ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9FHH5 | MEGRQYYPPRENVEGNRTTMGGGPHSPWHSPVPYLFGGLAAMLGLIAFALLILACSYWRLSGYLDGEENQSRERDLEVGDVKPDKTAVKPVALPEKFLVIMAGNVKPTYLATPSVKTCTCDDDDDEDDDVEGSDQVVPRSSESNGETH | Function: Probable subunit of an amino acid transporter involved in the regulation of the amino acid metabolism. Stimulates amino acid export by activating nonselective amino acid facilitators. Acts upstream genes involved in the salicylic acid (SA) pathway and in the geminivirus-host interaction.
Location Topology: Si... |
Q64MA3 | MGVGGSFWDLLKPYARHEGAGYLRGRRVAVDLSFWVVSHSAAIRARSPHARLPHLRTLFFRTLSLFSKMGAFPVFVVDGQPSPLKSQVRAARFFRGSGMDLAALPSTEAEASADALVQPRNAKFTRYVEDCVELLEYLGMPVLRAKGEGEALCAQLNNQGHVDACITSDSDAFLFGAKTVIKVLRSNCKEPFECYNMADIESGLGLKRKQMVAMALLVGSDHDLHGVPGFGPETALRFVQLFDEDNVLAKLYEIGKGVYPFIGVSAPNIDDLPSPSTKSLPRARSPHCSHCGHPGNKKNHIKDGCNFCLVDSLENCVEKP... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Endonuclease which cleaves flap structures at the junction between single-stranded DNA and double-stranded DNA. Possesses both si... |
Q9M2Z3 | MGVKYLWDVLEPCKKTFPLDHLQNKRVCVDLSCWMVELHKVNKSYCATKEKVYLRGFFHRLRALIALNCSIILVSDGAIPGIKVPTYKRRLKARFEIADDGVEPSKETSLKRNMGSEFSCIIKEAKVIASTLGILCLDGIEEAEAQCALLNSESLCDACFSFDSDIFLFGAKTVYREICLGEGGYVVCYEMDDIKKKLGLGRNSLIALALLLGSDYSQGVRGLRQEKACELVRSIGDNVILEKVASEGLSFAEKPRKSKKQVRPSVCSKKGTLPLVVINGNNRDPERLEEIKQVIDAFMNPKCHQADSNTVSRALAEFSF... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Endonuclease which cleaves flap structures at the junction between single-stranded DNA and double-stranded DNA with a specific cl... |
Q8W5R1 | MGVKNLWDILESCKKKLPLHHLQNKKVCVDLSCWLVQMYSANRSPAFAKDKVYLKNLFHRIRALLALNCTLLFVTDGAIPSLKLATYRRRLGSISHAAKESDQPNSHPSISLRRNKGSEFSCMIKEAKRLGMALGIPCLDGLEEAEAQCASLDLESLCDGCFTSDSDAFLFGARTVYRDVFIGEGGYVICYEMEDIEKTLGFGRNSLISLAVLLGSDYSNGVNGFGPETACRLVKSVGDNLILDQILSNGVKATRKCKGKNSGNKVDDMCPKASSCEVGMTQDSDGQFRDVINAYLEPKCHSPDSEAVQRVCGQHPFLRP... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Single-stranded DNA endonuclease activity in vitro . May not be active as double-stranded DNA endonuclease . Endonuclease which c... |
Q9VRJ0 | MGVKELWGVLTPHCERKPINELRGKKVAIDLAGWVCESLNVVDYFVHPRHHLKNLFFRTCYLIWEQVTPVFVLEGVAPKLKSQVIAKRNELQFRGVKPKNSPECTQSQPSKGDKGRSRFNHVLKQCETLLLSMGIQCVQGPGEAEAYCAFLNKHGLVDGVISQDSDCFAYGAVRVYRNFSVSTQGAQAAAGGAVDIYDMREITSRMDFGQQKIIVMALLCGCDYCPDGIGGIGKDGVLKLFNKYKETEILDRMRSWRGETDKYNALEIRVDDKSICSNCGHIGKTQSHTKSGCSVCRTHKGCDESLWKEQRLSIKSELTL... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Endonuclease which cleaves flap structures at the junction between single-stranded DNA and double-stranded DNA. Specific for 5'-o... |
Q17RS7 | MGVNDLWQILEPVKQHIPLRNLGGKTIAVDLSLWVCEAQTVKKMMGSVMKPHLRNLFFRISYLTQMDVKLVFVMEGEPPKLKADVISKRNQSRYGSSGKSWSQKTGRSHFKSVLRECLHMLECLGIPWVQAAGEAEAMCAYLNAGGHVDGCLTNDGDTFLYGAQTVYRNFTMNTKDPHVDCYTMSSIKSKLGLDRDALVGLAILLGCDYLPKGVPGVGKEQALKLIQILKGQSLLQRFNRWNETSCNSSPQLLVTKKLAHCSVCSHPGSPKDHERNGCRLCKSDKYCEPHDYEYCCPCEWHRTEHDRQLSEVENNIKKKA... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Endonuclease which resolves Holliday junctions (HJs) by the introduction of symmetrically related cuts across the junction point,... |
H1ZV38 | MNDTQDFISAQAAVLRQVGGPLAVEPVRISMPKGDEVLIRIAGVGVCHTDLVCRDGFPVPLPIVLGHEGSGTVEAVGEQVRTLKPGDRVVLSFNSCGHCGNCHDGHPSNCLQMLPLNFGGAQRVDGGQVLDGAGHPVQSMFFGQSSFGTHAVAREINAVKVGDDLPLELLGPLGCGIQTGAGAAINSLGIGPGQSLAIFGGGGVGLSALLGARAVGADRVVVIEPNAARRALALELGASHALDPHAEGDLVAAIKAATGGGATHSLDTTGLPPVIGSAIACTLPGGTVGMVGLPAPDAPVPATLLDLLSKSVTLRPITEG... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD(+)-dependent oxidation of geraniol to geranial. Is involved in the anaerobic degradation of the monoterpene beta-myrcene. Can also catalyze the oxidation of (S)-perillyl alcohol to perillyl aldehyde, and to a lesser extent, the oxidation of nerol, c... |
H1ZV37 | MTIDHQHIFVGGQWIAPKSTQRSNILNASTEELVGSVPKCNNEDMDRAVAAAREAMRSLAWAGLDGKGRAQHLRRFADAVERRGQQLARSVSLQNGMPINVADQLESAFVVSLLRYYASLAENLVEEEARPSPTGSTTLVRRDPVGVVGAIIPWNFPVALSIFKIAPALAAGCAVVVKPSSGTVLDSYVLAEAAAEAGLPPGVINWVPGDRGIGSHLVSHPGVDKVAFTGSTSAGRIIAEACARLLRPVTLELGGKSAAIVLEDADLDALIRSLPMSSVLNNGQACFSCTRILAPAGRYDEVVDAIAGAVSAYSVGDALD... | Function: Catalyzes the NAD(+)-dependent oxidation of geranial to geranic acid. Is involved in the anaerobic degradation of the monoterpene beta-myrcene. Seems to be specific for the trans-isomer geranial, since it does not act on the cis-isomer neral.
Catalytic Activity: (2E)-geranial + H2O + NAD(+) = geranate + 2 H(+... |
P0CM25 | MSDLEPLDPTLQNILDQKSLKWIFCGGKGGVGKTTTSCSLAVQLAACRESVLLISTDPAHNLSDAFSQKFGKDATKVNGFDNLYAMEIDPNGSLQEMIESSDQTGGMGGMMQDLAFAIPGVDEAMGFAEIMKHVKSMEFSVIVFDTAPTGHTLRFLSFPSVLEKALGKLSTLGGKFGPMIQQMQSMFGGGAPQEDMFAKLESMREIITEVNNQFKDPEKTTFVCVCISEFLSLYETERLIQELTSYEIDTHNIVVNQLLFPKAGDNCEQCSVRHNMQQKYLKEAYDLYEDEFHIVKLPLLTEEVRGVEKIKEFSKMLTQP... | 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 ... |
Q6IQE5 | MAASVEDEFEDAPDVEPLEPTLKNIIEQKSLKWIFVGGKGGVGKTTCSCSLAVQLAAVRESVLIISTDPAHNISDAFDQKFSKVPTKVKGYDNLFAMEIDPSLGVAELPDEFFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCRIDTHNIIVNQLVFPDNERPCKMCEARHKIQSKYLDQMEDLYEDFHIVKLPLLPHEVR... | 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, ... |
O43681 | MAAGVAGWGVEAEEFEDAPDVEPLEPTLSNIIEQRSLKWIFVGGKGGVGKTTCSCSLAVQLSKGRESVLIISTDPAHNISDAFDQKFSKVPTKVKGYDNLFAMEIDPSLGVAELPDEFFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCKIDTHNIIVNQLVFPDPEKPCKMCEARHKIQAKYLDQMEDLYEDFHIVKLPL... | 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, ... |
B0CPJ0 | MSTDLLPPTLQNILDQTSLKWIFCGGKGGVGKTTTSCSLAIQLAKCRKSVLLISTDPAHNLSDAFGQKFSKDATKVNGFDNLFAMEIDPTSAIQEMVEQCMLADSNGMMGSMMQDLAFAIPGVDEAMSFAEIMKHVHVKSMEYSVIVFDTAPTGHTLRFLSFPTVLEKALGKLSSLGSRFGPMISQMSSMMGGEAGSQEDMFAKLESMRGVITEVNTQFKDPEKTTFVCVCISEFLSLYETERLVQELTAYEIDTHNIVVNQLLFPKKSSNCEHCSVRQKMQQKYLAEAHELYDEFFHIIQLPLLTEEVRGPEKLNEFSK... | 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 ... |
B8AN27 | MQAGGGGDAGDTRGRHRIQAELKKLEQEARFLEEELEELDKTDKVSAALQELMVTAESKADPLLPVTTGPACQSWDRWFEGPQDLRRCKCWFL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Location Topology: Lipid-anchor
Sequence Mass (Da): 10491
Sequence Length: 93
Subcellular Location: Cell membrane
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Q9UJY5 | MEPAMEPETLEARINRATNPLNKELDWASINGFCEQLNEDFEGPPLATRLLAHKIQSPQEWEAIQALTVLETCMKSCGKRFHDEVGKFRFLNELIKVVSPKYLGSRTSEKVKNKILELLYSWTVGLPEEVKIAEAYQMLKKQGIVKSDPKLPDDTTFPLPPPRPKNVIFEDEEKSKMLARLLKSSHPEDLRAANKLIKEMVQEDQKRMEKISKRVNAIEEVNNNVKLLTEMVMSHSQGGAAAGSSEDLMKELYQRCERMRPTLFRLASDTEDNDEALAEILQANDNLTQVINLYKQLVRGEEVNGDATAGSIPGSTSALL... | Function: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif . Mediates export of the GPCR... |
A5UNX8 | MIETDVLVIGGGPAGSSAAKHAALGGAKVILLDKRSEIGAPKRCAEGVSKKGLAKLGIEPSPRWITKEIDGVRLTSPDGTDVWLTEEEIELPEAGYILERKVFDKHMAMDAARAGAEIRIKTLATGMDKIEDGFIVSTESMGKTEEIKAKIVIAADGPEGHVARWAGLKGSAKAKEMESGVQYEMVNVEFDREAVIEFYFGSCAPGGYVWIFPKGDDIANVGLAILQHKATKPAIEYLDDFIAKCPATKNAQAVELNVGGDPVGGMPKKMYDDNILVCGDAAGQVNPLTGGGIISGMTGGMYAGQVAAEAIKEGDHSKKF... | Cofactor: Binds 1 FAD per subunit.
Function: Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-g... |
Q4JA33 | MKELKYDVLIIGGGFAGSSAAYQLSRRGLKILLVDSKPWNRIGDKPCGDAVSKAHFDKLGMPYPKGEELENKINGIKLYSPDMQTVWTVNGEGFELNAPLYNQRVLKEAQDRGVEIWDLTTAMKPIFEDGYVKGAVLFNRRTNEELTVYSKVVVEATGYSRSFRSKLPPELPITEDLDDKDADVAYREVLLTKEDIEDHDYLRIFIDQETSPGGYWWYFPKGKNKVNVGLGIQGGMGYPSIHEYYKKYLDKYAPDVDKSKLLVKGGALVPTRRPLYTMAWNGIIVIGDSGFTVNPVHGGGKGSAMISGYCAAKAILSAFE... | Cofactor: Binds 1 FAD per subunit.
Function: Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-g... |
Q9HKS9 | METYDVLVVGGGPGGSTAARYAAKYGLKTLMIEKRPEIGSPVRCGEGLSKGILNEADIKADRSFIANEVKGARIYGPSEKRPIILQSEKAGNEVGYVLERDKFDKHLAALAAKAGADVWVKSPALGVIKENGKVAGAKIRHNNEIVDVRAKMVIAADGFESEFGRWAGLKSVILARNDIISALQYRMINVDVDPDYTDFYLGSIAPAGYIWVFPKGEGMANVGIGSSINWIHNRFELKNYLDRFIENHPGLKKGQDIQLVTGGVSVSKVKMPITMPGLMLVGDAARLIDPITGGGIANAIVSGMYAAQVTKEAIESNDYS... | Cofactor: Binds 1 FAD per subunit.
Function: Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-g... |
Q5JE27 | MTWKYDVVVVGSGIAGPIVARNVAKAGFSVLLIDKKWAIGTPKQCAEAISIKVFDKYDIPYDKRFINREIYGAKLYSPSGYELEMRYKEVSGVILERKVFDKMLAYYAAKAGADVLARTEALDVIRKDGKIVGIKAKHEDEPVEIYADIIVAADGVESTIARKAGINTYAPPHEFDSGYEYEMLIEGFDPDLIHLWFGNEVAPRGYVWVFPKDEDRANVGIGINSDNPKTAKYYLDKWLEENNIPAKKLLEINVGLIPVGGFVKELAKDNVVVVGDAARQVNPMHGGGMAEAMEAGTIASKWIVKALEEENLSLLQNYTK... | Cofactor: Binds 1 FAD per subunit.
Function: Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-g... |
A0A2I6PJ05 | MVPNANSNTVSLQSPNAIPPRTSSTGYITPFPPAKSVLRPVPESDWLGQNNTRNRSSSTTAIPLTGMHATGPQDPARYETEDLNYTSRKTWSEQKEKVLVGPFEYLFAHPGKDFRTLMVNSFNAWLEVPQESLDVITKVVGMLHTASLLVDDVEDNSLLRRGLPVAHSIFGTAQTINSANYVYFCALQELQKLKNPEAINVYTEELLNLHRGQGMDLFWRDTLTCPTEEEYLEMVGNKTGGLFRLAIKLMQAESGTPIDCVPLVNILGIIFQIQDDYRNLSSPEYGQNKGLCEDLTEGKFSFLIIHSIRSNPSNLQLLNI... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Catalyzes the trans-addition of the 3 molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl pyrophosphate (GGPP). GGPP is a precursor for the biosynthesis of many secondary metabolites, including the indole diterpene... |
A7LXT8 | MRNALFLIFISLCSVCKSSAQGYSNPVIPGFHPDPSVCKAGDDYYLVNSSFQYFPGVPLFHSKDLVHWEQIGNCLTRPSQLDLTNANSGSGIFAPTIRYNDGVFYMITTNVSGKGNFLVHTTDPRSEWSEPVWLEQGGIDPSLYFEDGKCFMVSNPDGYINLCEIDPMTGKQLSSSKRIWNGTGGRYAEGPHIYKKDGWYYLLISEGGTELGHKVTIARSRYIDGPYQGNPANPILTHANESGQSSPIQGTGHADLVEGTDGSWWMVCLAYRIMPGTHHTLGRETYLAPVRWDKDAWPVVNSNGTISLKMDVPTLPQQEM... | Function: Alpha-L-arabinofuranosidase involved in xyloglucan degradation by mediating the cleavage of terminal non-reducing alpha-L-arabinofuranoside residues in xyloglucan branches, converting the 'S' units to 'X' units.
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alph... |
A7LXU0 | MMKNSCRLLLILIGLWMANVSLAQKTFRNPIITGMNPDPSICRVGDDFYLVTSTFEYFPGLPVYHSKDLVHWKLIGHALSRPENNPLMGCNASTGGQYAPTLRYHDGTFYVIGTNYGGKGSQGVFYVTAKNPAGPWSDPVWVGNWYVDPSIEFIDGKMYFLSPDNQGSFLLGVMDPETGTFVEALRKVASGLGGSSPEGPHFYKIGDYYYIMSAEGGTGYEHREVIQRSKSPWGPYEPSPVNPVLSNMNCPDHPFQAIGHADLVQLKDGSWWAVCLGIRPVNGKYQHLGRETFLAPVTWDADGWPKVGKDGVVQETYLFP... | Function: Alpha-L-arabinofuranosidase involved in xyloglucan degradation by mediating the cleavage of terminal non-reducing alpha-L-arabinofuranoside residues in xyloglucan branches, converting the 'S' units to 'X' units.
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alph... |
C0HLA0 | MTSAGVAPTALRLLTALLLLLVAAPSHSLPLLTRGRWIVDEATGLRVKLACVNWVGHLEPGLPEGLNRLPVATVAHTISSLGFNCVRLTYSIHMLTRTSYTNATVAQTFARLNLTEAASGIEHNNPELLDLGHVAAYHHVVAALSEAGVMVILDNHVSKPKWCCAVDDGNGFFGDRYFNPNTWVEGLGLMATYFNNTPNVVAMSLRNELRGNRSTPISWSRHMQWGAATVHKANPKVLVILSGLQFDTDLSFLPVLPVTLPFKEKIVYEGHWYSFGVPWRTGLPNDVCKNETGRFKSNVGFVTSSANATAAPLFMSEFGI... | Function: May have glycosyl hydrolase activity.
PTM: Glycosylated.
Sequence Mass (Da): 61637
Sequence Length: 556
EC: 3.2.1.-
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B2ADA5 | MRAVYAILAGLLATGSASPLEARQSGNPFVGRSLFVNPKYSESLERTRQAFLSRGDQTNAAKVQYVQNKVGTFVWISNIFLLRDIDDAIRNARAAQSRGEKPIVGLVLYNLPDRDCSAGHSSGELSLDQNGLNRYRTEYVQPFAQKLKAASDLQFAVILEPDAIGNMVTGTTAFCRNARGPQQDGIAYAIQQLQASNIHLYLDVANGGWLGWADNLKPTTILQKAGSNARIRGYSSNVSNYNPYSTNNPPPYTAGSPSADESRYATSLGNALRERGLPTNFIIDQGRVALDGARKEWGEWCNVSPAGFGQPFTTNTNNPN... | Function: Probable exoglucanase that may play an important function in biomass degradation by catalyzing the hydrolysis of cellulose.
Sequence Mass (Da): 45612
Sequence Length: 429
Subcellular Location: Secreted
EC: 3.2.1.-
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D4HRL0 | MSLAVVFLLGFLAVSHGQQAGTETEEYHLPLTWERDGSSVSASVVIDSNWRWTHSTEDTTNCYDGNEWDSTLCPDADTCTENCAIDGVDQGTWGDTYGITASGSKLTLSFVTEGEYSTDIGSRVFLMADDDNYEIFNLLDKEFSFDVDASNLPCGLNGALYFVSMDEDGGTSKYSTNTAGAKYGTGYCDAQCPHDMKFIAGKANSDGWTPSDNDQNAGTGEMGACCHEMDIWEANSQAQSYTAHVCSVDGYTPCTGTDCGDNGDDRYKGVCDKDGCDYAAYRLGQHDFYGEGGTVDSGSTLTVITQFITGGGGLNEIRRI... | Function: Exocellobiohydrolase (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose . The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-gluc... |
Q9H936 | MADKQISLPAKLINGGIAGLIGVTCVFPIDLAKTRLQNQQNGQRVYTSMSDCLIKTVRSEGYFGMYRGAAVNLTLVTPEKAIKLAANDFFRHQLSKDGQKLTLLKEMLAGCGAGTCQVIVTTPMEMLKIQLQDAGRIAAQRKILAAQGQLSAQGGAQPSVEAPAAPRPTATQLTRDLLRSRGIAGLYKGLGATLLRDVPFSVVYFPLFANLNQLGRPASEEKSPFYVSFLAGCVAGSAAAVAVNPCDVVKTRLQSLQRGVNEDTYSGILDCARKILRHEGPSAFLKGAYCRALVIAPLFGIAQVVYFLGIAESLLGLLQD... | Function: Mitochondrial glutamate/H(+) symporter. Responsible for the transport of glutamate from the cytosol into the mitochondrial matrix with the concomitant import of a proton . Plays a role in the control of glucose-stimulated insulin secretion (By similarity).
Catalytic Activity: H(+)(in) + L-glutamate(in) = H(+)... |
Q9D6M3 | MADKQISLPAKLINGGIAGLIGVTCVFPIDLAKTRLQNQQNGQRMYASMSDCLIKTIRSEGYFGMYRGAAVNLTLVTPEKAIKLAANDFFRHQLSKDGQKLTLPKEMLAGCGAGTCQVIVTTPMEMLKIQLQDAGRIAAQRKILAAQAQLSAQGGAQPSVEAPAPPRPTATQLTRDLLRNHGIAGLYKGLGATLLRDVPFSIVYFPLFANLNQLGRPSSEEKSPFYVSFLAGCVAGSAAAVAVNPCDVVKTRLQSLERGVNEDTYSGFLDCARKIWRHEGPSAFLKGAYCRALVIAPLFGIAQVVYFLGIAESLLGLLQE... | Function: Mitochondrial glutamate/H(+) symporter. Responsible for the transport of glutamate from the cytosol into the mitochondrial matrix with the concomitant import of a proton (By similarity). Plays a role in the control of glucose-stimulated insulin secretion (By similarity).
Catalytic Activity: H(+)(in) + L-gluta... |
Q5RD81 | MADKQISLPAKLINGGIAGLIGVTCVFPIDLAKTRLQNQQNGQRMYTSMSDCLIKTIRSEGYFGMYRGAAVNLTLVTPEKAIKLAANDFFRHQLSKDGQKLTLLKEMLAGCGAGTCQVIVTTPMEMLKIQLQDAGRIAAQRKILAAQGQLSAQGGAQPSVEAPAAPRPTAIQLTRDLLRSRGIAGLYKGLGATLLRDVPLSVVYFPLFANLNQLGRPASEEKSPFYVSFLAGCVAGSAAAVAVNPCDVVKTRLQSLQRGVNEDTYSGILDCARKILRHEGPSAFLKGAYCRALVIAPLFGIAQVVYFLGIAESLLGLLQD... | Function: Mitochondrial glutamate/H(+) symporter. Responsible for the transport of glutamate from the cytosol into the mitochondrial matrix with the concomitant import of a proton (By similarity). Plays a role in the control of glucose-stimulated insulin secretion (By similarity).
Catalytic Activity: H(+)(in) + L-gluta... |
A0A0G2K5L2 | MADKQISLPAKLINGGIAGLIGVTCVFPIDLAKTRLQNQQNGQRMYASMSDCLIKTIRSEGYFGMYRGAAVNLTLVTPEKAIKLAANDFFRHQLSKDGQKLTLPKEMLAGCGAGTCQVIVTTPMEMLKIQLQDAGRIAAQRKMLAAQAQLATQGGGQPSVEAPAAPRPTATQLTRDLLRNHGIAGLYKGLGATLLRDVPFSIVYFPLFANLNQLGRPSSEEKSPFYVSFLAGCVAGSAAAVAVNPCDVVKTRLQSLERGVNEDTYSGFLDCARKIWRHEGPSAFLKGAYCRALVIAPLFGIAQVVYFLGIAESLLGLLQE... | Function: Mitochondrial glutamate/H(+) symporter (By similarity). Responsible for the transport of glutamate from the cytosol into the mitochondrial matrix with the concomitant import of a proton (Probable). Plays a role in the control of glucose-stimulated insulin secretion .
Catalytic Activity: H(+)(in) + L-glutamate... |
Q9H1K4 | MTHQDLSITAKLINGGVAGLVGVTCVFPIDLAKTRLQNQHGKAMYKGMIDCLMKTARAEGFFGMYRGAAVNLTLVTPEKAIKLAANDFFRRLLMEDGMQRNLKMEMLAGCGAGMCQVVVTCPMEMLKIQLQDAGRLAVHHQGSASAPSTSRSYTTGSASTHRRPSATLIAWELLRTQGLAGLYRGLGATLLRDIPFSIIYFPLFANLNNLGFNELAGKASFAHSFVSGCVAGSIAAVAVTPLDVLKTRIQTLKKGLGEDMYSGITDCARKLWIQEGPSAFMKGAGCRALVIAPLFGIAQGVYFIGIGERILKCFD | Function: Responsible for the transport of glutamate from the cytosol into the mitochondrial matrix with the concomitant import of a proton (symport system).
Catalytic Activity: H(+)(in) + L-glutamate(in) = H(+)(out) + L-glutamate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33849
Sequence Le... |
Q9DB41 | MIACRMSSQDLSISAKLINGGIAGLVGVTCVFPIDLAKTRLQNQQGKDVYRGMTDCLMKTARAEGFLGMYRGAAVNLTLVTPEKAIKLAANDFLRQLLMQDGTQRNLKMEMLAGCGAGICQVVITCPMEMLKIQLQDAGRLAVCHQASASATPTSRPYSTGSTSTHRRPSATLIARELLRTQGLSGLYRGLGATLLRDIPFSIIYFPLFANLNQLGVSELTGKASFTHSFVAGCTAGSVAAVAVTPLDVLKTRIQTLKKGLGEDTYSGVTDCARKLWTQEGPAAFMKGAGCRALVIAPLFGIAQGVYFIGIGERILKCFE | Function: Responsible for the transport of glutamate from the cytosol into the mitochondrial matrix with the concomitant import of a proton (symport system).
Catalytic Activity: H(+)(in) + L-glutamate(in) = H(+)(out) + L-glutamate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34166
Sequence Le... |
E5RQA1 | MSMGPAAGEGCGLCGADGGGCCSRHRHDDDGFPFVFPPSACQGIGAPAPPVHEFQFFGNDGGGDDGESVAWLFDDYPPPSPVAAAAGMHHRQPPYDGVVAPPSLFRRNTGAGGLTFDVSLGERPDLDAGLGLGGGGGRHAEAAASATIMSYCGSTFTDAASSMPKEMVAAMADDGESLNPNTVVGAMVEREAKLMRYKEKRKKRCYEKQIRYASRKAYAEMRPRVRGRFAKEPDQEAVAPPSTYVDPSRLELGQWFR | Function: Probable transcription factor involved in the regulation of flowering time under long day (LD) conditions. Plays a major role as repressor of flowering. Controls flowering time by negatively regulating the expression of EHD1 and HD3A.
PTM: Phosphorylated at Ser-68 by HD16/EL1, a casein kinase 1.
Sequence Mass... |
Q9H3K2 | MLAARLVCLRTLPSRVFHPAFTKASPVVKNSITKNQWLLTPSREYATKTRIGIRRGRTGQELKEAALEPSMEKIFKIDQMGRWFVAGGAAVGLGALCYYGLGLSNEIGAIEKAVIWPQYVKDRIHSTYMYLAGSIGLTALSAIAISRTPVLMNFMMRGSWVTIGVTFAAMVGAGMLVRSIPYDQSPGPKHLAWLLHSGVMGAVVAPLTILGGPLLIRAAWYTAGIVGGLSTVAMCAPSEKFLNMGAPLGVGLGLVFVSSLGSMFLPPTTVAGATLYSVAMYGGLVLFSMFLLYDTQKVIKRAEVSPMYGVQKYDPINSML... | Function: Plays an important role in maintenance of mitochondrial morphology and in mediating either calcium or potassium/proton antiport . Mediates proton-dependent calcium efflux from mitochondrion . Functions also as an electroneutral mitochondrial proton/potassium exchanger . Required for the mitochondrial tubular ... |
Q6UDL0 | MVTPRSAVPAARPLAARRLASVAWACAALLALVALQCATATKDIVTMHATRNSLIPKDTLTVAVVMIDSYDNRLVFHANKNLLFGASNTSARALAEAYNLLGEVYVTYAYYRWARDDRPVAVGRPAPDYVLGTRLLSGPGSQKIKPPEERPSFPLSGSLRGKSLLMPRKVIFNDPLQTLMPFVFTRYLSITLSGYWDISVNSGKNVFSLCVSSPATPPVEVIATPRSAKLRESRFPQWPRYLYVSSSETSVLVNVAAGTSYKPRLYNATLAGVKAFLEVQNYGSHVAAGQLLTIKQLLKHGCNREPDEPFVVAAALHFGA... | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in th... |
P16492 | MTILQLFLVFLNILEALCDYQLPKPRINKPPAEERLKLRNGYNTTLIEFDDGVQSFNLNWTKIIEHIPHDELIELWREANVTEPLVNTLLKRSDTYRPETNVHIPGHGNSYACALPYWSYTIDQWEDNKTTGYLGNFGIPSKTVLNEFFYDFQYVYTNRQFYTEATYVLNCLIGATTPAYPTISCHITPNYLFVSVEFTKFDSLTLLFGHSHYLPPLKGHIVYNDIEGASNDVFSLVIFSTYDLFGKHVESFKFDIAKVFREIIETPPLTFIKNLQDEMFTIEIRDGCNINNIVNPKTFLFAFKAVVAHFLVIDSLRTQQ... | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in th... |
P27416 | MPASSVRLPLRLLTLAGLLALAGAAALARGAPQGGPPSPQGGPAPTAAPARGPTLFVLVGDGSAWFVFQLGGLGALNDTRIRGHLLGRYLVSYQVVPPPVSAWYFVQRPRERPRLSGPPSGAELVAFDAPGVRRTYTTAAVWPAEVAVLADAEARCPAAVFNVTLGEAFLGLRVALRSFLPLEVIISAERMRMIAPPALGSDLEPPGPPAGRFHVYTLGFLSDGAMHQTMRDVAAYVHESDDYLAQLSAAHAAALAAVVQPGPYYFYRAAVRLGVAAFVFSEAARRDRRASAPALLRVESDARLLSRLLMRAAGCPAGFA... | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in th... |
P09260 | MFALVLAVVILPLWTTANKSYVTPTPATRSIGHMSALLREYSDRNMSLKLEAFYPTGFDEELIKSLHWGNDRKHVFLVIVKVNPTTHEGDVGLVIFPKYLLSPYHFKAEHRAPFPAGRFGFLSHPVTPDVSFFDSSFAPYLTTQHLVAFTTFPPNPLVWHLERAETAATAERPFGVSLLPARPTVPKNTILEHKAHFATWDALARHTFFSAEAIITNSTLRIHVPLFGSVWPIRYWATGSVLLTSDSGRVEVNIGVGFMSSLISLSSGPPIELIVVPHTVKLNAVTSDTTWFQLNPPGPDPGPSYRVYLLGRGLDMNFSK... | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in th... |
P15518 | MSMFTSTRTLTQTMDKPDDLTRSATETAVKLSNMNQRVSRFHDKMENEIEVRRVDDDTRVKMIKDAIAHLDRLIQTESRKRQASFEDIREEVKKSADNMYLTIKEEIDTMAANFRKSLAEMGDTLNNVETNLQNQIAIHNDAIAALRKEALKSLNDLETGIATENAERKKMYDQLNEKVAEGFARISAAIEKETIARERAVSAATTEALTNTKLVEKCVNEQLENVASEIRAIQEEIDREKAERKEAEDKIVNTLEDVVSKIQGGLSMVTKHQ | Function: Giardins are involved in parasite attachment to the intestinal mucosa and in the cytoskeletal disassembly and reassembly that marks the transition from infectious trophozoite to transmissible cyst. They may interact with other cytoskeletal proteins such as microtubules in the microribbons or crossbridges, to ... |
P39572 | MLMHEKLMAGQFFDLKTDRKPLMHHHQYQHHQQQPLHHLPHSQLPVQGSLGLPKMDLYTAYAYQQQLLGAALSQQQQQQQQQQQHQQLQQQHTSSAEVLDLSRRCDSVETPRKTPSPYQTSYSYGSGSPSASPTSNLLYAAQMQQQQHQQQQQQQQQQQQLASLYPAFYYSNIKQEQATPTAAPPKVTPTANLLQTFAAASAAAAAAAAASSTNSPRPASNASTMQIDVLENPLSPAVEATTPTTSSSGEAGKNTRPFKAFPRDPLVIAANFAATDVLLDNPRVERYTEYRKRVLEQIRSSNGGSRTVTNPKMRRTNSRS... | Function: Represses the expression of both the krueppel and knirps segmentation gap genes. Binds, in vitro, to the krueppel regulatory elements CD1 and CD2. It is required in the early embryo for the development of portions of the head and abdomen.
PTM: Phosphorylated at multiple sites.
Sequence Mass (Da): 49169
Sequen... |
I1JNS6 | MPPPLPSLCNFNLAILFLFLTPTFQIPLIAPISKDDTTQLYTLSVFLKTPLQPTKLHLHLGSSLSWVLCDSTYTSSSSHHIPCNTPLCNSFPSNACSNNSSLCALFPENPVTRNTLLDTALIDSLALPTYDASSSLVLISDFIFSCATAHLLQGLAANALGLASLGRSNYSLPAQISTSLTSPRSFTLCLPASSANTGAAIFASTASSFLFSSKIDLTYTQLIVNPVADTVVTDNPQPSDEYFINLTSIKINGKPLYINSSILTVDQTGFGGTKISTAEPYTVLETSIYRLFVQRFVNESSAFNLTVTEAVEPFGVCYPA... | Function: Involved in plant defense against Phytophtora sojae . Contributes positively to soybean resistance against P.sojae . Binds the P.sojae xyloglucanase XEG1 and inhibits its cell wall degrading enzyme activity and its contribution as P.sojae virulence factor . XEG1 acts as an important virulence factor during P.... |
P0DO21 | MASSCCLHAILLCSLLFITSTTAQSETSFRPKGLILPITKDALTLQYLTQIQQRTPLVPVSLTLDLGGQFLWVDCDQGYVSSTYRPARCRSAQCSLAGAGSGCGQCFSPPKPGCNNNTCGLLPDNTITRTATSGELASDTVQVQSSNGKNPGRHVSDKDFLFVCGSTFLLEGLASGVKGMAGLGRTRISLPSQFSAEFSFPRKFAVCLSSSTNSKGVVLFGDGPYTFLPNREFANNDFSYTPLFINPVSTASAFSSREPSSEYFIGVKSIKINEKVVPINTTLLSIDNQGVGGTKISTVNPYTILETSIYNAVTNFFVKE... | Function: Involved in plant defense against Phytophtora parasitica . Contributes positively to Nicotiana resistance against P.parasitica . Binds the P.parasitica xyloglucanase XEG1 and inhibits its cell wall degrading enzyme activity and its contribution as P.parasitica virulence factor . XEG1 acts as an important viru... |
O14908 | MPLGLGRRKKAPPLVENEEAEPGRGGLGVGEPGPLGGGGSGGPQMGLPPPPPALRPRLVFHTQLAHGSPTGRIEGFTNVKELYGKIAEAFRLPTAEVMFCTLNTHKVDMDKLLGGQIGLEDFIFAHVKGQRKEVEVFKSEDALGLTITDNGAGYAFIKRIKEGSVIDHIHLISVGDMIEAINGQSLLGCRHYEVARLLKELPRGRTFTLKLTEPRKAFDMISQRSAGGRPGSGPQLGTGRGTLRLRSRGPATVEDLPSAFEEKAIEKVDDLLESYMGIRDTELAATMVELGKDKRNPDELAEALDERLGDFAFPDEFVFD... | Function: May be involved in G protein-linked signaling.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36049
Sequence Length: 333
Subcellular Location: Cytoplasm
|
P49672 | MATACVKSLESVQCGTCEKTIANGTEFYALLFDKHPDLRHYFKGNENLTGADVKKSDHFKKQGQRLLLACHVLAHLENDPASFKAYAREIVDPHLRMSVHLEPKLWSEFWPIWLDYLSTKESVDDATKNAWLALGKKFSDECLDHLKNLGQPH | Function: High oxygen affinity. Probably supplies oxygen needed for muscle activity.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 17454
Sequence Length: 153
Subcellular Location: Cytoplasm
|
P40420 | MDLLLALLPALFWGSIVLFNVKLGGGPYSQTLGTTIGALIVSIVIYFFVQPVLSLRIFIVGIVSGLFWSLGQANQLKSIQLMGVSKTMPISTGMQLVSTSLFGVIVFREWSTPIAITLGVLALIFIIVGIILTSLEDKNDKKEGEPSNLKKGILILLVSTLGYLVYVVVARLFNVSGWSALLPQAIGMVVGGLVLTYRHKPFNKYAIRNILPGLIWAGGNMFLFISQPRVGVATSFSLSQMGIVISTLGGIFILREKKTKRQLIAIAIGIILIIAAAVFLGIAKTNS | Function: Involved in the uptake of glucose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30892
Sequence Length: 287
Subcellular Location: Cell membrane
|
Q97UY9 | MDKKMRPVIKASLHYLALAIVSVIWLIPVYAMLINGFKSNFEVLSTPVLVPPTKITFEAYVSVLLSLAKPLINSLIIVIPTSFISAFLGAMGAYFFYTLSYSFSRASSAISDVLFSLISLATFIPQEATLLPLTRLIVSMGLLDSYIGIIFALLIFYIPTGALLMSMFISVIPRSLIEAAKMDGTGDLKIFMKIVFPLSMPGFISTLIFIIIQAWNNFFIPLVLVTTPGMKLTSIAVLSYSGAYGTLYNDTFAAGMVASIIPLAIFVFLGRYFIRGLMALGGGGKGV | Function: Part of the ABC transporter complex GlcSTUV involved in glucose uptake. Responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31182
Sequence Length: 287
Subcellular Location: Cell membrane
|
O07881 | MDLLIALLPALFWGSVVLINVLVGGGPYNQIRGTTFGALIIGIILLLTGNAKFDDLTIIIVGLISGAFWALGQGYQLKSVSLIGVSKTMPISTGLQLVGTTLFSAIFLGEWSTGVQVTLGLVAMVLLVIGIALTSIKGKNEASESSKNFGKAMPILLISTVGYVVYVVVAQIFGVDGMNALFFQSIGMAIGGLILSAKHETSVKSTLWNLIPGIVWGIGNLFMFYSQPKVGVATSFSFSQLLVIVSTLGGIFLLGEKKDKRQMIGIWAGIVLIVIAPLYSEILKHNYN | Function: Involved in the uptake of glucose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30585
Sequence Length: 288
Subcellular Location: Cell membrane
|
P36143 | MYKKLAIATLLYSADYLPGVFALGHQVNKLLEEAGKKGDIETCLIVTTSLFNGTLSELAKNILQSIYTKIVLVEPLNCQEESIQKNSENLALLERPELSFALIKARLWELTQFEQVLYLDSDTLPLNKEFLKLFDIMSKQTTSQVGAIADIGWPDMFNSGVMMLIPDADTASVLQNYIFENTSIDGSDQGILNQFFNQNCCTDELVKDSFSREWVQLSFTYNVTIPNLGYQSSPAMNYFKPSIKLIHFIGKHKPWSLWSQKNFIKNEYHDQWNEVYEEFKEEHQLNNEVSKPKISDSDKTETPETITPVDAPPSNEPTTN... | Function: Self-glucosylating initiator of glycogen synthesis. Catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues. These chains act as primers for the elongation reaction catalyzed by glycogen synthase. Capable of transferring... |
P47011 | MAKKVAICTLLYSRDYLPGALTLAYQLQKLLKHAVVEDEITLCLLIEKKLFGDEFKPQEIALIRSLFKEIIIIEPLKDQEKSIEKNKANLELLKRPELSHTLLKARLWELVQFDQVLFLDADTLPLNKEFFEILRLYPEQTRFQIAAVPDIGWPDMFNTGVLLLIPDLDMATSLQDFLIKTVSIDGADQGIFNQFFNPICNYSKEVLHKVSPLMEWIRLPFTYNVTMPNYGYQSSPAMNFFQQHIRLIHFIGTFKPWSRNTTDYDDHYYQLWRSTQRELYSECHLSNYFTHLQLGNIETETNFYHEPPCLQDLLNHGKRE... | Function: Self-glucosylating initiator of glycogen synthesis. Catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues. These chains act as primers for the elongation reaction catalyzed by glycogen synthase. Capable of transferring... |
P0A3F2 | MNVLSVSSEIYPLIKTGGLADVVGALPIALEAHGVRTRTLIPGYPAVKAAVTDPVKCFEFTDLLGEKADLLEVQHERLDLLILDAPAYYERSGGPYLGQTGKDYPDNWKRFAALSLAAARIGAGVLPGWRPDMVHAHDWQAAMTPVYMRYAETPEIPSLLTIHNIAFQGQFGANIFSKLALPAHAFGMEGIEYYNDVSFLKGGLQTATALSTVSPSYAEEILTAEFGMGLEGVIGSRAHVLHGIVNGIDADVWNPATDHLIHDNYSAANLKNRALNKKAVAEHFRIDDDGSPLFCVISRLTWQKGIDLMAEAVDEIVSLG... | 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): 51709
Sequence Length: 480
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
|
Q89RJ4 | MDDFVRVGGLGAVSAALPRALRPFADIRIMLPGYRDIIEQLTHIQIVGRCPSFADLPACSLGRAATKDGLPVYVLLCSQLYDRPGNPYGDESGRDWPDNDIRFARFASAAAELAMGKLDKNWAADLIHANDWQASLVPAYLAWRGAKLPSILTIHNLAYQGLFPKDSLRRIGAPESAFHIDGLEFYDQVSFLKAGLVYASHLTTVSGTYAREITTAEFGCGLEGLLRLRSDAAELTGILNGIDESWDPRSCAQLAQQFGAGDWVGKKANADYVRKQFGLAVSRGPMFGIVARLVHQKGIDLVLSAADEIIDAGGQIVVTG... | 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): 50145
Sequence Length: 462
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
|
Q74ED9 | MTRLNILMAASECVPFAKEGGLADVVGVLPKYLAHMGHDVRVVMPLYSRIDPERFGLERLPGVLVVPMGIMGNQYCGVWEGRLPGSAVPVYFLEHEGYYGREGLYEEDNVGYMDNDNRFIFLSRAAMELPKLIGFAPDVFHAHDWHTAAVPVFLNTLYRDDPLVGGAASVLTVHNMQHQGNFYPGAMEVLGIGWEHFTFLGLEKDNQTNLLKGGLYHATVLNTVSEGYAREMQTPEYGWGLDGVVRARSADLVGILNGVDYEEWNPETDPHIVANYSRSDLSGKKLCKRDVQRFFGLPERDDVPLFGLVGRLVKQKGIDI... | 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): 56222
Sequence Length: 501
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
|
Q3JEW3 | MYIVMITPECAPIAKVGGLGDVVQGLSNELSIRGNTVELILPKYDCMRYERIWGLEKTHNNLWVPYHDQWIPCDVYFGFAEGLKCFFIEPHNGFFQRGTYYGQPDDPQRFAFFCKAALEFMLRSNKYPEIIHCHDWQTGLVPVLLFEQYKYLGMTHPRVCYTLHNMRHQGVTGGHILQQVGLDPAAYMTPERLLDHTYPHGVNLMKGGIVFSNFITTVSPRYLDEIRYTDQGYGLQHTLHEHSQKLGGILNGVDYKVWNPDIDPYIAARYNLKTLDKKYENKTALRHRLWLRDEYKPIVGVISRLDPQKGVELIRHALFY... | 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): 56489
Sequence Length: 487
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
|
P58393 | MNILSVASEVYPLVKTGGLADVVGALPSALLPHGVRTRTLVPGYPSVLKKLKKKKPVGRFDNLFGHPATVLAAEVNGVDLLVLDQPALYARDGGPYLDSTGRDYPDNFRRFAALSLAAAEIAGNGIIPNWKPDIVHVHDWQTALTPVYMRFGPAPDLPTVMTIHNIAFQGQFGASVFPELALPPDAFSTQFVEYYGDVGFLKGGLQTASAITTVSPSYAQEILTPEFGMGLDGLLSSRVADLTGIVNGIDGETWDPQTDPHIPAHYGPGTLKRRAGNRKALEERFGLEKGPGPIFCVISRLTWQKGMDLVAEAADDIVAL... | 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): 51408
Sequence Length: 480
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
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Q8UK38 | MRILAVTAEMFPFVKTGGLADATSALPQALERKGADVRTLLPLYRGLTPLVRGRKPVLVANILEQPVSVYYVVSDGHKLLLLEAASLFDRDGHPYGVKGEPFADNDLRFAVLSKVAAEIALGAIDGWQPDVVHVHDWHAALTCVYLADSTPSVASVLTLHNLAFQGQYPLERAGMLGLPSHLCTVDCLEYYDDMSFLKGGLTTASAVTTVSPTYAREILTPEMGMGMHGVLARRRGDLRGIVNGVDHDVWNPATDPYILANFTAATATRRSLNKYALLQALGLAPTQGPVFGVVSRLTWQKGIDLLPHVVPLIIERKGRL... | 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): 55309
Sequence Length: 509
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
|
Q89G86 | MTPARVLAVASEVYPIVKTGGLADVAGALPIALKAHGVEMRTLMPGYPDVMRLLSGAEEIRRWPDYFGGPGRLLAGAHDGLDLFVLDVPHLYARPGNPYVTTEGVDWPDNGVRFAALSRVAADIGHGLVPAFVPDIVHAHDWQAGLAPAYLHYDNRPRPGTVMTIHNMAYQGKFAPELIGAIGLPWSSFDVNGLEYFGGISFLKAGLQFADRITTVSPTYAREIQSDEGGMGLGGLLRARAGALSGILNGIDIAVWNPQTDSHIAYRFGAEDLTFRAANKAVLQQQFNLDSSDEAPLLGVISRLSWQKGLDLLLEAIPTI... | 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): 51786
Sequence Length: 482
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
|
Q747K8 | MKVLMVASEVAPFARTGGLAEVTAALPAALRRMGHDVRVIMPFYRCAAQTELGVRKARKSAEVSLNGETHKGFLRQAALGDVPVYLVENREFFSRDYLYGTPEGDYPDNPRRFAFFCRSVLQFLKRMDFRPDVIHCHDWQTALIPIILRLEAADDPFFARTATVFTIHNLAYQGLFPAPAIAETGLPSALFTTEWLEYYGQLNLMKGAILTADLITTVSETYRREIMTPTQGCGLEGVLARRGDDLFGIVNGIDTDEWNPAADKRIFRNYSARALAGKAADKLELQRELGMPAAPSVPLIGMVSRLAEQKGIDLVLELLP... | 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): 54142
Sequence Length: 484
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
|
B2KE25 | MNIVLAASEAFPFCKTGGLADVTGSLAKELSKHKGNRVILFLPHYRNINRVASLKVVPGTFLIPIGDRLETASLSYISWGNVLVFFINNTKYFDRPELYRTAAGDYFDNDERFIFFNRAVLESCKFIGYRPDIIHAHDWQAGLLPAYLKTVYKTDAFFTRTRSLFTIHNMAYQGQYPYSTFIKTGFHTVDYVPERFEYYGGISYLKSGIVYADYVNTVSPNYAKEITLDEKMGFGMEGLLRSRQDTFCGILNGLDTGVWDPEHDPLIPYSYESFSPVKGKAACKQFLQNMLGLEVSPSKPLVGIVSRMDYQKGLDLIPGV... | 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): 54518
Sequence Length: 482
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
|
B1YK70 | MKVWFAATEATPFIKTGGLADVVGSLPLALAEEGAEVSVILPNYGQIKEQYKLEMEFLFDFIVPVGWRQQFGAVLRLKQDGVTFYFIDNEYYFKRDGVIYGHYDDAERFAYFSRAVLEMIQRVDAEEVPDVIHCHDWQTGVLPAFLRIHYQHLNRYQEIKTVFTIHNLQYQGVFPEEVLGDLLGLSHEHFTAEGIAHNGLVNYMKAGLVHANQITTVSPSYRDEIMDPYYGETLEPVLQHRAVDVRGILNGIDYRQFSPETDEHLVENYDVKTVEEGKAANKAALQQELGLPVNPDVPLFGFVSRLVDQKGIDLLAHILP... | 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): 54769
Sequence Length: 483
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
|
B0S264 | MKILYCAAEADPFIKTGGLADVAGTLPLEMKKQGHDVKVVIPLYKLIDEEYKKKFEFEGSFYVDLDFKHHYVGVFKYIHRGVEFYFLDNEDYFNRDNVYGEYDDCERFVFFSKACVQLLRYIDFDCDIIHSNDWHTAMVNVYARDFAKGDPFYESIKTVFTIHNLKYQGVFSSNSLRQTDLSPMYFTEDALKFYDAINFMKGAIVFSDRVTTVSKTYADEIKYSFFGEGLDGVIRQYHYKISGITNGIDTTIWNPETDKYLFKNYSLKNIKDKDENKKALQRMYGLEEKNVPVFAMVTRLVENKGLELVRYIMDEFLTTE... | 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): 55635
Sequence Length: 474
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
|
A5FG96 | MEIFHISAECYPMAKVGGLADVVGALPKYQKNAGNDVRVVVPAYDTKFKKENNFECVHWGTVKLGNFNFPFSVLKESSDKLGYELYLIEIKELFNRPNVYGYEDDIERFLSFQIAVLDWIIARNKVPDIINCHDHHTGLIPFLLQFAYKYENLKDVKTVITIHNGLYQGWFGFDKLYYLPEFDLKHIGFLEWNNCINSLAVGVKCANAVTTVSPSYLNEINYSANGLESLFNSVRNKSKGILNGIDIEIWNPLKDQMIAANYSIENFEIGKQKNKEKLCEQFELDPSKPLFSFIGRLFEEKGGDLLPQASALALSEHFEE... | 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): 53910
Sequence Length: 473
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
|
Q41058 | MVYTISGIRFPVLPSLHKSTLRCDRRASSHSFFLKNNSSSFSRTSLYAKFSRDSETKSSTIAESDKVLIPEDQDNSVSLADQLENPDITSEDAQNLEDLTMKDGNKYNIDESTSSYREVGDEKGSVTSSSLVDVNTDTQAKKTSVHSDKKVKVDKPKIIPPPGTGQKIYEIDPLLQAHRQHLDFRYGQYKRIREEIDKYEGGLDAFSRGYEKFGFTRSATGITYREWAPGAKSAALVGDFNNWNPNADVMTKDAFGVWEIFLPNNADGSPPIPHGSRVKIHMDTPSGIKDSIPAWIKFSVQAPGEIPYNGIYYDPPEEEK... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch 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. May preferentially transfer short chains during branching. Responsible f... |
Q59833 | MTPRPSSSGPDPRKTTGKKPAGKTPTGKKPAKAAKKKAPRRTTASANASATTSVSGAEVAVSPAPDAADRERLLAGTHHDPHAVLGAHRVPGGVAFRVFRPYALAVTVLSGELRVGLHDDGDGFFSGLVPLKDVPAHRLLVAYEGTEQEVEDPYRFLPTLGELDLHLLGEGRHEQLWRALGAHPTTHEGVAGTRFAVWAPNARGVRVAGGFNFWDGTGHPMRSLGSTGVWELFLPGVGAGELYKFEITRPDGSRTFRADPLARRTEVPPATSSVVHASDYTWGDEEWLAHRADAPAHEAPMSVYEVHLPSWRPGLTYRQL... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q59832 | MALRDTSIPEPSGPVPPAPGACATAPPLDPTDRGRLLAGAHHDPHSLLGAHPVPGGIAFRVLRPFAREVGVVVDGERHTLASEEDGLFSGVLPLAGIPSYTLVVAYEQGETQETHDPYRFLPALGELDLHLIGEGRHEQLWQALGAEPMTHEGVTGTRFTVWAPNAQGVRVATDFTHWDGTAFPMRSLGSSGVWELFLPGVGEGTRYKFEIHSRYGHRFLKADPMARAAEEPPNTASVVTASRYEWGDAQWMRTRADTPVHEAPFSVYEVHLPSWRPGLTYRELAEELPAYVKDLGFTHVELMPVAEHPYGPSWGYQVTG... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
P16954 | MTGTTPLPSSSLSVEQVNRIASNQEQNPFDILGPHPYEHEGQAGWVIRAYLPEAQEAAVICPALRREFAMHPVHHPHFFETWVPEETLEIYQLRITEGERERIIYDPYAFRSPLLTDYDIHLFAEGNHHRIYEKLGAHPCELENVAGVNFAVWAPSARNVSILGDFNSWDGRKHQMARRSNGIWELFIPELTVGAAYKYEIKNYDGHIYEKSDPYGFQQEVRPKTASIVADLDRYTWGDADWLERRRHQEPLRQPISVYEVHLGSWMHASSDAIATDAQGKPLPPVPVADLKPGARFLTYRELADRLIPYVLDLGYSHIE... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q2JT08 | MGFLLSAEQVLQFVTNQWQDPYAVLGPQQIEQGETSFWLVRALVPNAKQVWLVERATGQAYPMQPLHPETLFELCFAPGTPVPDYFLRAQRVWDPEGQHLEEWEDPYRFPLEKVNHIGELDRYLFNEGNHHRIYEKLGAHPISVDGVQGVHFAVWAPNARNVSVIGDFNHWDGRQHQMKRLGESGIWAVFIPGVGPGAVYKYEVKTAWGDIYEKSDPYGFQQEVRPKTGSIVADLHTYTWHDQEWLEKRAATDPLRSPISVYEVHLGSWMHASTEDPPADGHLVPVEQKPNTRFLTYRELADKLIPYVKELGFTHIELLP... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q3SH78 | MRKLVEATQAGSEASVALAPSAPIQRLQAGLHHDPFEVLGVHVQPDGSKLVRAFLPAAEAVEVAGVRMTRVPGTDCFERLLPPGTALEAHPLLTWQDKRSGAWQRLRSPYSFAPQLGEMDLYLFGEGRHFEIWKVLGARVKTVDGVTGCLFAVWAPAVLRVSVVGDFNDWDGRRHPMRCRGVSGVWELFIPGLEAGHAYKYEILGRHGERVTKTDPYARQMFLRPETTSRVPDERPYAWGDAEWLAARTRFDWQHRPMSVYEVHPGSWRRRADGSFYSWRELTAELIPYVRDLGYTHIELLPVAEHPFDASWGYQVSGYY... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q9KNE8 | MKITKKPSKVQQFYDQLARAAFADPFSFLGPYIPAEQGALRVWMPGADNVALVVEGQARVALEREGEGGFVLKDGRNLRFTHYQLAVDWAGTEQLLDDPYQYHGLYAEYEDLHTPKQMYHHMGAQFVTLERDGKMVSGVRFLVYAPHAAACSLIGAFNHWDGRRHPMQRLDYGIWGIFIPGLPEGTQYKFELKGPHGEGLPHKADPWGFYAEQYPSFASVTYDHRRYQWQDTAWQQRPVTEKRKQALSFYELHVGSWKRGENGEFLNYRELADQLVPYLVEMGYTHVELMPVAEHPFYGSWGYQPVGLFAPTSRYGSPDD... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q0BPL4 | MSGTSSIARSTMAYVLAGGRGSRLLELTDTRAKPAVYFGGKSRIIDFALSNAVNSGIRRIGVATQYKAHSLIRHMQRGWNFFRPERNEGFDILPASQRVSETQWYEGTADAVYQNLDIIAGYEPEYMIILAGDHIYKMDYEIMLHQHVERQADVTVGCIEVPREEATGFGVMQVDDTGRITAFLEKPSDPPGMPGQPDIALASMGIYVFKTKFLFDVLRRDAADPDSKHDFGGDIIPDLVENGTAIAHRFSDSCVRSSKTAEAYWRDVGTLDSYWQANLDLTNVVPTLDLYDSGWPIWTYNEISPPAKFVYDDVGRRGMA... | Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glu... |
P43796 | MEILMKSGDLNKYDLVKNALVLVLAGGRGSRLHELTDKRAKPALYFGGNRRIIDFALSNCINSDLNRIGVVTQYAAHSLLLHLQTGWSFLPQERGEFVDMLPARQQIDDSTWYRGTADAVYQNMAIIKNHYRPKYILILAGDHIYKQDYSVMLMDHVNSGAKCTVGCIEVPRSEAHEFGVMAVNENLKVKAFVEKPKDPPAMVGKPDVSLASMGIYVFDADYLYKMLEQEVNTPQTSHDFGKDVLPKCLEEGALYAHPFSRSCMGRNTEGEIYWRDVGTLDSFWQSNIDLVSENPQLDIYDQSWPIRGNPIQAYPSKFFY... | Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glu... |
Q31IB9 | MKYYCETKSATDLTRKTLALVLAGGEGSRLKDLTKWRAKPAVPFGGKYRIIDFVLSNCVNSGIRKIGVLTQYKSHSLIRHVQRAWSFMRYEVGEFVELLPAQQRVDKGWYKGTADALYQNLDIMRRHTPDYVLVLGGDHIYSMDYSKMLYEHAESGADVTIGCIEVPRMEATGFGVMSVDECFKITKFTEKPANPDAMPHKPDKALASMGIYVFSTEFLFQKLIEDADNPNSSRDFGKDIIPSIIEDWQVRAFPFEDETGLPVYWRDVGTIESYWKASLDLCSITPDLNLYDEDWPIWTYQAQMPPAKFIFDDEGRRGEA... | Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glu... |
Q1ISX7 | MIETLGVLLAGGAGERLYPLTRDRAKPAVNFGGIYRIIDITLSNCINSGLRRVYILTQYKALSLNRHIREGWSGIVGNELGEFIEILPPMKRVSENWYMGTADAVYQNIYSIGSEQPRYVLILSGDHIYKMNYDLMMRQHKDSGADVTLATILIDPSETRHFGVVDVDNQSHVNGFVEKPKSTELRSPYDPSKVSASMGIYIFNTDVLIPVLLKDAEDPNSKHDFGHNILPKMVGEYKIYSFNFIDENKKEALYWRDVGTLDAYYDANLDLVSVAPVFNLYDKAWPIRTHQRQYPPAKFVFAEQGRMGTALDSVVSMGCI... | Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glu... |
B3E8Z1 | MFDGSNLGRNTIAMVLAGGKGERLMPLTLRRAKPSVTFGGKYKIIDFVLSNLFNSGIRRMYILTQYRAYSLNKHIRESWGKWTGLGEFCVAISPETSSDSEQWFKGTADAILQYLRFVETADADYVAVFGGDHIYKMDVTQMIQFHRMNRADLTIASLEVPKEEASRFGVFSVDDDNRVTAFTEKPKDPETIPGRETCFASMGNYIFPTRKLIEVLLEGKKHYEDLDFGKHVIPMMLEKGDRIYAYNFNDNLVPGMKSEERGYWKDVGTLDSYYEANMDLIHVSPQLNLYNYKWPILTNQGNLPPAKTVFDEEGRRGVNI... | Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glu... |
Q9L1K2 | MPATHHSSATSAERPTVVGRIPVLDVRPVVQRGRRPAKAVTGESFEVSATVFREGHDAVGANVVLRDPRGRPGPWTPMRELAPGTDRWGATVTAGETGTWSYTVEAWGDPVTTWRHHARIKIPAGLDTDLVLEEGARLYERAAADVPGREDRRELLAAVDALRDESRPAASRLAAALTPQVDAVLARHPLRDLVTSSDPLPLLVERERALYGAWYEFFPRSEGTPHTPHGTFRTAARRLPAIAAMGFDVVYLPPIHPIGTTHRKGRNNTLSATGDDVGVPWAIGSPEGGHDSIHPALGTLDDFDHFVTEAGKLGLEIALD... | Function: Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE-catalyzed polymerization with M1P. Is sp... |
D7BMJ2 | MSTLQHKTSSARRSSRRSVAAPDFVAVSRIPIVEVSPQLLDGTAPVKSTVDESFPVQATIFREGHDKFAARAVLVDGAGHTVDSVPMCDVSPGLFRFEGWLTPRVPGPHRFFVEAWSDPYATWLHNAEIKVPAGIDVGLVFAEAEVLFKAALKGTPVRSGERAAIRDALTVISKRRALPEVKLAAARSEEVRAAFAAYPVKELVSRSREYPVFVDRVRALVGSWYELFPRSVGATRDSESGEWTSGTLRTAATDLDRVAGMGFDVVYIPPVHPIGLTNRKGRNNSLTAVPGDPGSPYAIGSDAAGGHDAIEPSLGTFEDF... | Function: Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + alpha-maltose 1-phosp... |
Q56198 | MNKIILAADIGGTTCKLGIFDENLNRLSKWSIDTDTSDTTGYLLLKNIYDSFIQHIDKSDNTFSDVLGIGIGVPGPVNFETGEVNGAVNLYWKGTVNVRDIFKQFVDCPVYVDNDANVAALGEKHKGAGNGADDVVAITLGTGLGGGIISNGEIVHGHNGSGAEIGHFRVDHDQRFKCNCGKSGCIETVASATGVVNLVNFYYPKLTFKSSILQLIKDNKVSAKAVFDAAKAGDQFCIFITERVANYIAYLCSIVSVTSNPKYIVLGGGMSTAGLILIENIKTEYHNLTFTPAQQNTEIVQAQLGNDAGITGAAGLIYTY... | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 35033
Sequence Length: 328
Subcellular Location: Cytoplasm
EC: 2.7.1.2
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P0A4E1 | MGLTIGVDIGGTKIAAGVVDEEGNILSTHKVPTPTTPEAIVDAIASAVEGARVGHEIVAVGIGAAGYVNRQRSTVYFAPNIDWRQEPLKEKVEARVGLPVVVENDANAAAWGEYKFGGGKGHRNVICITLGTGLGGGIIIGNKLRRGHFGVAAEFGHIRMVPDGLLCGCGSQGCWEQYASGRALVRYAKQRANATPERAEVLLALGDGTPDGIEGKHISVAARQGCPVAVDSYRELARWAGAGLADLASLFDPSAFIVGGGLSDEGDLVLDPIRKSYKRWLVGGNWRPVADVIAAQLGNKAGLVGAADLAREPDPIM | Function: A probable glucose kinase (Probable). Required for glucose repression of many different genes, restores glucose kinase activity in E.coli glk mutants .
Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 33062
Sequence Length: 317
Subcellular Location: Cytoplasm
EC: 2.... |
B4SRZ6 | MSASSQPVLVADIGGTNARFALADTSLDAPLQQDSIREYAVAEFPSLGDAARHHLEQIGATASRGVFAVAGRVDGDEARITNHPWVISRSRTAAMLGFDELHLINDFAAQAMAISLLQSDDVVQVGGAAWVPGKPGQPRNYAVIGPGTGLGVGGLILRHGRCYPLETEGGHVSFPPGTPEEIRILEILSEQFGRVSNERLICGPGLVNIHRAVCEMAGIDPGQLQPVDVTARALHGDPQAMRTVDVFCAVFGAIAGDLVLTQGAWDGVFLTGGLTPKMLDSLQHSGFRQRFEHKGRFSSIMARVPSLAVMHPHAGLLGAA... | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 35246
Sequence Length: 335
Subcellular Location: Cytoplasm
EC: 2.7.1.2
|
Q55855 | MGAMGVNFLAGDIGGTKTILALVTINESSPGLARPVTLFEQTYSSPAFPDLVPMVQQFRQEAAFVLGNPISVAKACFAIAGPVIDNTCRLTNLDWHLSGDRLAQELAIAQVDLINDFAAVGYGILGLGSEDLTVLQAAPVDPSGAIAILGAGTGLGQCYVIPQGQGRYRVFASEGAHGDFAPRSPLEWQLLEYLKKKYSLGRISIERVVSGMGIAMIYEFLRHQYPERESAQFSKLYQTWNREKDQETKTVDLAAAVSQAALEGTDVLADQAMELFLGAYGAEAGNLALKLLPRGGLYVAGGIAPKIIPLLEKGSFMQGF... | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 37712
Sequence Length: 355
Subcellular Location: Cytoplasm
EC: 2.7.1.2
|
Q9X1I0 | MPKLKLIGVDLGGTTFSVGLVSEDGKILKKVTRDTLVENGKEDVIRRIAETILEVSDGEEAPYVGIGSPGSIDRENGIVRFSPNFPDWHNVPLTDELAKRTGKKVFLENDANAFVLGEKWFGAGRGHDHIVALTLGTGIGGGVVTHGYLLTGRDGIGAELGHVVVEPNGPMCNCGTRGCLEAVASATAIRRFLREGYKKYHSSLVYKLAGSPEKADAKHLFDAARQGDRFALMIRDRVVDALARAVAGYIHIFNPEIVIIGGGISRAGEILFGPLREKVVDYIMPSFVGTYEVVASPLVEDAGILGAASIIKERIGG | Cofactor: Mg(2+) is the most effective ion. It can be efficiently replaced with Mn(2+) or Co(2+) and to some extent with Ni(2+).
Function: Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ATP as the phosphate donor. Can also phosphorylate 2-deoxyglucose, with lower efficiency. ITP can also serv... |
O34824 | MGKYFGTDGVRGVANSELTPELAFKVGRFGGYVLTKDKQRPKVLIGRDTRISGHMLEGALVAGLLSIGAEVMRLGVISTPGVSYLTKAMDAEAGVMISASHNPVQDNGIKFFGGDGFKLSDEQEAEIERLMDEPEDKLPRPVGADLGLVNDYFEGGQKYLQFLKQTADEDFTGIHVALDCANGATSSLATHLFADLDADVSTMGTSPNGLNINDGVGSTHPEALSAFVKEKNADLGLAFDGDGDRLIAVDEKGNIVDGDQIMYICSKHLKSEGRLKDDTVVSTVMSNLGFYKALEKEGIKSVQTAVGDRYVVEAMKKDGY... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable).
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamin... |
C4Z1Z8 | MGKYFGTDGFRGEANVTLTVDHAFKVGRFLGWYYGKNHEDGKAKIVIGKDTRRSSYMFEYSLVAGLTASGANAYLLHVTTTPSVSYVARTEDFDCGIMISASHNPFYDNGIKLINAAGEKMKEDVIAEIEKYLDGELGEIPYATRENIGCTVDYTAGRNRYMGYLMSLAIYSFKGIRVGLDASNGSAWTLAKAVFDALGAKTYVINAAPDGTNINANCGSTHIEGLQDLVRREHLDVGFAFDGDADRCLCVDEKGEVITGDHILYIYGCYMKDRDKLVGNKVVTTVMSNFGLYKAFDAVGIEYEKTKVGDKYVYECMSEN... | 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): 49226
Sequence Length: 450
EC: 5.4.2.10
|
Q74K59 | MLKYFGTDGVRGVANAGLTPEMAFKLGRDGGYVLTKDKKDGERAKVLVSRDTRISGQMLEYALISGLLSVGIEVLEVGVITTPGLSYLVRAQGADAGVQISASHNPVEDNGIKFFGSDGLKLSDAKEEEIEKLIDAPEDKLPRPSAEGLGTVTNYHEGASKYLQFIENTLPEELSGIKVVVDGANGAASALISRLFADMGVDFTTIATHPDGLNINDHVGATHTKKLQEEVVKQGAQLGLAFDGDADRCIAVDENGNEVDGDHIMYVIGSYLADHGRLKKDTIVTTVMSNLGFTKALERRGLKNIRTQVGDRYVSEEMRA... | 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): 49164
Sequence Length: 451
EC: 5.4.2.10
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Q88YE8 | MKYFGTDGVRGIANSGLTPEMAFRLGRAGGYVLTEHAENKSTQPRVLVARDTRISGQMLEEALIAGLLSAGIEVLRLGVITTPGVAYLVRIQDADAGVMISASHNPVEDNGIKFFGGDGFKLSDAKEEEIEELLDQPKDTLPRPAAEGLGTVADFPEGNLKYSQFLEQTIPDDLSGIHLAVDGANGSTSNLVSRIFADLNVEFDTMATAPDGLNINKGVGSTHPEALSKFVVEKGAQVGLAFDGDGDRCIAVDELGNIIDGDKIMYICGKFLSERGKLKQDTVVTTVMSNLGLYKALEAAGLHSKQTQVGDRYVVEEMLK... | 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): 48376
Sequence Length: 451
EC: 5.4.2.10
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Q53876 | MGRLFGTDGVRGVANADLTAELALGLSVAAAHVLAEAGTFAGHRATAVVGRDPRASGEFLEAAVVAGLASAGVDVLRVGVLPTPAVAHLTGALGADLGVMLSASHNAMPDNGIKFFARGGHKLADELEDRIESVYADHRTGAPWDRPTGSGVGRVRDYDEGLDQYVAHLVGVLPNRLDGLKIVLDEAHGAASRVSPEAFARAGAELVTIGAVPDGLNINDGCGSTHLDLLKAAVVEHGADLGIAHDGDADRCLAVDHTGAEVDGDQILAVLALAMREREALRSDTVVATVMSNLGFKLAMEREGIRFVQTGVGDRYVLEE... | 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): 46896
Sequence Length: 452
EC: 5.4.2.10
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Q9HT00 | MCGITGYIGTDPTGRIVHEGLQNLEYRGYDSAGIALAGGGSLSVHKTGGEVGDLPVPSREDGTRGIGHTRWSTHGEPTRENAHPHTDCTGDVAVVHNGIIENYAALADELRADHVFHSDTDTEVVPHLIETHLADGVSLLTAVQRTTERLTGSYALAITAAGHDGIVVARSDSPLLLGHGDTGTFVASDATAFIEHTNRVTYLRNGDIAHLTETEWTVYNDGARVSRDIEALDWSADAAGKSGYDHYMLKEIHEQPRALRQAISGRISDLGTDVTLDMELSTETLQNVAELQIVACGTSYHAGLYAKELLETHADLPVTV... | 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): 63631
Sequence Length: 601
Subcellular Location: Cytoplasm
... |
O26060 | MCGIVGYIGDSEKKSVLLEGLKELEYRGYDSAGLAVLSNDRLEVFKTQGKLENLKLELKNKEFLDFGVSIAHTRWATHGKPSSANAHPHFTENLALVHNGIIENYASLKKELENKGHAFLSQTDTEVIAHLLEETLKSESDLLKAFEKSISLLKGSYAILMLHKRAKESLFYAKSSSPLVVGKGKEGVFFASSLSVLAPKVDQFVILEENSVGRISLENFKDLNNIENMKDYAFEDKDYSKGNFRNYLEKEIYEQHSSLLECLEGRLEALSVYCEIDPEFLKNVSEITLCSCGSSYHASLASVYLFERLAKIRARAILAS... | 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): 67071
Sequence Length: 597
Subcellular Location: Cytoplasm
... |
Q72V57 | MCGIVGYAGKKNAESVLVVGLICLEYRGYDSAGIAVLDQGDILVRKSKGKIKDLEAYLREFPAPGNVGIGHTRWATHGEPNQINAHPHTDTNSTVAVVHNGIIENYLELKSQLKKKGHVFQSLTDTEVLPHLLEESKKNGKSNKDSFLELFGKIHGKWAISSVFETEPDRVYFAQDGAPLLIGKGKGEYFLASDISPLTRNCEEVYYVNSGEWGYFSQNEFKLFDFSGKELNPTFKKQELRWEDLDKGGYPHYMIKEIHEQAGIFRKIIQERILENSEIVFPEIKLSKDVLSRVNRIIIQAAGTSYYAGMIGKHYLENFA... | 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): 67943
Sequence Length: 610
Subcellular Location: Cytoplasm
... |
Q8TLL3 | MCGIVGYAGRNAAAPVIIESLKKLEYRGYDSAGITVLSKGIETYKAVGKIVNLEVEIPKNLGGTVGIGHTRWATHGRPSTKNAHPHNSGGNPGKISLVHNGIIENYMALKEQLTGEGYVFNSETDTEVIAHLVHKHIYGKPDGKEAKCELLVGLREALKEIEGSYALAILSADEPGKLVLARKDSPLVIGLGKGENFAASDVTAFLNHTRDVVFVNDFETAVLSPTSVEIFDREGKPREKKIEKIEWDFEAAEKAGYEHFMLKEIHEQVTAIHNTLAGKVSELEGDIYLKELNLSEDEIRKLARVQILACGTSWHAGLLG... | 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): 67753
Sequence Length: 618
Subcellular Location: Cytoplasm
... |
Q8TZ14 | MCGIVGYTGERDAAPIIVDSLVRLEYRGYDSAGVATIHEGRLYLEKDAGKLTEGGEPTKLQRSLRKLPGKIGIGHTRWATHGDPNRRNAHPHTDCRDEIAVVHNGIIENFMQLREELEDKGHRFDSETDTEVVPHLIEQGMKEGKSFFEAFVEAVRRLEGSYAIAAICTREPDVILAARKESPLVVGLGDDGNFLASDIPAILPETNRVIPIDDGEIVVVKRDEVRILDAETLEDVTEEKEVQIVEEDPHTLERRGYPHFMLKEIHEQPEAVRNTLRIERENLMEMAEELVGGDYTKLYIVACGTSYHAGLGAKYATELL... | 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): 68112
Sequence Length: 614
Subcellular Location: Cytoplasm
... |
Q6LWM9 | MCGIIGYIGNEKASKILLKGLKRLEYRGYDSCGIATIDDTIKLKKNTGKVLEVSKKENFEDMTGFIGIGHSRWATHGGITKNNAHPHYDCSEKICIAHNGIISNYKELKELLISKGHIFKSETDTEVIPHLIEEEIKDFKEITEKTYINAIQNTIKKLNGTYALLILNQDFPEMLVGVRNESPLILGIKKDECFIGSDISAFLEYTKLAMPLNDRDIVILRKENDEIDIEVLNYGKQVQRDTIELQWDMESAEKEGYEHFMLKEIMEEPVILKNSMKISKLEIENLGKEIEKCDKIYITAMGTSLHAAMVAEYWFSGLNK... | 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): 67138
Sequence Length: 599
Subcellular Location: Cytoplasm
... |
Q6MHV9 | MTVIALAAGKGTRMKSPLPKVLHPVAGRPMIEKVIQASKQAGAAEVRVIVGHGQNLVRQVVEPMGVACYVQDEQLGTAHAVRCAKPETIEGVVVIMNGDHPLIEASDIKDFVRIFRDEKCDLAVVTAVLKNPGEFGRIVRHKGDLAAIVEAKDASAEALKIREINTGIYIVKASVLSEYLPQISNNNAKKEYYITDLIALCIQDKCRVQAIQSTPKVAVGVNNQLELARATRLLFKRKALRLMEDGVLMIDPRTVYVEESVEIGAGTVIYPNVFIRGRTKIGSFTVIESNAFISDCEIGDSVQIRGGSYLESSKLHNKVS... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q8G5P1 | MALSAAIVLAAGEGTRMRSNKPKVLHAFAGKTFLNRVMDSVAALNPDTLAVVVHFQAERVAEAARSYDEQVTIVNQDDIPGTGRAVQCAMAQLTEAGKVDGPVLIAASDMPLLDSETLHRLVEFHTASGNGATVLTTILDDPTGYGRIIRDREGNVLRIVEQKDANRSELAVQEVNTSVYVFEASVLTEAIAGLKSNNAQGEFYLTDALETAKAAGKVGAFAAPDPLTVEGVNDRVQLAALSKTYNRRVCERWMRDGVTILDPETTWIEDDVQIGRDATILPGSFLQGHTVVGEDAIVGPYTTLIDATVDEGAVVERSRV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q494C1 | MSYINFSAIILAAGRGNRMLSDTPKVLYQIGGKFMLQHLIDSVMQVGVSSIYVVHGYKGEMIIKEINTNQYKIPVYWILQHDLTGTGDAVQRVLPFISDDEEVLVLYGDVPFVSYKTLQRLHVIKSQCDISMLTATLPNPKGYGRIVRNQEGSVVSIIEHDDIINDDQKKIKEVSTGIFIAISNHLKCWLSTLTTHKSKNEFYLTDIIQIAHQSGYSIHTMCPDDTFEIMGVNSKSDFVDLDKQYQQRKVQCLLSSGLMIIDPNRFDLRGTLVHGKDVYIDINVIIEGHVSLGNRVKIGASCILKDTIVADDVEIYPFSI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q7VT27 | MLNVVILAAGLGKRMQSDLPKVLHTLAGRPMLDHVIGSARQLQPARIIVVVGHGADRVKAAFEGQPGLQFALQQPQHGTGHAVQQAVPQLLEGDGEDDVTLVLYGDVPLVQPATLQNLLQARGRGVAVLTEVLADSTGYGRIVRDAQGQVCRIVEHKDASEAERAIKEVNTGILAAPTARLKDWLGRITNDNAQGEYYLTDVIGLAVGDGVPVGAAQPGASWETLGVNSRVQQAQLERAWQSELARRQLEAGVTLADPARFDVRGTLSCGRDVFIDVGCVFEGTVTLGDGVRVGPHCVLRDVAVQAGARIEAYSHLQQAK... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
A4YUF4 | MTARSSLTIVLAAGEGTRMRSSLPKVLHPIAGESMLAHVLAAAPQGDGAAIAVVIGPGHDAVEKEAKRLCPDVAIFVQRERLGTAHAVLAAREAIARGADDLLVAFGDTPLITAETFARLRAALAQGAALAVLGFRAVDPTGYGRLLLDGSKLVAIREHADASEAERAITLCNAGVMAMDGRRALAILDKIGNTNSKGEYYLVDAVAIARSQGLDAVVIETSEDEVRGINTKAQLAQAEAAMQARLRQAAMDAGVTLIAPETVYLAADTTFGRDVTIEPFVVIGPGVSIGDGAVVHSFSHVVQSKLGSNTLLGPFARLRP... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q5ZRK6 | MNLQIIILAAGQGKRMYSDTPKVLHHLAGKPLLTHVVETAQQLNPNAIHVIYGHGGEQIKSSLPNLPVHWVHQAEQLGTGHAVLQAMPHIPDDAYVLVLSADVPLIQVETLQSLIECSQRQNPDHSVLALLVAELENPSGLGRIIRNNQGEIYSIVEEKDANEQVKNIKEIYSGVCCTLANNLKKWLPQLSNSNAQGEYYLTEIISLAVQNKTPITSLTAKNSFEVQGINNRQQLQQLERIWQQRAANQLMEKGATLADANRFDLRGELYCGKDVYIDINCIFTGKVVLGNGCKIGPNCSLTNVTLGDGCEVYANSVLEG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q8YAD4 | MSKRYAVVLAAGQGTRMKSKLYKVLHPVCGKPMVEHVVDQISTLNVDKVVTIVGHGAEKVQEHLAGKSEFVKQDEQLGTAHAVLQAKAELAGKDGVTLVVCGDTPLIEASTMEALLKYHHEKRAKATILTTVIEDPTGYGRIIRDDLGIVEKIVEHKDATEKEQRISEINTGTYCFDNKALFEALENVSNDNVQGEYYLPDVIKILKDSDEVVAAYRMESFEESLGVNDRIALAEASKLMQRRINENHMRNGVTLVNPESTYIDIDVKIGQDTVIEPGVMLRGKTVIGDDCVVTSGSEIVNSVIGERVHVRTSSIFESKV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q2W7U1 | MASSKLAVIVLAAGMGTRMKSSLPKVMHPLAGRPMVSHLLDTVSGLSPDRMVVVVGPDMELVGKTVAPFPTVIQADRLGTGHAVLQAKAALGQFDGDVLVLYGDTPLITRATLERMLAERRGPRDPAVVVLGFKPQDPGHYGRLVVGAEGLKAIVEYRDATPDQRENPLCNSGVMAIDGNRLWSLIERVDNKNSKGEYYLTDIVALARADGATCTHVEGDEAELLGVNARSELAVAEALVQARLREAAMDNGATLIDPATVWFSWDTKIGRDVTIWPHVVFGPGVTVGDNVEIKGFCHFEGCMVEAGVAAGPFTRLRPGA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q0AR24 | MSRSRSAIILAAGQGTRMKSKTVKVLHKVAGRPMLDWAVALAGDCGASDIVTVWGAHSPAVRDAAEALGTRTALQDPPKGTGHAVLAARAALADLSGDAIVLYADTPLITAATVARVFEALEGGASVAVLGFEPDDPAAYGRLITNEAGDLDRIVEFKDASEAERAVGLVNSGVLAAPAELLFDLLGEVGNDNANGEYYLTDVVGLARARDLRAAVVVADADEVLGVNSRADLAEAEAAFQSRMRQSMMADGVTLIAPETVFFAHDTQIARDVVIEPNVVFGPGVVIEEDVVVHAHSHIAGAHLKRGAHAGPFARLRPGA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q2RPX0 | MTKTAAVILAAGQGTRMKSALPKVLHPLAGRPMVAHLIHALGAVAPSRTVVVIGPGMESVADRVAPLPTVLQAERLGTAHAVAQAGEALAGFDGTVLILYGDTPLITPETLTRMVEARLAAEDPAVVVLGFRPADPLQYGRLITSPAGLEAIVEYKDATAEQRAIGLCNSGVMAVDGRVLFALLAAVGNDNAKGEYYLTDIVALARGMGRACAVVEGAAEELLGVNSRSELAAAEAVIQGRLREKAMEGGATLTAPETVFFSADTRLGRDVSIGPFVTFGPGVEIGDGVEIKGFCHIEGARVAAKATLGPYARLRPGATI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q1AXL7 | MAQAGSASPLFAVVLAAGKGTRMKSNRAKVLHTLCGVPMVNYVIGAIRPLVPERLLVVVGHQAEQVRAVLPEDAEPVLQPEQRGTGDAVRVALEAIPEEEGVLLVVNGDGPLISDRTLGELLERHRSAGVGATVLVAELPDPSGLGRVREDAGVVRITEERDATEAERRNRLCNLGLYAFELPELRRAIREISSGAGRGELYLTDVLEIIGRRSRAVTYRLKDLEEANLVNDRSQLARAEEILRRRILDAHMKEGVTVRDPVSTHIEASVEIGRDTVILPGTFLRGRTRIGSDCVIGPSTDLVDTVVEDGATVEHSVGRG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
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