPKVGTWDDIEAFTAKYDLCVDLTVNHISDESPEFTDFIANGFDSEYADLFVHVDKFGEISPDDMAKIHIRKEKEPFREVTLSDGTKTRVWCTFTEQQIDLNYESDLAYQLMESYIGFLTSKGVNLLRLDAFGYTTKRIGTSCFLVEPEVYQILDWVNQVALKHGAECLPEVHDHTSYQYAISRRNMHPYGFALPPLLLYSLLDANSTYLKNWLRMCPRNMVTVLDTHDGICIPDVEGVLPDEKIKVLIDNIDARSADPIMRRSAANIHSVGAIYQLTCTFYDALMQNDDAYIAARAIQFFTPGIPQVYYVGLLAGCNDHELMEQSGELRDINRHYYTLEEVEQDIQKPVVQRLLSLMKFRSNYPAFDGHFELNYSNNSSVAMAWRHGDYYCHLFVDLNFKTVKVTYTDVETGETRHLEC | 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 degrading it when the environmental conditions change. Cannot catalyze the phosphorolysis of sucrose or glucosylglycerate.
Catalytic Activity: 2-O-(alpha-D-glucopyranosyl)glycerol + phosphate = alpha-D-glucose 1-phosphate + glycerol
Sequence Mass (Da): 54825
Sequence Length: 480
EC: 2.4.1.359
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Q8ECL7 | MHNIHRRHFLKAAGAVTAGLVTANIALNANASSVAPKPSSGKSVIGLIAPKMEVVRVGFIGVGERGFSHVEQFCHLEGVELKAICDTHQAVVDRAVEHIVKQKRPKPAVYTGNDLSYRELLNRDDIDIVIISTPWEWHAPMAIDTMESGKHAFVEVPLALTVEECWQIIDTAERTQKNCMMMENVNYGREELMVLNMVRQGLFGELLHGEAAYIHELRWQMKEINHKTGSWRTYWHTKRNGNLYPTHGLGPVSQYMNINRGDRFDYLTSMSSPALGRALYAKREFPADHERNQLKYINGDMSTSLIKTVKGRTIMVQHDTTTPRPYSRHNLIQGTNGVFAGFPNRIAVENDGFGTSYHKWDTDMQKWYDKYDHPLWQRIGKEAEINGGHGGMDFVMLWRMVYCLRNGEALDQDVYDGASWSVVNILSEQSLNNRSNSVNFPDFTRGAWEHAKPLGIVGA | 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-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids.
Sequence Mass (Da): 51965
Sequence Length: 459
EC: 3.2.1.49
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Q01S58 | MDKTSRRDLLKLASLAGIGAGLARSQGSSKSMAGVSFKPNGTVRIGVIGTGGRGGSLIENFSAVEGVQITALCDTVKDKVLKQQAWLDKAGKASHPIALFHSDDHAFENLVKRDDVDLVVVSTPWVWHTRMAVAAMKQGKHVAVEVPAARTIDECWELVNTSEATQRHCIQLENCCYGYNEMMVLNMVRAGLFGELTHGGAAYNHDLRSILFSAEGEGEWRRFEHLNRDGNLYPTHGLGPVAHYMDVNRGDRFDTLVSMSSISASLQQYRKEKIPAGDPRQKEVYKEGDFNVSLIRTVKGRVIELEHNVSSPQPYDRINLIAGTKGIFRDYPPRIYFDGARREDFETLDRYKEKYEHPLWKKVGELAKELGGHGGMDFVMAYRLIQCMKEGTPPDIDVYDAAAWSAPGPLSEASVANGSAPQKFPDFTRGKWQTRQPV | 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 | MSQTPAVSRRLLLGSAAATGALATGIGSAAPVAAAEQAPRRRPGQKSMIGVPFAAHPTVRVAVIGLGNRGGGMITGWAAVPGCTVTAVCDIRADRAERAADRLESKGNPRPAEYGGSADSYARMLRRDDIDLVYIATPWEFHYEHGRAALLSGRHAVVELPVATELRQLWDLVDTSERTRRHLLLSENCNYGRNELAMLKAAHDGLFGDLTNGHGGYLHDLRELLFSDTYYTDSWRRLWHTRSTASFYPMHGLAPIAAAMDVNRGDRMTTLRATTTAPKGLADYRARFVPRDHPSWKETYINGDLVTCMIETAKGRTVRAEHDVSSPRPYSRINTLAGSRGIVEDYAGSAPTGARIYVEPDHGGHTWRDFETYRKEYDHWLWQKVGDDAANNGGHGGMDYVLQWRTVQLMRAGLVPDIDVYDSAAWCSPVPLSVTSLARGGRPVEIPDFTRGAWRERRPGLDSAPTDMPPAG | 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 Length: 472
EC: 3.2.1.-
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B2FLK4 | MFAMKRREFIAASAAVAASSLLPQTPAWARGRKVRLAMIGTGMRGLVLLKELVRRDDVEVVALCDIEPIMLGRAMDMVAKAGKPAPKTYGQDRDTHAWKRLLEQKGIDGVIIATPWEYHAPMAIAAMQAGVAVGCEVVAGITLQDHWDVLKTQLSTGTPYMLLENVCYRRDVMAALQMVRQGLFGELVHLQAGYQHDLRGVKFNSGDPNQPYDSGVEFGPKGWSEARWRTEHSVERNGELYPSHGIGPCAMYTGINRGNRFTHINAFATKARGLHEYTVAKSGGTTHPSTKVKFKLGDIVTTTLACENGETILLQHDTSLPRPYSMGFRVQGTKGLWMDVNHSIHIEGRSPPHQWEEFKKYQDEYEHPLWKQNADTAASAGHGGMDWFVIHAFVEALKAKAPMPIDIYDAVTWSAITPLSEQSIANSFQTLEFPDFTAGAWKQRKPIFAFDGKY | 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 | MNDAAPQNPGQDEAKGTGEKDNGGSMSPRSALRTTAGVAGAGLGLSALGTGTASASVPEAAQTAVPAAESDESAAPKRQGRTMAGVPFERRSTVRVGIIGLGNRGGSMIDLFLAVPGVRVVALCDTVRDKAASAAAKVVKAGQPAPAVYTKDEHDYEQLCARGDVDFVYVATPWDFHFEMAKTAMLNGKHVGVECPVAMRLDELWKLVDLSERTRRHCMQLENCAYGKNEMRVLRMAHAGLFGDLLHGAGAYNHDLRGLMFDPDYYEGPWRRLWHTRLRGDLYPNHGFGPVANYLDINRGDRAVSITSMGTPALGLAQYREENMPPGDASWKETYVSSDRTISLVQTAKGRVVRLEHDVSTPHPYSRINSLGGTRGVFEDYPERIYIEPDHANDEWGDFAAYADWDHWLWKEHANPPGGHGGMDYIMVFRLMQCVRLGLVPDFDVYDAATWTAPVPLSHASIKANGKPQQIPDFTRGEWKKSRPGTDSEKPSEP | 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 | MENTRRNFLKKVTAAGIGAAGLAVTDQAMAAVNQPGEAAQQKKKPAGKSDGMLRFGFIGTGSRCQEHINNVLGIQGNKIVAICDIQKGPLEKTLKHIAKFNVPEPKVYTGGEREFEKMLNNEEFDCVIIASPWEWHVPMAVAAMKAGVPYVGVEVSAANTVEECWDLVNVSEATGSHLNILENVCYRRDVMAALRMVREGLFGEMIHGTCGYQHDLRDVKFNDGIHYTYQEGGELRMGPTAYAEAQWRTQHSVTRNGDIYPTHGIGPVANCLNINRGNRFLSLTSMATQSRGLHNFVVDKGGANHPYAKIHFNLGDIVTSMIKCANGQTVIVTHDTNLPRPYSLGFRIQGTRGLWMNDGNHVYVEGQSKPHRWDASDDWFKKYDHKLWSTLELKAKEAGHGGMDYIMMYDFIDAIRNKKPTPMDCYDAAAWSAISGLSEMSIARGGAVVDFPDFTRGQWIHRQPAFAL | 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-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids.
Sequence Mass (Da): 51923
Sequence Length: 468
EC: 3.2.1.49
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E4Q361 | MSFPKGFLWGAATASYQIEGAWNEDGKGESIWDRFTHQKGNILYGHNGDVACDHYHRHEEDVSLMKELGIKAYRFSTAWARIFPDGFGNINQKGLEFYDKLINELVENGIEPVVTLYHWDLPQKLQDIGGWANPEIVNYYFEYAMLIINRYKDKVKKWITFNEPYCIAFLGHWHGIHAPGIKNFKVAMDVVHNIMLSHFKVVKAVKENNIDVEIGITLNLTPVYLQTERLGYKVSEIEREMVNLSSQLDNELFLDPVLKGSYPQKLLDYLVQKDLLDSQKVNNMQQEVKENFIFPDFLGINYYTRSVRLYDENSGWIFPIRWEHPAGEYTEMGWEVFPQGLFDLLIWIKESYPQIPIYITENGAAYNDKVEDGRVHDQKRVEYLKQHFEAARKAIKNGVDLRGYFVWSLIDNFEWAMGYTKRFGIIYVDYETQKRIKKDSFYFYQQYIKENS | 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), pNP-beta-D-cellobioside (pNPC), lactose, pNP-beta-D-xylopyranoside (pNPX) and cellobiose in the order of decreasing activity, respectively. Very low activity with soluble polysaccharides synanthrin and locust bean gum. Very low, but detectable activity with insoluble substrates such as cotton and filter paper. No activity with pNP-alpha-L-arabinofuranoside (pNPAr) or carboxymethylcellulose (CMC) as substrates. Synthesizes galactooligosaccharides (GalOS) from lactose. Hydrolyzes pretreated corn stover releasing both glucose and xylose. This multifunctional enzyme may provide C.owensensis the benefit of utilizing a wide variety of available carbon sources in its natural growing environment as the ability to convert a wide range of soluble oligosaccharides to monoses is required in order to assimilate them.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 53195
Sequence Length: 452
Pathway: Glycan metabolism; beta-D-glucan degradation.
EC: 3.2.1.21
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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 | MEVQCGGAGFIPESSRSSHELGNQDQGIPQLRIVLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVSTWDGKELVVVDTPGIFDTEVPDADTQREITRYVALTSPGPHALLLVVPLGRYTVEEHKATQKILDMFGKQARRFMILLLTRKDDLEDTDIHEYLEKAPKFFQEVMHEFQNRYCLFNNRASGAEKEEQKMQLLTLVQSMVRENGGRCFTNKMYESAECVIQKETLRMQELYREELEREKARIRREYEEQIKDLRDELEREIRRARMEREFKEREAIFTKNQQNARKEVENTSMILELIIKAWEIASFIFNQFMKD | 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
Sequence Length: 328
Subcellular Location: Cytoplasm
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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 and regulation of the DNA damage response occurring during T cells proliferation . Required for the survival of peripheral T cells, natural killer (NK) and NK T-cell development and the maintenance of normal liver function (By similarity). May promote the survival of mature T lymphocytes upon cytokine withdrawal (By similarity). May regulate Ca(2+) homeostasis by modulating lysosomal Ca(2+) stores, preventing its accumulation in the absence of T cell activation (By similarity). May play a role in mitochondrial DNA segregation in hematopoietic tissues (By similarity). Is a regulator of liver endothelial cell homeostasis (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 34846
Sequence Length: 307
Subcellular Location: Lysosome membrane
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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 the DNA damage response occurring during T cells proliferation . Required for the survival of bone marrow hematopoietic stem cells, as well as of peripheral T cells, natural killer (NK) and NK T-cell development and the maintenance of normal liver function . May promote the survival of mature T lymphocytes upon cytokine withdrawal . May regulate Ca(2+) homeostasis by modulating lysosomal Ca(2+) stores, preventing its accumulation in the absence of T cell activation (By similarity). May play a role in mitochondrial DNA segregation in hematopoietic tissues . Is a regulator of liver endothelial cell homeostasis .
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 34653
Sequence Length: 308
Subcellular Location: Lysosome
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Q8K3L6 | MEDHGFEELSTRTHDLNVRRLTKGNINFLLSTGQETYSVEDSGLLRILLVGKSGCGKSATGNSILRRPAFESRLRGQSVTRTSQAEMGTWEGRSFLVVDTPPIFESKIQNQDMDKDIGNCYLMCAPGPHVLLLVTQLGRYTVEDAMAVRMVKQIFGVGVMRYMIVLFTHKEDLADESLEEFVTHTGNLDLHRLVQECGRRYCAFNNKASGEEQQGQLAELMALVRRLEQEHEGSFHSNDLFVYTQVFLRGGYSEHQEPYKFYLTKVRQEVEKQKRELEEQEGSWMAKMLCRVTSCLDWHIAVSVLLIVLGLTLLITLINMYIGRWK | 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 | MSRWKVVILCLLSFMFEIGHASFQCNPKTYDGAFLNIVCVCNATFCDEIEPIGEIAEGKAIVYRSSLDGDRLKRMSMKMKEKLRKNESVNVTITIDASERFQNIFGFGGAFTDSAGDQFVSLSETLQNYIVDSYFGKNGLEYNIGRVPIASCDFSTHEYSYDDVHDDFELKHFALPDEDLKLKIPFIKKAIEKTEGNIQLFASPWSAPGWMKVTGRMRGGGAMRNDKRVYQAYADYFFKFFEAYSSHAITFWGLTIQNEPSTGADMAWRWQTMNYTAETMRDFLKKYLGPKLKENKLTETLKVMVLDDGRGLLPGWADTIFNDPEATKYADGVAVHWYGNLYSPAVLLDITQRHHPTKFIFGTEACAGYFGHHGPIMGDWFRAESYADDIITDLNHHVTGWTDWNLCLDETGGPNWAYNVVDSPIIVNRTAQEFYKQPMFYALGHFSKFLPRGSTRVFTKIEGNLAVSATSVVIEGGRRATVILSKASNSLLTRIVDSSTGFSIVLNLPPRSIHTVIWKKRK | 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 | MILNISVSLLIFLAFYGFSSDAKSLPCSEVKKEYGIVCRCNATYCDTIEPLGTVTSGKAVVYTTSRNGKRMNRSELKHTTSSTAKTKVYVNTTQSFQPVMGFGAAFTDAAGINMKMLPQTMQDQIIQQYFSDDGLGYVFGRVPMASTDFSTHEYSYDDVKFDFDLKNFNLTVEDLQYKIPFIKKAMTASGGKLKLFATPWSSPGWMKTSGRMVGAGELLGDQNGKYYQTWAQYFVKFFEAYHAQGIDFWSLTPQNEPTTGIDPLWKWQTLFFDASMERNFIKKLLGPALASSPVTKNLKIMINDDQRINLPHWPNVILTDPTAAQYVHGIAIHWYEDFIDPATVLTETHEKFPDYFLLATEACAGYFPADGPKLGSWSRAEQYANDLIKDMGNWVGGWVDWNYILDLQGGPNLAKNFVDSTIIVNATAQEYYKQPIWHVMAQFSKFVKPGAIRVGINIIEKSVDVEGLSFLNQDGTKTVVLLNKNEVLSFDVAISDVSAPNVIYDLTIQPNSLITIVYK | 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 | MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRRIY | 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 metastatic behavior of malignant cells.
PTM: Phosphorylated by PKC.
Catalytic Activity: H2O + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-D-mannosamine + UDP
Sequence Mass (Da): 79275
Sequence Length: 722
Pathway: Amino-sugar metabolism; N-acetylneuraminate biosynthesis.
Subcellular Location: Cytoplasm
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I7FJX8 | MIELDRLDLGGGRRLVITSEPDAAVPQVRDADGHWRRAGPGDGVAEAMLDALNQNPGTTKHGNFTLLSWASQTARGERPITVDQTNESVIVGDAAVVKWATHLQEGPHPAPARIKALRGNGFRGMPMPWGLVTWQTADHPETLVVTVDEYLPDAVDGWTWAVALVTDAAQDRAAVPALVDAVTAVGCVVAELHAAQADTARPATAADARSWREAALETVETAATLGTSVSGELLRARREDVEAVVGTLGDLAGIPVLAGHGDLHVGQVLRAGGRYVVTDFDGNPVLPAEARVKPVPAALDVAGMAQSLAHVAIVACKYTELAPAALADVDRLARTTFVGAYTDRLETLGHRSVYDPAPLRALRLQQVLREIIYAARHLPRWMYVPDAALPALLDEGTST | 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 bacterial GlcNAc metabolism. Is unable to phosphorylate maltose.
Catalytic Activity: ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate + H(+)
Sequence Mass (Da): 42337
Sequence Length: 399
EC: 2.7.1.8
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A0A1H7TQR5 | MTPNWSELVAAADPALVLPSGERRAEVAVPGPLRLDALLDLGEGHAVGVVRSADAARWTVPLVRDGAGGVRRSRPGDGTAEHLVAALARRGATPDAAFVLEAFTGAAPVTGERGIIVDQTNESVIVGECAVVKWAVRLPAEGEPGSPAAQRIAALARGGFTEMPRPWGLLTLAEGAQPVLLASVVAYLPGALDGWDWAVDDVRRLARGELTMDQALLPAAQLGTLTARMHAALAARGRTPATAADVAAWGVRMREELDEAVASVPGAEGERLKAWAPRIADVYAELDALAGTPLIDVHGDFHVGQILRADGRYAVVDFDGNPVLPADQRAARQPAALDVVGMTASLDHVGRVVVFRTPDVDPAPVRAWIAAAQRSFLDAYRTTLARLDADDLFDDRLLTPLRYAQEVREYLYAVRHLPHWVYVPDLSLTDLLPERLKD | 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 bacterial GlcNAc metabolism. To a lesser extent, is also active on glucose, but is unable to phosphorylate maltose, 18 other sugars and several aminoglycoside antibiotics.
Catalytic Activity: ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate + H(+)
Sequence Mass (Da): 46730
Sequence Length: 438
EC: 2.7.1.8
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O07563 | MLRGTYLFGYAFFFTVGIIHISTGSLTPFLLEAFNKTTDDISVIIFFQFTGFLSGVLIAPLMIKKYSHFRTLTLALTIMLVALSIFFLTKDWYYIIVMAFLLGYGAGTLETTVGSFVIANFESNAEKMSKLEVLFGLGALSFPLLINSFIDINNWFLPYYCIFTFLFVLFVGWLIFLSKNREYAKNANQQVTFPDGGAFQYFIGDRKKSKQLGFFVFFAFLYAGIETNFANFLPSIMINQDNEQISLISVSFFWVGIIIGRILIGFVSRRLDFSKYLLFSCSCLIVLLIAFSYISNPILQLSGTFLIGLSIAGIFPIALTLASIIIQKYVDEVTSLFIASASFGGAIISFLIGWSLNQDTILLTMGIFTTMAVILVGISVKIRRTKTEDPISLENKASKTQ | 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 | MKANKYLIFILGALGGLLYGYDNGVISGALLFIHKDIPLNSTTEGIVVSSMLIGAIVGAGSSGPLADKLGRRRLVMLIAIVFIIGALILAASTNLALLIIGRLIIGLAVGGSMSTVPVYLSEMAPTEYRGSLGSLNQLMITIGILAAYLVNYAFADIEGWRWMLGLAVVPSVILLVGIYFMPESPRWLLENRNEEAARQVMKITYDDSEIDKELKEMKEINAISESTWTVIKSPWLGRILIVGCIFAIFQQFIGINAVIFYSSSIFAKAGLGEAASILGSVGIGTINVLVTIVAIFVVDKIDRKKLLVGGNIGMIASLLIMAILIWTIGIASSAWIIIVCLSLFIVFFGISWGPVLWVMLPELFPMRARGAATGISALVLNIGTLIVSLFFPILSDALSTEWVFLIFAFIGVLAMIFVIKFLPETRGRSLEEIEYELRERTGARTE | 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 | MPATEKASAPHWSFLSSDVISIMKSNPSTLLLPLAALSLASCANPQKEETKRPNIIFMMTDDHTTQAMSCYGGNLIQTPNMDRIANEGIRFDNCYAVNALSGPSRACILTGKFSHENGFTDNASTFNGDQQTFPKLLQQAGYQTAMIGKWHLISEPQGFDHWSILSGQHEQGDYYDPDFWEDGKHIVEKGYATDIITDKAINFLENRDKNKPFCMMYHQKAPHRNWMPAPRHLGIFNNTIFPEPANLFDDYEGRGKAAREQDMSIEHTLTNDWDLKLLTREEMLKDTTNRLYSVYKRMPSEVQDKWDSAYAQRIAEYRKGDLKGKALISWKYQQYMRDYLATVLAVDENIGRLLNYLEKIGELDNTIIVYTSDQGFFLGEHGWFDKRFMYEECQRMPLIIRYPKAIKAGSTSSAISMNVDFAPTFLDFAGVEVPSDIQGASLKPVLENEGKTPADWRKAAYYHYYEYPAEHSVKRHYGIRTQDFKLIHFYNDIDEWEMYDMKADPREMNNIFGKAEYAKKQKELMQLLEETQKQYKDNDPDEKETVLFKGDRRLMENR | 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 host gastrointestinal tract .
PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Sequence Mass (Da): 64585
Sequence Length: 558
EC: 3.1.6.-
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Q97UZ1 | MKRKYPYSLAKGLTSTQIAVIVAVIVIVIIIGVVAGFVLTKGPSTTAVTTTVTSTFTTTTTIPSTTTSTPSNTVVFYTWWGGGDGGEALSQIIPAVKQYAGLQMQTYSIPGAGGTNAKYAILALIQAGKPPAAFQVHYGPEMISYVEAAPNGIHTFVNMTPYLIQWGLLNNAVYAVLQAGAYNGTLLSVPINVHRGAVLYVNTQLLREYNLPFPYNFSTLVYDTVQLANHGVSPWIIPGGDGGWDQFNVWEDIFLYLAGPQLYNELIYGTLNFSNPTVQKLINETNYWFLNFTSYNYPGWQSMSWEQAFALIAQGKVAFQANGNWVTNYASYINVTVYPPLPQYISNSSVSVVETPFPGTQHYYALVIDTIGIPVGPQEQQALQLAHFWSSYQGQEVWTKYKAVTYYKNGTDWYAQPAQWYDYQQLINTSEQNFVYQLSDGGVFDDVFAQIDSGLLTLQQVGKVGLSAWNSTLVSSMQQEQNEWLAAAKLGLGYLGFPGHPFAGYYPPWVTNPSAYGLTNNTQKTSNSVMLFLLPFLALPLAIASIDNKYYLLK | 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 | MAKRQTWEQMRQIFVQAVNAVHPEKVFADFQKFDLRPQIGENATDISIKLNGERQDISGKTCHIVGFGKAVLGMANKVQQDLGATSAGGVLSVPVNTLKQFQQPVAPGLVVHEGAANNLPDENALKAAREIKQLAEKMTAQDILFVFISGGGSALLPLPRSPLTLEDKRSIADKLMKRGASIQEINAVRIACSDIKGGRLARLAGQAGLLVTFVLSDIIGDPLELIACGPTIQPEAAASPSDILKKHHVWEELSPEIRRVFEQPEEQKNTSLPEHKVFVVGSNVIATSTAAHEAERLGYIPCVLSCAVQGDVAQVAGDYQRLLHGIQEAKQHGILDPQLREKYAFGERSYPTFRRALEDHMSSKKPLFLICGGEPVIKVSGHGLGGRSQHLALLMSQALHRDEAMRDCTFLSAGTDGIDGPTDAAGAFGDSSVVESYLGDHTLDELAETLRNCDSYNFYKNLAQGEHHVLTGHTGTNVMDLHFLVVP | 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 | MAAALQVLPRLARAPLHPLLWRGSVARLASSMALAEQARQLFESAVGAVLPGPMLHRALSLDPGGRQLKVRDRNFQLRQNLYLVGFGKAVLGMAAAAEELLGQHLVQGVISVPKGIRAAMERAGKQEMLLKPHSRVQVFEGAEDNLPDRDALRAALAIQQLAEGLTADDLLLVLISGGGSALLPAPIPPVTLEEKQTLTRLLAARGATIQELNTIRKALSQLKGGGLAQAAYPAQVVSLILSDVVGDPVEVIASGPTVASSHNVQDCLHILNRYGLRAALPRSVKTVLSRADSDPHGPHTCGHVLNVIIGSNVLALAEAQRQAEALGYQAVVLSAAMQGDVKSMAQFYGLLAHVARTRLTPSMAGASVEEDAQLHELAAELQIPDLQLEEALETMAWGRGPVCLLAGGEPTVQLQGSGRGGRNQELALRVGAELRRWPLGPIDVLFLSGGTDGQDGPTEAAGAWVTPELASQAAAEGLDIATFLAHNDSHTFFCCLQGGAHLLHTGMTGTNVMDTHLLFLRPR | 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
|
Q6MAS9 | MHIIHIASELAPLAKVGGLADVVLGLCRELSWKGHDVDIIIPKYDCMDSEQIRDLTVDYFELPSFYNGEWFFNTVWMGWVENLKVYFIEPHHPRFFFNRGCFYGCEDDLERFLYFSRTALEFLYKKSILPDIIHLHDWQTAVIAPLYKDMYQKLGYTKPKILFTIHNMEYQGKCAAHDLNYIGLDGNRYQQHSFMQDNLYPHLINLLKGGIVYSDFVTTVSPNYAKEVLTPKEGRGLEATLVEYQHKFKGILNGIDYSYWNPEIDRFLPAHYSLREMPKNKKDRNTVDKKGFIKKILREKLYLAEEHRPIIGCITRLVPQKGIDLIKHTIRHIVEKKGQFILLGSSPIPSINDEFHRLKHQYTDHPHIHLILHHSEELAHLIYAGSDMFIVPSLFEPCGLTQIIALKYGTVPIVRRTGGLADTIIDVDHTDQQPDKKNGYVFDDPDANGIDSAIDRAIHCWFEEPEKWRQLMLNGMKMDFSWNQSSDCYLKIYQAISAKN | 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 | MRVLHVCSELFPLLKTGGLADVAGALPGAQIAAGMDVRVILPAFPDLKKGIANLQVVRELDTFAGHVTLLFGHFNGVGIYLIDVPELYERAGSPYHDPALYAYADNYLRFALLGWMGCEMACGLDHYWRPDIVHAHDWHAGLTCAYLAARNRPAKSVFTVHNLAYQGLFAAGHMANLHLPSDFFQVYGLEFYGQISYLKAGLFYADHITTVSPTYAHEITLPAYGYGMEGLLKTREEEGRLSGILNGVDETIWNPTHDPLLTNHYSREALANKAENKRHLQTAMGLKVDDKAPVFAIVSRLTSQKGLDIALSAIPDLLEQGGQLVVLGAGDADLQEGFLAAAAEYHGQVGVQIGYHEAFSHRIIGGADVIMVPSRFEPCGLTQLYGLKYGTLPLVRRTGGLADTVSDCSLENLADGLASGFVFNDCSVGSLSRAIRRVFVLWSRPTLWRYVQRQAMAMDFGWQVSAQAYGALYQRLHTH | 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 | MKIAYVSYEVSPFAKAGGLADVAGALPKYIKNAGEDIYVVMPFHKNIENNYDISKFEVVKTGLIPDSHTHKSPFSVYKSYLEGSSVVIYFIKTDSLYDSKNIYDEENIFLKTSYFCDSALKTIKECEPDTNVININDWHTSLIPVYLKTHYLQDNILKKIATILTIHNIGYQGLFNPEVLNQAGLPNYLFNMNALEYYGKVNVLKGGILFSNIINTVSPTYAKEIQSEEYGYGLEGILKVRSEDLFGILNGIDYSIYDPLKDPHIFHPIESYEDKLKNKTSLQEYLGLTKDENITLISFIGRLFEQKGIDLISKIMDLLLLNDIQFVLLGTGDKKYEEYFVTLTKLYPKKISINITFDVDLAQKIYAGSDIFLMPSKYEPCGLGQMYSMRYGTVPVVRYTGGLKDTVSEYNPKDKKGTGFGFHEYKEADLLYTLMKAIYFHQKRKDDWTNIFENCMKEDFSYEKTAKKYIELYKIALDKKRGY | 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 | MKVLHAAAEVYPLVKTGGLADVLGALPEALIGAGADVRLVLPGLPAILAGVEQQQVVHEIGAVFGAGRVTLRLGRLAHNGVPAYVIDAPYLYQRPGNPYLAPDGGEWPDNLQRFGLLGWVAAHLAAGELDPGWTPDVLHAHDWHAAMACAYAACHPATRAATVYTIHNLAYQGLFDEDDFHLLGLPSRLMVPVGLEFHGQLSFMKAGLKYAHRITTVSPTYAHEIATEAFGCGLDGVIRARGADVSGILNGVDGAVWNPASDPLIAAPYSADMLDGKALCKAALQRELGLAVDAGAPVFAVVSRLTSQKGLDLLLDALPALLNFPAAGGPQLAVQGNGDPALEAAFTAAAAAHPGRVAVRLVYDEALAHRIMAGADAMLVPSRFEPCGLTQLYALRYGTVPVVRHVGGLADTVVGASEASVQADRATGFMFGPATPAALAQALLQAVAAHGQPALWHRLMLRGMAQNFSWTAAASQYMALYRETQQAMQATGKL | 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 | MRVLFAAAECAPMVKVGGMGDVVASLPSALAKLGHDVRLIIPGYSKLWGLLDISKDPIYTAQTMGAEFSVYETKHPTSNLPIYLVGHPVFDPERIYGGEDEDWRFTFFASATAEFAWNVWKPQVLHCHDWHTGMIPVWMHQDPEISTVFTIHNLKYQGPWRWKLERMTWCPWYMSGDHTMAAAMLFADRVNAVSPTYSREIRTSEYGESLEGLLNYISGKLRGILNGIDLDEWDPATDKALPANFSSGKMSTRKKNKEALQRQMGLEVNNDKYLLGMVGRLVDQKGVDLLLQVSRRLLAYTDSQIVVLGTGDQILESALWELAIDHPGRFAVFLTYDDYLSRLIYAGSDAFLMPSRFEPCGISQLLAMRYGSIPIVRNVGGLVDTVIPHDPINKSGTGFCFDRFEPIDFYTALVRSWEAFRHRRSWKELQKRAMTQMYSWERSAMEYETMYKEVSGYKEPSPDAIEVEKFSVGQDADPSLKNEKLSVGQDEDSSLKNERFI | 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 | MDPFFLNTQHVELLVSGKQSSPQDLLGIVSESLNQDRIVLFRPGAETVFVELRGKIQQAESHHSGIFSLPVMKGISPQDYRVYHQNGLLAHDPYAFPLLWGEIDSFLFHEGTHQRIYERMGAIPCEIDGVPGVRFIVWAPHAQRVSVIGDFNGWHGLVNPLHKVSDQGVWELFVPGLTAGACYKWEMVTESGQVLIKSDPYGKFFGPPPWSVSVVIDDSYEWTDSEWLEERIKKTEGPMNIYEVHVGSWRWQEGQPLNYKELADQLALYCKQMHYTHVELLPVTEHPLNESWGYQTTGYYAPTSRYGSFEDLQYFIDTMHQHGIGVILDWVPGHFPIDSFAMSGFDGTPLYEYTRNPSPLHPHWHTYTFDYAKPEVCNFLLGSVLFWIDKMHVDGIRVDAVSSMLYLDYGRYAGEWVPNRYGGRENLDAIRFLQQFNTVIHEKYPGVLTFAEESTTFPKITVSVEEGGLGFDYKWNMGWMHDTLHYFEKDFPYRPYHQSDLTFPQWYAFSERFLLPFSHDEVVHGKRSLIGKMPGDAWRQFAQLRLLLGYQICQPGKKLLFMGGEFGQGREWSPGRELDWELLDISYHQGVHLCSQELNALYVQSPQLWQADHLPSSFRWVDFSDVRNGVVAYLRFADADAKKALLCVHHFGVGYFPHYLLPILPLESCDLLMNTDDTRFGGSGKGFREPEILTPEIARQEREAAGLIEADDESGPDCWGLDIELPPSATLIFSVTLQ | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 84651
Sequence Length: 738
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q0TQ16 | MRNCKELKHEKNGNVTEKIGKNKGKSKKVSKDESLLSFDLFLEGKEHSAYKFMGAHFVTENRKRGVRFTTWAPRSSKIYVIGDFNNWELKEEYSMKKINERGIWSLFLPKLEEGIKYKFAVVNECGNNTVYKADPYAFKSELRPNTASVLTKIKSFRWGDKRWLNKREKEGLDNKPMNIYELHLGSWKRKDGEFMTYEEISEVLVEYVKEMGYTHVEFMPINEHPLDASWGYQGVGYYSVTSRYGDLNGLKALINKLHKNNIGVLLDWVPSHFCKDEHGLFMFDGSPTYEYGAWWKANNEGWGTCNFDLGRPEVKSFLFSNAMYWINEFHIDGLRVDAVSNMLYLDYGREYGEWEPNIYGGNGNLEAIAFLKELNTIIKKEGKGAITVAEESTSWEGITKPVEEDGLGFDYKWNMGWMNDTLSYIELDPIYRKYHHNKMNFSMMYNYSEKFILPISHDEVVHGKKSLINKMWGDDWKKYAGLRLYASFMMGHPGKKLMFMGCEFGQFVEWREWEELQWNIIEEFDIHKKTQEYFKALNHFYLENSSLWSLDYEEEGFKWIDADNSEESVLSFIRIGKNKKEKLIFICNFTPEVYYDFKVGVPELGEYVEVFNSDSLEFGGAGNIMGDSILKATEESFKDFDYSIIVKVPPLGTLVLKVK | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 77008
Sequence Length: 659
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q8NR40 | MTVDPASHITIPEADLARLRHCNHHDPHGFYGWHETEAGSVIRTRQVGATQVNLLIDDTSHVMTPIGDDIFAIDLGHRERADYRLEVTWPDQEPQVKADPYYFLPTVGEMDIYLFSEGRHERLWEILGANIKTYQTALGTVRGTAFTVWAPNAIGCAVVGGFNGWNASQHPMRSMGGSGLWELFIPGIEEGEVYKFAVQTREGQRRDKADPMARRAELAPATGSIVASSEYQWQDSEWLRERSQTDLASKPMSVYEVHLGSWRWGKNYEDLATELVDYVADLGYTHVEFLPVAEHPFGGSWGYQVTGYYAPTSRWGTPDQFRALVDAFHARGIGVIMDWVPAHFPKDDWALARFDGEALYEHPDWRRGEQKDWGTLVFDFGRNEVRNFLVANALYWIEEFHIDGLRVDAVASMLYLDYSREHGEWEPNIYGGRENLEAVQFLQEMNATVLRLHPGALTIAEESTSWPGVTAPTWDGGLGFSLKWNMGWMHDTLEYFSKNPVHRAFHHSELTFSLVYAFSERFVLPISHDEVVHGKGSLWDRMPGDTWNKAAGLRTFLAYMWSHPGKKLLFMGQEFGQREEWAEGQGLPWDIVDGWQGEYHEAIRTLTRSLNGVYSDSPALHTQDFTGEGFTWNKGDDATNNILAFTRFGSDGSQMLCVFNLSGTSQPEYQLGVAAGGEWKLVLNTDDAEFLGAENDIATSVQAAATPRDNFAYSLSLHVPAMSAQFYSLQK | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 82593
Sequence Length: 731
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q6A8Q7 | MAHDEFGGLTGWDLEGFHSGGDTEVWKRLGSHVVTIDDDERGPITGTRFAVWAPNAQAVEVISDFNWWTGDRMRLIPGSGVWGTFVEGVDEGTLYKFRIQDQWGTWHEKVDPMARYSEQAPQNASIVTETHYEWNDDEWIARREASRAHAEPMSVYEVHLGGWRHGLSYRELADQLVSYVTWQGYTHVEFMPLAEHPFAPSWGYQVTGYFSPTSRYGSPDDLRYLIDKLHQAGIGVIMDWVPGHFPKDDWALGRFDGTALYEHADPRQGEHKDWGTYIFNYGRNEVKSFLVSSALYWISEFHADGLRVDAVASMLYLDYSREEGQWVPNKYGGRENLEAIDFLRYVNSHLYSRHPGILMIAEESTSFPGVTKPVDDGGLGFGFKWNMGWMNDSLRYLELNPFHRQYHHGEMTFAMVYQYSENFILPISHDEVVHGKGSMITKIPGDDWQQFASLRAFYSYMWSFPGKQLVFMGQEFGQRHEFDESVSLEWFVADLWGHGGLKRLFRDLNKIYKENPALWQLDSDPRGFEWINADDAGNNLFSWLRRSDDGSTIACFTNFSPNPQTDYRIDLPMEGVWTEILNTDSLEYDGTGEFGNLGQIVAAPLPAPDRLRAVATVCVPPMGSVWLRHNPSATAALPGDPGVQ | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 73563
Sequence Length: 644
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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P32775 | MYNIPDNVKGAVEFDPWLKPFADVLSERRYLADKWLYDITHATPDGSYQSLSKFARDSYKSYGLHANPETKEITYKEWAPNAERAFLVGDFNNWDTTSHELKNKDEFGNFTITLHPLPNGDFAIPHDSKIKVMFILPDGSKIFRLPAWITRATQPSKETSKQFGPAYEGRFWNPENPYKFVHPRPKFSESVDSLRIYEAHVGISSPEPKITTYKEFTEKVLPRIKYLGYDAIQLMAIMEHAYYASFGYQVTNFFAASSRFGTPEELKELIDTAHSMGILVLLDVVHSHASKNVEDGLNMFDGSDHQYFHSISSGRGEHPLWDSRLFNYGKFEVQRFLLANLAFYVDVYQFDGFRFDGVTSMLYVHHGVGAGGSFSGDYNEYLSRDRSFVDHEALAYLMLANDLVHEMLPNLAVTVAEDVSGYPTLCLPRSIGGTGFDYRLAMALPDMWIKLIKEKKDDEWEMGSIVYTLTNRRYGEKVVAYCESHDQALVGDKTLAFWLMDAAMYTDMTVLKEPSIVIDRGIALHKMIRLITHSLGGEAYLNFEGNEFGHPEWLDFPNVNNGDSYKYARRQFNLADDPLLRYQNLNEFDRSMQLCEKRHKWLNTKQAYVSLKHEGDKMIVFERNNLLFIFNFHPTNSYSDYRVGVEKAGTYHIVLNSDRAEFGGHNRINESSEFFTTDLEWNNRKNFLQVYIPSRVALVLALKE | 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 | MAGVLGMILAGGEGSRLKPLTETRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYIHMKKGWNLSGITDRFIDIIPAQMRDGKRWYEGTADAIYQNLRFVEIVAPDQVCIFGSDHIYKMDIRQMLDFHRRMEAELTVSALRMPISQASQFGVIEVDENGKMVGFEEKPSNPKSIPGEPEWALVSMGNYIFEAETLSKELREDAENNQSSHDFGKDIIPKMFPRGKVYVYDFTTNKIKGEKESTYWRDVGTIESYWSAHMDLLDKDPEFSLYNRSWPLHTYYPPLPPATFVDVKDKKVKITDSLISGGSYIQGSTIYKSVLGFRSNIAAGSFISESVILGDVKIGAGCTIKRAIIDKDVEIAAGTIIGEDLEMDRKRFHVSDEGIVVIAKGSKVGF | 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-glucose + diphosphate
Sequence Mass (Da): 45497
Sequence Length: 405
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.7.7.27
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Q9KLP4 | MQDTLAVILAGGMGSRLSPLTDDRAKPAVPFGGKYRIIDFTLTNCLHSGLRRILVLTQYKSHSLHKHLRNGWSIFNPELGEFITVVPPQMRKGGKWYEGTADALFHNMWLLARSDAKYVVVLSGDHIYRMDYAAMLEEHISKNATLTIACMQVPRHEASAFGVMAIDDDSRITCFVEKPADPPCIPNRPDHSLASMGIYIFNMDVLKKALTEDAEIEQSSHDFGKDVIPKLIATGSVFAYSFCSGKGRVARDCYWRDVGTIDSFYDANMDLLQPVPPMNLYQKNWAIRTYEQQYPPARTVSSATGNEGIFINSIIANGVINSGGSVQHSIISSNVRINDSALIVDSILFDDVEVGEGCKLIHCIIDKHVKIPPYTEIGLNPIEDRKRFHISERGVVVVPESYQFSTE | 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-glucose + diphosphate
Sequence Mass (Da): 45372
Sequence Length: 407
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.7.7.27
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Q2RS49 | MDQITEFQLDINRALKETLALVLAGGRGSRLRDLTNRESKPAVPFGGKYRIIDFPLSNCMNSGIRRMCVITQYRAHTLIHHIQRGWGFLRAEIGEFVELWPAQQQTDKESWYLGTADAVHQNLDLIRMHDPRFVLILAGDHIYKQDYSKLLAHHIARGSDCTVACVDVPREEATGYGCVEVDNDDNIVHFLEKPANPPGIPGRPDRAFASMGIYIFNADFLYEILESDALNEASQHDFGRDIIPSQVGKARIVAHRFSQSCVYSVGRREPYWRDVGTVDAYWSANIDLVSVTPALDLYDADWPIWTYQMQRPPAKFVFDTDERRGMAKDSLVSAGCIVSGGAVTGSLLFNDVRVNSYSSVIDTVILPMGDIGRHARLTKCILDTGCRIPEGLVIGEDPILDAKRFHVTEQGITLVTPDRLALL | 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-glucose + diphosphate
Sequence Mass (Da): 47376
Sequence Length: 423
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.7.7.27
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B7K5U7 | MKKVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPLSNCINSEILKIYVLTQFNSASLNRHLTRTYNFTGFSDGFVEVLAAQQTAENPKWFQGTADAVRQYLWAFQEWDIDEYLILSGDHLYRMDYRDFIQRHRETGADITLSVVPIDEERASSFGLMKIDDHGRVVDFSEKPKGDELKQMQVDTTVLGLTPEQAKESPYIASMGIYVFKKEVLAQLLEENPDQTDFGKEIIPFSAKDYNLQAYLFKGYWEDIGTIKAFYEANLALNRQPSPRFSFYNEEYPIYTRSRYLPPTKALNCTITESMVSEGCILKDCRIHNSILGIRTRIEANCTIEDTMLMGADYYESPSLRESKAQEGKIPMGIGEGSTIRRAIVDKNARIGRNVTIVNKENIDESNQEESGFYIRNGIVVILKNATIADGTVI | 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-glucose + diphosphate
Sequence Mass (Da): 48547
Sequence Length: 429
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.7.7.27
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Q21M27 | MLDPNSRYVSRLTRDTVALVLAGGRGSRLHELTDWRAKPALHFGGKFRIIDFPLSNCVNSGIRRIGILTQYKAHSLIRHVIRGWSSFKKEFGEYVEILPASQRYSPNWYQGTADAIYQNLDILQAEAPKYILVLSGDHVYQMDYGAIIAHHVETGADLTVSCIEVPIEEAAGSFGVMTVDDDNRIIRFDEKPQRPTELANKPGYTLASMGNYVFNTEFLFDQLRKDAADPDSEHDFGKNIIPNIIAEKLVSAYRFRDHDTNETAYWRDVGTLDSFWEANMELVSPNPSLNLYNHDWPIWTYQTQLPPAKFVFDDDSRRGYAVDSMVSGGCIVSGGKVKSSLLFSDVHIHSYAEIEESVLLPEVEVHRSAKIKKAIIDSACVIPEGMIIGHDHEHDKARGFRVTKKGVTLVTREMLGQQPAGTSAK | 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-glucose + diphosphate
Sequence Mass (Da): 47762
Sequence Length: 425
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.7.7.27
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A6TF50 | MTSLAAGKPAPLGASYDGKGVNFALFSAHAERVELCVFDEQGNEQRFDLPARSGDIWHGWLAAAGPGLRYGYRVHGPWDPAQGHRFNPAKLLIDPSAHRVEGDLPDDERLHGGMWQPDRRDSAAVAPKSQVVDLRYDWRGDKPPRTPWGETVIYEAHVKGLTLLNPQLPEAIRGTYKALGHPAMIAYFKSLGISALELLPVAQFASEPRLQRMGLSNYWGYNPLAWFALDPRYASDPDRALDEFRDAVKALHAAGIEVILDIVLNHSAEIDLEGPTVSLRGIDNRSYYWVREDSDYHNWTGCGNTLNLSHPGVVEWARQCLRFWVDECHVDGFRFDLASVMGRTPEFRQDAPLFEAIRRDSVLSQVKLIAEPWDIGPGGYQVGNFPPLFAEWNDHFRDSARRFWLQQNVSLGDFAQRFAASSDLFARDGKPPSATVNLVTAHDGFTLRDCVCFNQKHNEANGEENRDGTNNNYSNNHGIEGLEANFAVIERRRASAHALLTTLLLAQGTPMLLAGDEQGHSQHGNNNAYCQDNALTWLDWRQANPGLTAFTAALIHLRRRIPALTRNRWWQEGDGNVRWLNRNAQPLTAAEWQQGAACMQIQLSDRWLLTLNATAEVVDMVLPEGEWRAVPPFAGEDNPVIMAVWHGPAHGVCVFQRS | 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 dextrin.
Sequence Mass (Da): 73651
Sequence Length: 658
Pathway: Glycan degradation; glycogen degradation.
EC: 3.2.1.196
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Q8YDC6 | MQAIIDAEQSFKFPVLVGDIGGTNARFSILVDSNAEPKEFPVLQTADYATIDEAIQHAILDQTAIQPRSVILAVAGPVDGDEIDLTNCDWVVRPKKMIADLGFEDVTVLNDFEAQALAVVSLEGHHMEQIGGKPEEAVATRVVLGPGTGLGVAGLVCTRHAWVPVPGEGGHIDIGPRTERDYQIFPHIERIEGRVTGEQILSGRGLRNLYLGICAADKITPTLETPVDITSAGLDGSNPQAAETLDLFATYLGRLAGDLALIFMAHGGVYLSGGIPVRILSALKAGSFRAAFEDKAPNKAIMRDIPVRVITYQLAALTGLSAFARTPSRFEVSTEGRRWRMRR | 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
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Q62HW8 | MSTGAQTKAAAASQHADGPRLLADVGGTNARFALETGPGEITQIRVYPGAEYPTLTDAIRKYLKDAKIGRVNHAAIAIANPVDGDQVRMTNHNWSFSIEATRRALGFDTLLVVNDFTALAMALPGLTDAQRVQIGGGTRRQNSVIGLMGPGTGLGVSGLIPADDRWIALGSEGGHATFAPMDEREDLVLQYARRKYPHVSFERVCAGPGMEIIYRALAARDKKRIAANVDTADIVERAHAGDALALEAVECFCAILGTFAGNLAVTLGALGGIYIGGGVVPKLGELFMRSPFRARFEAKGRFEAYLANIPTYLITAEYPAFLGVSAILAEQLSNRTGGASSAVFERIRQMRDALTPAERRVADLALNHPRSIINDPIVNIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGTIPMSHSQVHLGDTATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAYGDLYMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITSSNTPLAKRATVALETDHIEMRESQLSMISRILHLVMIDILAVGVAIRRAAPNAELAEAMARAKARAGASAGDEAADVLDWLSHGAAPAAKD | 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
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Q9A6N3 | MDGNHSGGLGLVGDIGGTNARFALVEFDGQDPRLIEPTAYRGEDYGTAEDAIEEYLRKVGVKHPDQAVVAVAGPIDHGQVHMTNLDWRISEDGLRRAGGFRNAKLINDFTAQALAAPRVGPKDLRQIGELPTSGEGDLAILGPGTGFGVAGLVRRHGQEIPLATEGGHVAFAPVDDVEIEVLRALTRRLDGGRVSVERILSGPGMEDLHVDLAAAEGRGVEALTAKQITERAVEGCADSLATVNRFCAILGSTAGDIALTLGARGGVFIAGGIAPRIIDILEKSPFRERFDSKGRLSGFTRSIPTHVILHPHTALIGAAVALTPEGRAAVS | 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
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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
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Q7P1R6 | MSTGLPEAWPRLLGDVGGSNARFALETAPGVIEDILTLSNERYPTLEDALRDYLAQVGARRVAHAAIGIANPLNGDLVRMTNCHWSFSIEATRRALGLSTLLLLNDFTALALALPRLPRRELAQVGGGAPRPDAPLALIGPGTGLGVSALVPHAGGWRALAGEGGHTSFAPANEREIGIWRYASARFGHVSHERLLSGSGLSLLHRALCALDGAEEAGLAPAEVSARGLSGADARCREALEIFCALLGSAAGNLALTLGARGGVYIGGGIVPRLSGFFEQSPFRRRFEDKGRMSAYLADIPVYLITSAYPALPGVAAHLADHLAPRSDPAPVAAPTHPRGGTAGDMHA | 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
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Q47XU3 | MKNSQDTQVINLVADIGGTNIRLAITDKDNNINEIKTYQCKDFPHLSNVIYHYLKENGLLNSQVNACLAIACPVDTDSISMTNLPWKFSQKQLKEELKLHSLTLINDYTAIAMAIPLLSDKQKVKIGHGEAENKQPIAVCGPGTGLGVANLVNINNHWYCLGGEGGHTDFAPVDELDVKIFQQLKTTKKRLSYEQLLSGYGLEQIYQALVIINNQEATNAEQSKLSAKEISTQAIAGTCPICQQALSQFCKILGSFSGNLALTTGSFGGVYIAGGIVPRFIDYLKNSEFRARFETKGRMSHLNEQIPTYIITESQPGLLGAAAYLNQVFP | 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
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P21908 | MEIVAIDIGGTHARFSIAEVSNGRVLSLGEETTFKTAEHASLQLAWERFGEKLGRPLPRAAAIAWAGPVHGEVLKLTNNPWVLRPATLNEKLDIDTHVLINDFGAVAHAVAHMDSSYLDHICGPDEALPSDGVITILGPGTGLGVAHLLRTEGRYFVIETEGGHIDFAPLDRLEDKILARLRERFRRVSIERIISGPGLGNIYEALAAIEGVPFSLLDDIKLWQMALEGKDNLAEAALDRFCLSLGAIAGDLALAQGATSVVIGGGVGLRIASHLPESGFRQRFVSKGRFERVMSKIPVKLITYPQPGLLGAAAAYANKYSEVE | 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
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Q89DN1 | MSRKYFGTDGIRGRANGLITPELALKVGQAAGLAFQRGDHRHRVVIGKDTRLSGYMIEYAMVAGFTSVGMDVLLVGPMPTPAVAMLTKSMRADLGVMISASHNLFEDNGIKLFGPQGFKLSDDVEKQIEQLLDEPIDKRLAQSASLGRARRIDGVHDRYIEFAKRTLPRDLSLDGLRVVVDCANGAAYKVVPEALWELGADVVPIGVEPDGFNINKDCGSTSPEALSKKVREMRADIGIALDGDADRVILVDERGHVVDGDQLLAVIAQSWKEDGRLSRPGIVATVMSNLGLERFLKGQGLDLVRTPVGDRYVLEQMLSGGYNLGGEQSGHIILSDYATTGDGFVAALQVLAVVQKSRRPVSEVCHRFDPLPQILKNVRHKGGKPLDDSDVKSAISDGEKRLNGHGRLLIRSSGTEPVIRVMGEGEDRILVEDVVDTIVSALGQAAA | 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
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C0ZIM8 | MGKYFGTDGVRGVANTQLTPELAFKIGRVGGYVLTRHKQEGKPKVVIGRDTRISGQMLENALLAGLLSVGAEVVRLGVISTSGVAYLTRALGADAGVMISASHNPFPDNGIKFFGSNGFKLSDEVEAEVEQYLDAAEDTMPRPTGEQIGTVLEFLEGGQKYLSHLKSTVSERFDGLKVVLDCANGAVSSLAARLFADVDAEVITIGANPNGININDQCGSTHPERLVEEVLKHKADLGLSFDGDADRCIAVDNNGEIIDGDYIMAICARALKAKGKLNNNTVVTTVMANMGFFKGMEECSINTTKTAVGDRYVVEEMLRGGYNLGGEQSGHIVFLDYNTTGDGLLTGLQLLNIIKESGKPLSELKQVMVKYPQLLINVRVEDKSKLNGNEAIAQAIREVEEDLAGNGRVLVRPSGTEPIVRVMAEGPDAAQLEGLVNRIVDVVKQQLV | 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
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Q8Y5E6 | MGKYFGTDGVRGVANSELTPELAFRLGRMGGYVLTRHVGEHPRVLVARDTRISGEMLESALIAGLVSVGIEVMRLGVISTPGVAYLTKAQGASASVMISASHNPVDDNGIKFFGSDGFKLSDDQEEEIEQLLDTAEDTLPRPSGEGLGTVSDYFEGKQKYIQYLKQTIENDFNGYHIALDCANGATSGLATHLFADLDADISSMGASPNGLNINDGVGSTHPEALAAFVLDKKADVGLAFDGDGDRVIAIDEIGQIVDGDKIMFICAKYLREQGLLNNNTIVSTVMSNLGFYKGLKELEIEDVQTAVGDRYVVEAMREGNYNLGGEQSGHIIFLDHNTTGDGLLSGIQLINVMKATGKKLSELAAEMKTFPQKLENIRVSDKNHVTDNPKVSKVIDEVEAEMAGNGRVLVRPSGTEPLVRVMVEAATKEETDEYCERISAVVRSEMALND | 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 | MDNKLFGTDGLRGRVNAYPMTPDVVMRLALSAGLHFRNGSRRHKVLIGKDTRRSGYIYEYALSSGFCAAGMDVFLTGPLPTPAISFLTRDMRADVGVVISASHNPACDNGIKFFDHMGFKLPDAVEAEIAARVEGYAQDWRLPDPDHVGRAFKLEDSPGRYNVFLKNSIPLDVNFEGLKIVLDCAHGAAYRVTPQVFEELGAKVIKIGVDPDGSNINQRVGSLFPQQVARMVAEAEADIGIALDGDADRVIVADEKGRILDGDQIMAICALDLMERGALPGNLLVATVMSNMALEVFMKDHGGRLLRTPVGDRYVVEAMRAQGAVFGGEQSGHLIFLNHSTTGDGTLAALQLMKIMVRKGKPLSELATLLSPFPQKLVNVPVARKIPFSEAPAIEAAVKDAEATLSGRGRVLLRYSGTESLARVMVEAQDAALVESLCDSLAEVVARALA | 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
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Q027B2 | MAKDLFGTDGIRGVAGQYPLDRDTVYAFGVALGKDAALHAAKPEILIGADTRESGTWIAELVAGGLASQGAQVRYAGVITTPGVAYLTRTGSFVAGVMISASHNPYDDNGLKVFGHSGFKLPDDEELLIEQEIFRLREAPVAPQPLSLTVEEPLVRQYLKYLSGISSVRLDGVRVAIDCGNGASYRLAPELFQGLGADVVTICCEPNGRNINLNCGALHLEALQQAVVAHRAHFGVAFDGDADRAIFVSSSGQVVNGDAVLLACGRALKAAGKLAGNTVVSTVMSNLGLERAFDAAGIRMVRTPVGDKYVLEEMVRLGAALGGEQSGHVIFREYSTTGDGMLTALRLFEIAQQAGTGLDELTADLKIYPQRLVNVRVREKKGLLELPAVAKEIRRVEDAFGGAGRVLVRFSGTEPLARVMVEGPNLEQVESFSTSIADVIRREMGE | 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 | MPKHTKKDPREGAPSATGEPQKQAAGRKLFGTDGVRGVANQPPMTPEMALRLGRAIAFVASHGKSRQVRVVIGKDTRLSGYMLETAIASGVCAMGGRVMLSGPIPTPAVAQLTQSMRADAGVVISASHNPYQDNGIKIFGPDGYKLPDTAEEEIERLMESHELDEARVVGAAIGSAVKLDDARGRYVVFCKNTFPTALSLDGVKIVVDAAHGAAYRVAPSVFTELGANVTALGVKPNGRNINRETGALHPEHVKAEVLKRGAAIGIALDGDADRVIMVDERGEVVDGDAIMALCALRMLRTGKLPRNTIVTTVMSNLGLERALKAQSGHVVRTAVGDRYVVEAMRNGGYSFGGEQSGHLIFLDHATTGDGIVAALQVLAIMMEEDKPLSELASKAMQRVPQVLENATFATRLPLDSMQRTRVTVDRIEKTLGDKGRILVRWSGTEPKLRVMVEGEDASTIGAYALEIIEAAKQDVAGASA | 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 | MCGIVACILKDGSAAPVLLECVRRLEYRGYDSVGIATSDPMIRIKKDSGKIDEVDAELDLADLPGTMGIAHVRWATHGLPTAENAHPHTDCSGEIAVVHNGIIENYLEVKEELESEGHIFRSETDTEVIPHLIEKYMDEGMDLEAATATALRKLRGAYAIAAVSSREPGRIVGARKESPLIVGVGEGEYFLASDVPAILNHTSRVIYLDDGEMVILDGDLRVTDMEGNTVEKEVHSIDWSADMAEKGGYDHFMLKEIHEEPSAVRDTLTEWDEVLGVVEEIGEVERICFVACGTSYHASLVGKYLFESLLGIPTDVILASEFRYSAGALNDRTLAIFISQSGETADTLNALRAANSRAKTLAIVNVLGSSATREAQHVLYTRAGPEIGVAATKTYVSQLTVIYMLVAAMGAPELMDRLERVPEFMERALEDEDGIKELAATCSDVSDFFFIGRGFAYPTALEGALKLKEITYIHGEGYAAGELKHGPLALIDNGVPVVAISPPGPCHDKTLSNVEEVRARGARVIGVGSISDESLRKEADDFIGLDPEVDDVISPLVYIVPLQLLSYHVSVERGLDPDKPKNLAKCVTVE | 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
EC: 2.6.1.16
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O68956 | MCGIVGYVGHRPARDIVVDALRRMEYRGYDSAGIALIDGNGGLTVRRRAGRLANLEATLAETDSNDGDGLGGSTGLGHTRWATHGRPTDRNAHPHRDAAGKIAVVHNGIIENFAPLRAELEAAGVEFASDTDTEVAVHLVARQYTQGDTAGDFPASVLAVLQRLEGHFTLVFASADDPGTIVAARRSTPLVLGIGDGEMFVGSDVAAFIEHTRDAVELGQDQAVVLTADGYRITDFAGNDHLEAGRDFREFHIDWDLNAAEKGGYDYFMLKEIAEQPSAVADTLLGHFDKNRIVLDEQRLSDQELREIDKVFIVACGTAYHSGLLAKYAIEHWTRLPVEVELASEFRYRDPVLDRSTLVIAISQSGETADTLEAVRHAKTQKAKVLAICNTNGSQIPREADAVLYTRAGPEIGVAATKTFLAQIAANYLVGLALAQARGTKYPDEVAREYRELEAMPDLIKRVLAGMDSVAALAERFAPSSTVLFLGRHVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALIDENLPVIVVMPSPKNAAMLHAKLLSNIREIQARGAVTVVIAEEDDDTVRPYADHLIEIPSVSTLFQPLLSTIPLQVFAAGVARARGYDVDKPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q9K1P9 | MCGIVGAIRAHHNVVDFLTDGLKRLEYRGYDSSGIAVNTDGKIKRVRRVGRVQLMEDAAREKGISGGIGIGHTRWATHGGVTEPNAHPHISGGMIAVVHNGIIENFESERKRLEGLGYRFESQTDTEVIAHSINHEYAQNGGRLFEAVQEAVKRFHGAYAIAVIAQDKPDELVVARMGCPLLVALGDDETFIASDVSAVIAFTRRVAYLEDGDIALLASDGIKRLTDKNGLPAERKVKVSELSLASLELGLYSHFMQKEIHEQPRAIADTAEVFLDGGFIPENFGKDAKSVFESIRSVKILACGTSYYAALTAKYWLESIAKIPSDVEIASEYRYRSVIADSDQLVITISQSGETLDTMEALKYAKSLGHRHSLSICNVMESALPRESSLVLYTRAGAEIGVASTKAFTTQLVALFGLAVTLAKVRGLVSEEDEARYTEELRQLPGSVQHALNLEPQIAAWAQQFAKKTSALFLGRGIHYPIALEGALKLKEITYIHAEAYPAGELKHGPLALVDENMPVVVIAPNDSLLDKVKANMQEVGARGGELFVFADLDSNFNATEGVHVIRAPRHVGKLSPVVHTIPVQLLAYHTALARGTDVDKPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q6CYJ9 | MCGIVGAVAQRDVAEILLEGLRRLEYRGYDSAGLAVVDSEGHVARLRRLGKVQVLSQAAEEHELHGGTGIAHTRWATHGEPSEENAHPHISEHITIVHNGIIENHEPLRELMIGRGYRFVSETDTEVVAHLVHFEQKQNGGTLVEVVKRVIPQLRGAYGMVVLDNRDSSVLVAARSGSPLVIGRGVGENFIASDQLALLPVTRRFMFLEEGDVAEITRRDVRVFDKSGQLATREEIESKVSYDAGDKGAYRHYMQKEIYEQPMAIKNTLEGRFSHGEINLSELGPKADELLAKVEHVQIIACGTSYNSGMVSRYWFEALAGIPCDVEIASEFRYRKPAVRKNSLMITLSQSGETADTLAALRLSKELGYLGSLAICNVAGSSLVRESDMALMTKAGVEIGVASTKAFTTQLTVLLMLVARVGRLRGMDAQIEHDIVHGLQALPARIEQMLSQDKLIESLAEGFSDKHHALFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVVVVAPNNELLEKLKSNIEEVRARGGELYVFADEDAGFTSSENMKIIPLPHIEEVIAPIFYTVPLQLLSYHVALIKGTDVDQPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q9HT25 | MCGIVGAIAERNITPILIEGLKRLEYRGYDSAGVAVFDNEGRLQRCRRVGKVASLEEGLAGTPLLGRLGIAHTRWATHGAPTEGNAHPHFSSDEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSIGDLTLALKDAVKELHGAYGLAVISAAQPDRIVAARSGSPLVIGLGLGENFLASDQLALRQVTDRFIYLEEGDIAEIRRDSVRLWDVQGNDVQRETVQYHEGAEAADKGEYRHFMLKEIHEQPSVVQRTLEGRLGQNQVLVESFGPQAAELFAKVRNVQIVACGTSYHAGMVARYWLESLTGIPCQVEVASEFRYRKVAVQPDCLFVTISQSGETADTLAALRNAKELGFLSSVAICNVATSSLVRESDLTLLTQAGPEIGVASTKAFTTQLVALLLLTLGIGQVQKRLADGVEAELVDELRRLPTRLGEALAMNRTVEKVSELFAEKHHTLFLGRGAQFPVALEGALKLKEISYIHAEAYPAGELKHGPLALVDSDMPVVTVAPNNELVEKLKSNLQEVRARGGELVVFADEGAGIEAGEGTHVVGMPHIGDVLSPILYTIPLQLLSYHVAVLKGTDVDQPRNLAKSVTVE | 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
EC: 2.6.1.16
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A4XIS1 | MSKKSTFIILAAGEGKRMKSKYSKVVQKIMGKPMILYIIDEIEKNFEDGRIVVVVGNKKEDVYKVLEGRNVRFAYQEKQLGTAHAVMCAMSEISDDSEDVFVLYGDVPFIKADTLKKLSQKRKEEAAALCLLTAIFENPYGYGRIIADENGNVLKIVEERDATEEQRKIKKINPGFYCFEKQELVNVLSKIDNKNSQNEYYLTDAIEILNRSGKKVVKVTVEDNFEVMGINSRYELFVAEQELKLRINKEHLSKGVQIIDIYSTYIHPDAQIGKDTVIYPGTFILGKTSIGEDCVIGPQSYIVDSKIGNNCHILFSVIENSEIKDNVKIGPYAHLRPNSLLEEGVKIGNFVEIKNSKLGKNTKSAHLTYIGDADIGENVNLGCGTIFVNYDGYKKHRTVVENNAFIGCNSNLIAPVKIGENAYVAAGSTITEDVPANALAIARERQTNKEGWVLRRKQMYENR | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 52009
Sequence Length: 463
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q9PPA2 | MKTSILILAAGLGTRIKSQKPKVLQELCQKSMILHILKKAFALSDDVSVVLSHQKERVEKEILEYFPKTQILEQDLQNYPGTAGALSGFEPKNERVLILCGDMPLVEQTSLEALLGNNAKLNLAVFKARDPKSYGRVVIKNDSVEKIVEFKDANTQEKEINTCNAGVYVIDSRLLKELLPLIDNNNAAKEYYLTDIVKLAKEKDVMIKAVFVDEDEFMGINDKFELSIAENFMQKKIKKYWMQQGVIFHLPQSTFIGADVEFVGECEVYENVRIEGKSKIINSIIKSSSVIENSIVENSDVGPLAHLRPNCELKNTHIGNFVECKNAKLNTVKAGHLSYLGDCEIDSGTNIGCGTITCNYDGVKKHKTIIGKNVFVGSDTQFIAPVKIEDEVIIAAGSTVSINVEKGALFINRAGHKMIKDYYYKKFQK | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 47906
Sequence Length: 429
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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A0R3C7 | MTASTEAAVVVLAAGAGTRMRSDTPKVLHTLAGRGMLAHVLHTVSEIDARHLVAVLGHDRERIAPEVARLSEELGRAIDVAVQDQQLGTGHAVNCGLTALPHDFAGMVVVTSGDVPLLDTATLTGLITSHGSGDAAATVLTTTLPDPTGYGRILRTQDHEIIGIVEQADATESQRTICEVNTGVYAFDIADLRSALTRLRSDNAQHELYLTDVVEILRQDHRTVRALHVDDSALVTGVNDRVQLSDLGKVLNRRIVAAHQRAGVTIIDPGSTWIDIDVQIGQDTVVHPGTQLLGATRVGSHCVIGPDTTLTHVTVGDGASVVRTHGSESVIGAGATVGPFTYLRPGTNLGADGKLGAFVETKNCTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGENKSRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVLRDDVPPGALAVSAGPQRNIEGWVAKKRPGSAADKAARKALGDES | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 50295
Sequence Length: 482
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q1DCI1 | MSVLAAVVLCAGKGTRMKSEKAKVLHPILGRPLCAYPLKRALELGATSVVPVVGHQAEAVEKAVRGLFPDAPLRFALQREQRGTADAVRSAEEALKGYSGRVLILYGDVPLLRRETLEALLAAHDQAGGKLAMVTTTLEDPTGYGRVIRDGGKVTRIVEHKDCTPEQRAVRECNAGIYSVDADFLWKALAEIKPQNAQGEYYLTDLVEMAAKRGPVGSVEADATETAGVNDRVELAARARVLQQRINEAHMRAGVSLQDPATAYIEEGVTVGPDTEIGPSVTLAAGTVVGKGCTIGQGSVLHASTVADGTVIKPYSVLEEARVGERNVIGPFSRLRPGTELAEDVHLGNFVETKKARIGKGSKANHLTYLGDAVIGSGCNVGAGTITCNYDGVNKHLTELGDGVFIGSDTQLVAPVKVGDGSYVGAGTTVTKNVPPGSLAVSRTPQVTKEGWVATKKARQAKARAG | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 49029
Sequence Length: 466
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q67JC8 | MSDITAVLLAAGHGTRMKSDLIKVMHPLAGKPMIGHIVDNVRRAGLEDIVVVVGYQQERIREYLGDRVRYAVQSEQLGTGHAVLQAAGLIDETEGGHVLVMYGDNPFIGPELIERLIRAHVEADAAASLLTAELADPGALGRILRDPATGAFLGSVEYKDATPEQRRIREIWTGVAVFRRAGFTALLNRLDRNNAQGEYYLPQVWEILLQRGEKVQALLLASEEDALAPNDRVELARAEARLRRQINERHMRNGVTIINPDATYIDEDVEIGRDTVIWPFTFIHGKTVIGPHCKIGPMTTIVSSTVAEGCVVEQSVVEESYVGPGCRIGPMAHLRPGCELEGAAEIGNYAELKKAKVGRGVKCHHHSYLGDATIGAGANIGAGTITANYNGVEKFRTEIGSGAFIGTNVNLIAPITVGDGALIAAGSTVGPRLEIPADALVVERAQAVIKEGRAASLKEAWRQRKMNREGT | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 50885
Sequence Length: 471
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q2JII9 | MAERELSVAILAAGKGTRMRSQLPKVLHKLGSLSLIERLLRTVLTLKPHRCLVVVGYEQEQVRQALREYPVEFVEQAQQLGTGHAVQQLLPVLGGFQGDLLVINGDVPLLRAETLQALVERHRQVNPEVTLLSAQVADPYGYGRVFCDAQQRVLELVEERDCTPAQRQNRRINSGVYCFHWPALAQVLPHLNRNNAQQEYYLTDAVKRVGKAIALDVADPQEIVGVNDRRQLAQAYQILQDRLKEAWMEAGVTFVDPDSSSLEETVELAPDVVIEPQTHLRGVCRIGPGTRLGPGSWIESSEIGSGCHILYSVVSHSRIGNHVWIGPYAHVRPHSQIGDHCRIGNFVETKNAQIGSHSNAAHLAYLGDAKLGSQVNIGAGTIIANYDGQQKHFTEIGDRSKTGANSVLVAPLQVGSDVTIAAGSTIPARYPLPDDCLVIARSRPVVKPGWRLGIRSSRPQEPQPMPPGSLKIYPLRLFPGQDLKQELERLARQQPLQAGFVLSAVGSLSQATLRLADQTGDHLLSERLEILALSGSLCPDGVHLHLTVADARGQTWGGHLRPGCLIYTTAEIVLADSPEYRFSRQPDPATGYLELHIQPVAGDPCWPSPPPQPQQNQQTKPEADNSRPKSLQ | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 69354
Sequence Length: 632
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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P25462 | MAQAVVPAMQCRVGVKAAAGRVWSAGRTRTGRGGASPGFKVMAVSTGSTGVVPRLEQLLNMDTTPYTDKVIAEYIWVGGSGIDIRSKSRTISKPVEDPSELPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRGGNNVLVICDTYTPQGEPLPTNKRHRAAQIFSDPKVGEQVPWFGIEQEYTLLQKDVNWPLGWPVGGFPGPQGPYYCAVGADKSFGRDISDAHYKACLYAGINISGTNGEVMPGQWEYQVGPSVGIEAGDHIWISRYILERITEQAGVVLTLDPKPIQGDWNGAGCHTNYSTKTMREDGGFEEIKRAILNLSLRHDLHISAYGEGNERRLTGKHETASIGTFSWGVANRGCSIRVGRDTEAKGKGYLEDRRPASNMDPYIVTGLLAETTILWQPSLEAEALAAKKLALKV | 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 Length: 423
Subcellular Location: Plastid
EC: 6.3.1.2
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O29313 | MVRRLRGDCMEEVERAKAVLKENNVRQVLCAFADVRGYLQMFSIPAREFVDGSAFENGIGFDGSSVRGFRTIEKSDMVWMPDASSLKIIPWIDDPIQKSAIMFGNVYEAWGTEIADCDPRGYVAKRYEDMLKSEGMSAIFGPEIEFFLFEGVDFTRLSWDMWVSPNGGAGDSWGPPRIMPISSELESGYMIRPKEGYFRPPPEDTTVEYRNELVYYLEQLGIDIEYHHHEVATAGQVELDFKPKQLVDVGDAFYLYKFAAKNIAAMHGLYATFMPKPLYLDNASGMHTHQSLWKGEPFSGEAVFADPDDEYMLSQKARYYIGGLLEHAKALTALCAPTVNSYKRLVPGFEAPIYICWSPRNRSALVRVPMYVKKPSAIRVEYRGVDPSCNPYLAITAQLAAGLDGIKKKIDPGDPLLEDVYELTPAQKRELGVGELPTTLRDAIDHLASDELMQEVLGSHIFDAFMELKIDEWNQYCLYITPWEFMKYFDI | 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 + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 55723
Sequence Length: 491
Subcellular Location: Cytoplasm
EC: 6.3.1.2
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P34497 | MTHLNFETRMPLGTAVIDQFLGLRPHPTKIQATYVWIDGTGENLRSKTRTFDKLPKRIEDYPIWNYDGSSTGQAKGRDSDRYLRPVAAYPDPFLGGGNKLVMCDTLDHQMQPTATSHRQACAEIMHEIRDTRPWFGMEQEYLIVDRDEHPLGWPKHGFPDPQGKYYCSVGADRAFGREVVETHYRACLHAGLNIFGTNAEVTPGQWEFQIGTCEGIDMGDQLWMSRYILHRVAEQFGVCVSLDPKPKVTMGDWNGAGCHTNFSTAEMRAPGGIAAIEAAMTGLKRTHLEAMKVYDPHGGEDNLRRLTGRHETSSADKFSWGVANRGCSIRIPRQVAAERKGYLEDRRPSSNCDPYQVTAMIAQSILF | 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
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Q8HZM5 | MATSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKGVEELPEWNFDGSSTFQSEGSNSDMYLVPAAMFRDPFRKDPNKLVFCEVFKYNRKPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADKAYGRDIVEAHYRACLYAGIKIAGTNAEVMPAQWEFQIGPCEGIDMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEESIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRGASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCLLNETGDEPFQYKN | 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 the enzymes responsible for the removal of ammonia (By similarity). Essential for proliferation of fetal skin fibroblasts. Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (By similarity). Plays a role in ribosomal 40S subunit biogenesis (By similarity).
PTM: Palmitoylated; undergoes autopalmitoylation.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 42028
Sequence Length: 373
Subcellular Location: Cytoplasm
EC: 6.3.1.2
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P16580 | MATSASSHLSKAIKHMYMKLPQGEKVQAMYIWIDGTGEHLRCKTRTLDHEPKSLEDLPEWNFDGSSTFQAEGSNSDMYLRPAAMFRDPFRKDPNKLVLCEVFKYNRQSADTNLRHTCRRIMDMVSNQHPWFGMEQEYTLLGTDGHPFGWPSNCFPGPQGPYYCGVGADKAYGRDIVEAHYRACLYAGVKIGGTNAEVMPAQWEFQVGPCEGIEMGDHLWIARFILHRVCEDFGVIVSFDPKPIPGNWNGAGCHTNFSTKNMREDGGLKHIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSSIHEFSAGVANRGASIRIPRNVGHEKKGYFEDRGPSANCDPYAVTEALVRTCLLNETGDEPFEYKN | 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 acid, GABA) in a pyridoxal phosphate-independent manner .
Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 42146
Sequence Length: 373
Subcellular Location: Cytoplasm
EC: 6.3.1.2
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Q12613 | MATEAAVVSNPNTLAKYLKLDQKGSIMAEYIWIDADGETRSKSRTLKEKEYTPEDLPMWNFDGSSTGQAPGDNSDVYLKPVAVFPDPFRGSPNILVLSECWNADGTPNKYNYRHECAKLMEAHAAHEPWFGLEQEYTLLDLSNRPFGWPANGFPAPQGPYYCGVGTGKVVQRDIVDAHYKACLYSGVKISGTNAEVMPAQWEFQVGPCVGIEMGDHLWLARFLLARIAEEFGAKVSVDPKPIPGDWNGAGLHSNFSTKEMRVEGGMKHIEAAIKKLEGRHKEHIAVYGEGNEKRLTGRHETGAIDQFSYGVANRGASIRIPREYTAKGYGYFEDRRPASNADPYRITGILMETIYGSVDN | 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
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P04773 | MATSASSHLNKGIKQMYMSLPQGEKVQAMYIWVDGTGEGLRCKTRTLDCEPKCVEELPEWNFDGSSTFQSESSNSDMYLSPVAMFRDPFRKEPNKLVFCEVFKYNQKPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLLGTDGHPFGWPSDGFPGPQGLYYCGVGADKAYRRDIMEAHYRACLYAGVKITGTYAEVKHAQWEFQIGPCEGIRMGDHLWVARFILHRVCKDFGVIATFDSKPIPGNWNGAGCHTNFSTKTMREENGLKHIKEAIEKLSKRHRYHIRAYDPKGGLDNARRLTGFHKTSNINDFSAGVADRSASIRIPRTVGQEKKGYFEARCPSANCDPFAVTEAIVRTCLLNETGDQPFQYKN | 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 the enzymes responsible for the removal of ammonia (By similarity). Essential for proliferation of fetal skin fibroblasts. Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (By similarity). Plays a role in ribosomal 40S subunit biogenesis (By similarity).
PTM: Palmitoylated; undergoes autopalmitoylation.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 42320
Sequence Length: 373
Subcellular Location: Cytoplasm
EC: 6.3.1.2
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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
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Q2N784 | MTDPKVPRQRRIIDRRKLAAAVEALAEQQGEKARPAVLKVLREALEKGRDELSQRLLDRPSAGHQITAGHAFLVDQLVRVIFDHVTTHLYPVANRSSSERIAVLAVGGYGRAEMAPQSDVDIAFLHPSRRTPWCEQVTEAMLYFLWDLGFKVGQSSRTPEDMVRMAREDLTIRTALLEARFVWGDRELYDEARKRFWSEVVNGTERQFVAEKLAERDARHERMGGTRYVVEPNVKEGKGGLRDLQTLYWIGKYIHRARGAAELVDAGLLTETEYHGFRRAEGFLLAVRCHLHEITGRPEDRLTFDFQKQIAERMRFAERREKSAVERFMQYYFLQVKRVGSLTGVFLAQMDQQFARKRARTGLLAGFNAKSRMLKGYTVFGGKIAAPGDNWFRDDPVRLIEIFQLAEANGLEIDPRSMRQADRDSVLIKDQVRNDPRANAIFLDLLCGRNDPETALRWMNEAGVFGKFVPDFGRVNAQMQFNMYHHYTVDEHTIRAIGFLSKIEKGELAKEHPRSTREIHKVKSRRVAFVAALLHDIAKGRGGDHSILGAEVAEELCPRFGLDEDETDLVAWLVLQHLLMSSTAQKRDLTDPKTIEDFVAEVQSLERLRHLAILTSVDIRAVGPGTWNSWKGQLLGELYDAAHERLRLGHMKHHRSERVAAKKEAVREALGGKAALLEKHGRLLPDSYWIAEPENVISRNIVQYDVAREISEDLSIHCEFDEERGATLVTVIAADHPGLFYRIAGGIHLAGGNIIDARIHTTRNGWAIDNYLVQDPVGQPFAEERQLARIEQAIADAIANRGELVPKLAKRPLKQTRAGAFDVRPRVLFDNDASGRFTVIEVNARDRAALLNRLGRALFENQVIVQSAHITAYGERAADTFYVTDLTGAKITDESRMDTIRQALLDAASDARQAELEPA | 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 glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Mass (Da): 104003
Sequence Length: 919
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
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Q5FPT6 | MKETSFWGETPSLSFADDTDKPLSDRTASPPCDPASSLQTALDTAAAQGQTTRENVLSILRRHLGSGNATVRREFEKRRMSGIDAARALARQADDMVCALAELAAQKHESPGETLCLCATGGYGAGLLAPFSDIDILFLIPGDPTPAMTARIEFILYALWDLGLRVGHATRSIAECVRDADSDLTIRTALLDLRFLHGERGLARDLRCALGADLQNDRLCEFVMGKIAEREQRHRRFGDNPYMVEPNIKEGRGGLRDLQTLNWMGRAALGCAVSTPDRSGQPAEAPQTPSFASFGLLTDRESLRARRSWDFLWTVRLHLHYITGRAEERLTFDVQPVIGGRMGYATHGRQRGVERFMRHYFLTARDVMRLTSVLQPVVLMHLQDQTTGEPPKVVPGPEEFQTIAGRICPIEPVTFAAQPREMFRLLDCGRRHDLPLHPIAMQQIIRNERHAVTLRDDPETAKIFLDLLCEPSADETKAVPFWLPILNETGLLGRLLPDWSRVVGQMQFDSYHIYTVDEHIVEAVRMMGQIEAGRMADEIPLAYTLASDLRSRRALYVAVLLHDIGKGRGGDHSEIGADLALTICPQLGLDPEETDTVSWLVLHHLLLSQTAFTRDIDDPRTILDLADTIQSPERLRLLLLLTIADMRAVSPKVWNAWKATLLRELFSRVAEVLEGGLAATERDSRVNHARELARDGLTGILPESSIDRFLDLGYPSYWLGFDTDTQMRHARMVHDSDRYRSPVTVEAYPIPERGVTELTVLCADHPGLFSQIAGALAVSGASIVDARIHTLSDGMALDTFWVQDGEGCSFEEPHQLGRLNHLVEQALSGRLDIRKGIEDASHHSTSRRMRAIHVPPRVVIDNTASDRHTVIEVNGRDRPGLLHDVTSALSSASLQISSAHITTYGMRAVDVFYVRDLLGMKITDPVRLARLRETLLASLTSAPVTTPAS | 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 glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Mass (Da): 105398
Sequence Length: 949
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
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P43919 | MLFSPTLSSLLTPSAVKIERENLKQFELENFSCYSIFELIENRCDFYDALLIQLWQEIGLSEQQGISLIAVGGYGRREMFPLSDLDFLILVEQTPSHEIEEKITQFIQFLWDCGFEVGNSVRTLEQCELEGKQDITIATNLLEARFLTGNRPHFDVLNELVKRADFWSKEDFFNAKVQEQIERYQRYHNTAYNLEPDIKFSPGGLRDLHLLYWVALRHSGALTLEAILQSGFIYPQEYQQLQESRAFLFKVRFALHLILKRYDNRLLFDRQIKVSELLGFRGEGNPAVEKMMKCFFQALHRISLISNLLIQHYRENVLSSNQDTVIDQLDDDFQLINQSLCLRNSFVFQEKPARILDLFFYLTQYEHVNIHSDTLRQLQISLEQLSQKLCEIPAAREKFLRLFNQSNAIKRAFMPMHQYGVLTAYLPQWQAIEGLMQFDLFHIYTVDEHTLRVMLKLESFLPKGSAQEHPIAHRIFSQLSDRTLLYIAALFHDIAKGRGGDHAELGAEDVADFAQLHGLDRREIDTLAWLVQSHLLMSITAQRRDIHDPEVVMNFAEAMQNQVRLDYLTCLTVADICATNGNLWNSWKRSLFASLYEFTEQQFSQGMKELLDYSEKSAENRKLAQQILTQDYSDITSISIEKLWTRCPEDYFVRNTPKQIAWHTSLLVDFVEALLVKISNRFSLGGTEVFIYCQDQPHLFNKVVSTIGAKKFSIHDAQIITTQDGYVFDSFIITELNGELVEFDRRRELEQALTVALQSEKLPALSIVPNRQLQHFTVQTDVRFLQENKKEHTEMELVALDKAGLLAQVSQIFTELNLNLLNAKITTVGEKAEDFFILTNQFGQALAREERERLNSVIIQQIR | 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 glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Mass (Da): 100173
Sequence Length: 863
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
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Q31G41 | MATTTDKQVSPTSPSFVYNLDHEDRNTSLKSGRAVLTDFNEQQFVKFDKGCSIETLLKERTSFIDQLLKKIWEHFFSKDECEQLTLVAVGGYGRGELQPYSDIDLLILGENFIELQPKIVEFITYLWDIGFEVGHAVRNLEDCIEAGREDVTTATNLLEARWLAGNYEQFLSLQNLFNLKSFWPSHEFFQAKLEEQEKRHKRYNDTLYQLEPNIKESPGGLRDIQTILWVAKRHFGASSLQELMQHNFISLQEYKEIQAAYLYLNRIRFALHRLKKRHEDRLLFDHQQQLAELLNHDDRPEHNDSIKAVEAFMKPYYQNAHIVARLNEILLQHFKEEIYHFAEDKIEPINPRFRIINNYLDVVKENLFAKNPTALLEIFIIIENYQHLIQGIRSRTIRLIRNHLHLIDDQFRSDPINKALFIEIFRQPKGVNAAVKRMYAYGILGAYLPSFKKITGLMQFNIFHAYTVDEHTILVIRNLRRFFIKQHAYEFPTAHQIATQLCKPEILLLAGLFHDIAKGRNGAHEKLGAVDAKAFSQKHNLNKNDTDLLSWLVLRHLDFSYVAQKKDLSDPEIIQQFAEKVGTQQRLDYLYLLTLADVRSTSDEVWNDWKNQLFLQLYHNTTQALDSSSSQPRDRVKQAIFNKEKASELLKKRGLIPMHFQGFWQAFEQTDFFNRQSAAEIARITRVLFEEDHEAINIHLQPTTSRGATELIIYMHDRDYLFAQFTQIIDKLDLNIVEAKIYSGEDDMTLVIIYLLNRESTSITDPMILTEIEETLKHQLFLKDDTMPPTQPEPRRIRVFEMPTHIQFQEINEELTELSISTKDIPGLLAKIGQAFKSCKIRVHDAKINTVGEKAEDTFMISSTTNESIHTRHSQEELKQALLNNIEQ | 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 glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Mass (Da): 103724
Sequence Length: 888
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
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Q5QXT0 | MANVQEDKDFHGRWPDRTLQPCLKDYKALLESYQNWSAARFVTADIDELVHHRATFFDQLISQLWQQFQLEDEPASILAVGGYGRETLHPGSDIDLLILVGPENAEAEAKLSEKLGQFVTFLWDLHLDIGHSVRTIEDCFAQSENDITIATNLIESRYLSGAESLYNEFHQQLLNDFPWSSRDFYQAKLDEQKQRHQQYHSTSYNLEPNIKSSPGGLRDIQTVGWIAKRHFRTHSDENLVEYGYMTADEFVELRDCMNWLWRIRFALHLEAGKREDRLLFDFQPGVAVRLGYGNDGKASVETMMKDYFKVVLRVSELNQMLLQFFHQAILGTQDLQHAEHISDDFAVANKLLTARHDNVFDNHCNIIRAFVCIAEHPQIQGIHSNTIRLLRNARAQLSEPLSHDPECRDLFNQLIQHPRGCGLSFALMHHHSVLASYLSQWQQIVGQMQFDLFHAYTVDEHTFRLVRNLYRFSDEDYQDQFPLCEKLVAQMDRRYCLYLAGIFHDIAKGRGGDHSELGEMDARNFCHQHGYSEEDAELVAWLVRHHLTMSVTAQKRDIHDPEVIQDFANQVSTPERLDYLYCLTVADIRATNQSLWNNWKATLLEELYNATSYLLQQDSNKPTLDIRQKINENKASAMALLLSAGFEKAEILALWGRFTADYFFRHTAEQISWHSQHILNLPSEQLPLILIGDENNYGTTELFIYHHEEGHLFASVAGVLDSQQLNILDAQILATRDGFVMDTFVVLQRDGKPLTEPHRIEEVKQQLLDVLHKRIPVPSTKRPLSRRMKNFSVATEVTFIPSKHHGRTTFELVTLDRPGLIAKLAAILQQQNVILLAAKITTIGEQAEDLFIVTTEQQTALSDKQKKTLKAKIIKDLEF | 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 glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Mass (Da): 101332
Sequence Length: 879
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
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P41393 | MSNSLSNTVPPDLSAQPENPGEWPKSDFNCATIKALIDAFQRWLGEAFDSGIAAERLIEARTEFIDQLLQRLWVEYGFGSINDIALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGERLALLWDIKLEVGHSVRTLEECLLEGLSDLSVATNLIESRLLIGDVALFLELQKHIFSDGFWPSEKFFAAKVEEQNDRHQRYHGTSYNLEPDVKSSPGGLRDIHTLQWIARRHFGATSLDEMVGFGFLTEAERNELNECLHQLWRIRFALHLELNRYDNRLLFDRQFSVARRLRYEGESNQPIEHMMKDFFRVTRRVSELNQMLIQLFEEAILALTEDEKPRPIDDDFQLRGTLIDLRDDTLFIREPQAILRMFYTMVRNSSITGIYSTTVRHLRHARRHLTQPLCYIPEARTLFLSMLRHQGGLSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFAKEETRSRHPLWLELWPRLTHPELILIAALFHDIAKGAGGDHSILGAQDVLKFAELHGLNCAQTQLVAWLVRHQLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLHYLVCLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMENINEQALHQIWNRCRANYFVRHTPNQLAWHARNLLKHDLSKPMILLSSHATRGGTEIFIWSPDRPYLFAAVSAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRTQMIRVGLEQTLSQRSWQPPAPRRQAAKLRHFSVPTEVNFLPTHTDRKSFLELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVQQRLTEALNPNDKG | 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 glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism (Probable).
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Mass (Da): 102344
Sequence Length: 887
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
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