ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q42689 | MAFALRGVTAKASGRTAGARSSGRTLTVRVQAYGMAAEYIWADGNEGKPEKGMIFNEMRSKTKCFEAPLGLDASEYPDWSFDGSSTGQAEGNNSDCILRPVRVVTDPIRGAPHVLVMCEVFAPDGKPHSTNTRAKLREIIDDKVTAEDCWYGFEQEYTMLAKTSGHIYGWPAGGFPAPQGPFYCGVGAESAFGRPLAEAHMEACMKAGLVISGINAEVMPGQWEYQIGPVGPLALGDEVMLSRWLLHRLGEDFGIVSTFNPKPVRTGDWNGTGAHTNFSTKGMRVPGGMKVIEEAVEKLSKTHIEHITQYGIGNEARLTG... | Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 41285
Sequence Length: 380
Subcellular Location: Plastid
EC: 6.3.1.2
|
P20478 | MSARILEDSPNARINKTILDRYLSLPLQENIVQATYVWIDGTGEDLRCKDRTLDFIPQSPKELPVWNYDGSSCYQAEGSNSDTYLYPVAIYKDPFRRGNNILVMCDTYKFDGTPTDTNKRKTCLEVANKCAAEEPWFGIEQEYTFLDFDGHPLGWPKNGFPGPQGPYYCGVGANKVYARDIVDAHYRACLYAGIKVSGTNAEVMPAQWEFQVGPCEGISIGDDLWMARFLLHRISEEFGIVSTLDPKPMPGDWNGAGAHTNVSTKAMREDGGIRDIEKAVAKLSKCHERHIRAYDPKQGQDNARRLTGKHETSSINDFSA... | Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 41304
Sequence Length: 369
Subcellular Location: Cytoplasm
EC: 6.3.1.2
|
P81643 | XIAGSEEYGKHCFKGAVADAYLAKH | Function: Plays a key role in the nitrogen metabolism of microorganisms, animals and plants.
Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 2677
Sequence Length: 25
Subcellular Location: Plastid
EC: 6.3.1.2
|
I3R584 | MSDTSTVKSQCEDQNIDLIRLLYVTPSGVIQANTVDVSEVDAAVESGVTLSEVIQVYDAFACRNRNSRFDAVGEVHLCPDPETFRPLPYADRAGAMLCNIRTLDGEPWDVDSRSSLQSVERDLRAKGLSPQVAFESEFSLFSRDGDGKINRGDEAGAYRTESIRGTHDAILHIVDALKAQGIDVKKYHPEFSPGKHEIVTGHHTGLEAADEHLLLRETVKSVAEQDGYQATFLPKPFDDGTNGCHINVSLWNGENQFFDPNHGDISETARQFIAGVLDHAPAVLALTAPTVNSYSRLQPRHGAAGYICWGWLNREALIRV... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the breakdown of putrescine via the biosynthesis of gamma-L-glutamylputrescine. Not required for glutamine synthesis . Is not able to compensate for the loss of glutamine synthetase .
Catalytic Activity: ATP + L-glutamate + putrescine = ADP + gamma-L-glut... |
P04771 | MSLLSDLINLNLSESTEKIIAEYIWVGGSGMDLRSKARTLPGPVDDPAKLPKWNYDGSSTDQAPGDDSEVILYPQAIFKDPFRRGNNILVICDVYTPAGEPLPTNKRYDAAKIFSHPDVVAEVPWYGIEQEYTLLQKDVNWPLGWPLGGYPGPQGPYYCGVGADKAYGRDIVDAHYKACVYAGINISGINGEVMPGQWEFQVGPSVGISAGDEVWAARYILERITELAGAVVSFDPKPIPGDWNGAGAHSNYSTKSMREEGGYEVIKKAIEKLGLRHKEHIAAYGKGNERRLTGRHETADINTFSWGVANRGSSVRVGRD... | Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 39205
Sequence Length: 356
Subcellular Location: Cytoplasm
EC: 6.3.1.2
|
P81107 | DVNWPLGWPVGGYPG | 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): 1614
Sequence Lengt... |
Q02154 | MTKFKLEYIWLDGYTPVPNLRGKTQIKEFDEFPTLEQLPLWGFDGSSTMQAEGSSDCVLKPVAIYPDPARTNGALVMCEVMMPDGHAHASNARATILDDEDAWFGFEQEYFFYQNGRPLGFPEQGYPAPQPYYTGVGYSNVGDVAREIVEEHLDLCLAAGINHEGINAEVAKGQWEFQIFGKGSKKAADQIWMARYLLQRLTEKYGIDIEYHCKPLGDTDWNGSGMHCNFSTKYLREVGGKEYFEALMASSDKNLMDHIAVYGPDNDKRLTGKHETAPWNKFSYGVADRGASIRVPHSFIKNDYKGYLEDRRPNSQGDPY... | Function: Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 36979
Sequence Length: 326
Subcellular Location: Cytoplasm
EC: 6.3.1.2
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Q9RDS6 | MDKQQEFVIRTLEERDIRFVRLWFTDVLGFLKSVAVAPAELEQAFDEGIGFDGSAIEGFARVYESDMIAKPDPSTFQVLPWRAEAPGTARMFCDILMPDGSPSFADPRYVLKRALARTSDLGFTFYTHPEIEFFLLKDKPVDGSVPTPADNSGYFDHTPQNIGMDFRRQAITMLESMGISVEFSHHEGAPGQQEIDLRYADALSTADNVMTFRLVMKQVALEQGLQATFMPKPFSEYPGSGMHTHLSLFEGDRNAFYESGAEYQLSKVGRSFIAGLLRHAAEISAVTNQWVNSYKRIWGGTERTAGAGGEAPSYICWGHN... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the catabolism of polyamines. Catalyzes the ATP-dependent gamma-glutamylation of polyamines. Substrates include putrescine, cadaverine, spermidine and spermine, with a preference for short-chain polyamine putrescine . No complementation of the L-glutamine... |
P22878 | MSIKAEYIWIDGTQPTAKLRSKTKILSDGSRLPRWGFDGSSTNQAEGHASDLVLEPVFSCPDPIRGGDHLLVLCEVLHTDLTPHPSNTRALLRPVAERFAGQEPIFGIEQEYTFLKGDRPLGFPEGGGYPAPQADYYCGVGADAIFGREIVEKHLDLCLAAGLGLSGINAEVMPGQWEFQVGALPPLEVSDHMWVARWLLHRVAEEFGVTASLDAKPAKGDWNGAGAHTNFSTRAMREGYDPIITACEALGQDDKPLEHVRQYGTGIEDRLTGAHETAPWDAYSYGASDRGASVRIPWQVEVEKKGYIEDRRPNANVDPY... | Function: Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mass (Da): 37417
Sequence Length: 340
Subcellular Location: Cytoplasm
EC: 6.3.1.2
|
Q5NPH0 | MPVSFLSLASQPQIIDYPAIKEEIDSIKKVAAGDPVSEYRAVSLVLKQTVLKGREVIAEALTRRPHQGRIAALSYAYLTDQIIQLALYAMVGDDEKATDNLVILAVGGYGRGEMALHSDVDIAFLSRRSPRKAQKKLIESLISLLWDVGLRVSQSHRSLSDMVKMAKKDITIRTALLESRYLVGDKALFEEASTRFIQKVVAGSGRDFVAAKLLEWDERHLARGDSRYLVEPHLKEGKGGLRDLQSLFWIAKYLYLEKEARHTVLTSPILTDYALVKADLIAGHEAKRFRRCENFLWAVRCHLHILVKRPEERLNFDVQR... | 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 ... |
O24495 | MPVISKASSTTTNSSIPSCSRIGGQLCVWPGLRQLCLRKSLLYGVMWLLSMPLKTLRGARKTLKITHFCSISNMPSSLKIELVPCSKDNYAYLLHDEDTGTVGVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDRIPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDDTNIYCGRENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLSIPDSATEAEA... | Cofactor: Binds 1 Fe(2+) or Fe(3+) and 1 Zn(2+) ion per subunit. Electron spin resonance indicates the presence of a mixture of protein molecules that contain either Fe(2+) or Zn(2+).
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activi... |
Q9SID3 | MQTISKASSATSFFRCSRKLSSQPCVRQLNIRKSLVCRVMKLVSSPLRTLRGAGKSIRVSKFCSVSNVSSLQIELVPCLKDNYAYILHDEDTGTVGVVDPSEAEPIIDSLKRSGRNLTYILNTHHHYDHTGGNLELKDRYGAKVIGSAMDKDRIPGIDMALKDGDKWMFAGHEVHVMDTPGHTKGHISLYFPGSRAIFTGDTMFSLSCGKLFEGTPKQMLASLQKITSLPDDTSIYCGHEYTLSNSKFALSLEPNNEVLQSYAAHVAELRSKKLPTIPTTVKMEKACNPFLRSSNTDIRRALRIPEAADEAEALGIIRKA... | Cofactor: Binds 1 Fe(3+) ion per subunit. Electron spin resonance clearly indicates the presence of Fe(3+) .
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + gluta... |
A5FZE9 | MAISHRGFTITRVPMLADNYAWLVAHGGASAFVDPADAAAAIEAVEAAGGRLDWVLLTHHHDDHIAGAVDLAARFGARIAGNAADAARLPRLDAALAPGQTIDLGGEAVRMIATPGHTVGHVTYLFGDAAAACGDTLFSLGCGRMFEGTPAQFHASLQALAALDPETLMLCGHEYTLSNARFARHVDPDNAALAARAAEAERLRAAGAPTLPVRLADELAANPFLRAASAEEFARLRAAKDKF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 25336
Sequence Length: 243
Pathw... |
A0KIK2 | MYPVITVPAFNDNYIWLIRHENHCLVVDPGDAEPVLERLAALDLQLDAILLTHHHHDHVGGVTALLGHFPHARLYGPKLDPMPAHHGQWLDDGDQINWHGLSLEVIHVPGHTHGHIAYYGHGMLFCGDTLFSAGCGRLFEGTPAQMHASLQRLAALPDDTLIYCAHEYTLSNLRFAYAVEPDNHAIQQRIGLISKLRQQGLPSLPSRLGDEREFNVFLRCEQDSVKFSAEKHALKCLENPEDTFTVLRSWKDVF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28622
Sequence Length: 254
Pathw... |
Q8U9W1 | MKPLEIDVFLCRSDNFGVLLHDPESGATAAIDAPEEGPILRALDGHGWKLTHIFTTHHHQDHVEANLVLKDKFRCEVHGPYDEAIAIPGLDRSQADGDEFEFAGRRVQVIATPGHTAGHICYYLPDDGLLFAADTLFAMGCGRLFERPAADMWHSFQKLMALPDDTRVYFGHEYTLSNARFALTVDPDNAVLRERAARVETARQANEFTIPTTIGLEKQTNPYMRVADAGIRRHLGLEGAADADVFAEIRTRKDNF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28555
Sequence Length: 256
Pathw... |
Q21YF8 | MQLIPLPAFTDNYIWMVHDERHALVVDPGDAQPVLEALQQLGLQLETILVTHHHPDHTGGVAALRAATGAQVFGPAREPMPEPLIRLTGDQQLQALGLNFQVIDVPGHTACHIAYFCADVDGAPLLFCGDTLFSAGCGRLFEGSPAQMLASLDTLAALPDATRVCCAHEYTLSNLKFACAVEPVNQALTDYTVKAEALRSQQQPTLPSSILLERQINPFLRTRQATVTQAVQAFDASARDEVSIFAALRQWKNQF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 27765
Sequence Length: 255
Pathw... |
Q2IJC6 | MIFDRRRYGKDNYTYLLAAGGDAALVDPGDPDAALALAAAHGVRPRWILHTHGHADHTGGTAAVARALGAQVLGHGGDAARYRPDVDLAGRAEVALGALALRVHPVPGHTPGSVLLEWEGRLLTGDTLFWAGCGNCRHGGDPARLAESFLGPIARLDGGLEVHPGHDYAAPNLAFALALEPDGAAARARLAEVEAAHAAGLEPAPSTLAGERAVNPFLRLDAPGVAAAVARAEPSAAAAGPARRFVALRALRDRA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 26228
Sequence Length: 255
Pathw... |
A3QET2 | MHTVTPIPAFNDNYIWLIHAKDSGGHYVVDPGDAKAVLDYLEQHQIVLDGILITHHHSDHTGGIAELQASHDHKLTVYGPDNENIKGINHPISGQTESVKPEKLDSDAAVFHLPGHTLGHIAYLIDDHLFCGDTLFSAGCGRLFEGTPAQMHHSLQTLAQLDETTLVYPAHEYTQANLAFALTVENDNEALIAHAAKVKQLRDQNLPSLPSSIGLEKQINPFLRPEQASIKQNLSCHFAQDVTDDGTSFTLLRQWKDNFL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28740
Sequence Length: 260
Pathw... |
Q8EE27 | MLTITAINAFNDNYIWVLQQDTQQAVYVVDPGDVNVVLDYLNAHQLTLAGILITHHHRDHTGGIAALVAYVEQTTGHTLAVYGPQSEAIQGVNIAIEPQITQILHLPFLNSPVQVLSVPGHTAGHIAYLVDGALFCGDTLFSGGCGRLFEGTPAQMCHSLRLLAALPAETRVYCAHEYTLANLKFAQAADPSNAKLKAYNEQATALRAQGKATIPSTIGLERSINPFLRGLTPTIVDSIKQQFCDQDLSNVDELTYFTLLRQWKDIF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 29167
Sequence Length: 267
Pathw... |
A8H589 | MLHITPLAAFNDNYIWVFQSQQNTGAESSGIYVVDPGDGQVVIDYLIQTGQALLGILITHHHHDHTGGIEQLIRRFGAQIAVYGPQSENIIGVNHPIVANGDISLTNAGLNAKVIQLPGHTLGHIAYLIEDVLFCGDTLFSAGCGRIFEGSAEQMYQSLSELGQLPDNTKVCCAHEYTIANLAFANRVEPNNAALIDYTKKAQALRAQNLPTLPSSIGQEKAINPFLRSDSEEICQSLSIQFQQPINNPLQSFSLLRQWKDNF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28825
Sequence Length: 263
Pathw... |
Q8Z553 | MKFDTVIMGGGLAGLLCGLQLQQHGLRCAIVTRGQSALHFSSGSLDLLSALPNGQPVTDITAGLDALRRQAPEHPYSRLGAQKVLTLAQQAQTLLNASGAQLYGDVQQAHQRVTPLGTLRSTWLSSPEVPVWPLSAQRICVVGVSGLLDFQAHLAAASLRQRDLNVETAEIDLPELDVLRDNPTEFRAVNIARLLDNEEKWQLLYDALSPIATNCDMIIMPACFGLANDTLWRWLNERLPCALTLLPTLPPSVLGIRLHNQLQRQFVRQGGIWMPGDEVKKVTCRRGTVSEIWTRNHADIPLRPRFAVLASGSFFSSGLV... | Function: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor.
Catalytic Activity: a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45754
Sequence Length: 419
Pathway: Polyol m... |
Q9KLJ6 | MMHYDVAVIGGGIAGYSAALRALQAGKKVVLINQGQSALHFSSGSIDVLGRLPDGSVVNQPFDALSALQQQAPEHPYSKVGRKNSEKGLMWFKRTLDSAHVPLHHEPDGANHWRITPLGTLKNTWLSQPFVYPYRGNADFSRIMIVAIDGYRDFQPAMLRDNLAQRPELANTPMLTVNVSIPGFEGFRRNPNELRSIDIARLLRQESAWNALCDQLMRVARPDDLVIMPAIMGNGDGLHLMSKLQQVTQLRFHEVPTMPPSLLGIRIEEALHRSFIQGGGVQLKGDKVIGGNFAGSRLTAIHTQNLRDFPISAEHYVMAT... | Function: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor.
Catalytic Activity: a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate
Sequence Mass (Da): 48019
Sequence Length: 436
Pathway: Polyol metabolism; glycerol degradation via glycerol ki... |
P15421 | MYGKIIFVLLLSGIVSISASSTTGVAMHTSTSSSVTKSYISSQTNGITLINWWAMARVIFEVMLVVVGMIILISYCIR | Function: This protein is a minor sialoglycoprotein in human erythrocyte membranes.
PTM: The N-terminal extracellular domain is heavily glycosylated on serine and threonine residues.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8463
Sequence Length: 78
Subcellular Location: Membrane
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Q65QH0 | MFKEITPQQAWQLMIEENATLVDIRDEQRFTYSHAKGAFHLTGQSYGKFQIQCDFDDPVIVSCYHGISSRNVAAFLVEQGYDNIYSIIGGFEGWQRAGLPIETAY | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 11973
Sequence Length: 105
Subcellular Location: Cytoplasm
EC: 2.8.1.1
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Q9CL12 | MSAFSEISPQQAWQLVQQHAAALLDIRNETHFALAHPAQAFHLSHQSYGEFEMQYEDDHPVIVICYHGVSSRGAAMYLIEQGYTQVYSVTGGFEAWERDGLPIERIG | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 12081
Sequence Length: 107
Subcellular Location: Cytoplasm
EC: 2.8.1.1
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Q6CZL2 | MEQFEAISIEQAHSRWQEGGVVVDIRDPQSFAAAHVPGATHLTNETLPDFVRGADFEAPVMVICYHGISSRNAAQYLISQGFDSVYSIDGGFEAWQHRYPQDTQA | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 11670
Sequence Length: 105
Subcellular Location: Cytoplasm
EC: 2.8.1.1
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Q48NU0 | MTEFKRIPPEQAQALREQGAVLVDVRDAQTFQSNHIPDSVHLDNHSIADFIAKADLDKPLVVVCYHGNSSQSAAAYLVGQGFSDVYSVDGGFELWRATYPDETVQG | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 11652
Sequence Length: 106
Subcellular Location: Cytoplasm
EC: 2.8.1.1
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Q15ZU3 | MEQFAHISVQETQQKLAAKEARLVDIRDEQSFVAGHIEGAVHLTNGTLVNFTQETDFDTPVIVCCYHGVSSQQAAQFLLHQGFEEVYSMDGGFEAWRQSLPFVSGE | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 11834
Sequence Length: 106
Subcellular Location: Cytoplasm
EC: 2.8.1.1
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Q9I5U8 | MSDTFQRIAPEQVRQLRENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQGFSDVYSLDGGFELWRSVYPADTSSGEAE | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 11963
Sequence Length: 110
Subcellular Location: Cytoplasm
EC: 2.8.1.1
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A9VI58 | MKKYILSLDQGTTSSRAILFNKEGKIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRETAVVWDKTTGKPIYNAIVWQSRQTVEICDELKEKGYSEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENGELLFGTIDTWLVWKLSGGKAHITDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRQSSEIYGETIDYHFFGQNVPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAWGLDGKVNYALEGSIFVAGSAIQWLRDGLR... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), including enzyme I, and histidine-containing protein (HPr) are required for the phosphorylat... |
P18157 | METYILSLDQGTTSSRAILFNKEGKIVHSAQKEFTQYFPHPGWVEHNANEIWGSVLAVIASVISESGISASQIAGIGITNQRETTVVWDKDTGSPVYNAIVWQSRQTSGICEELREKGYNDKFREKTGLLIDPYFSGTKVKWILDNVEGAREKAEKGELLFGTIDTWLIWKMSGGKAHVTDYSNASRTLMFNIYDLKWDDELLDILGVPKSMLPEVKPSSHVYAETVDYHFFGKNIPIAGAAGDQQSALFGQACFEEGMGKNTYGTGCFMLMNTGEKAIKSEHGLLTTIAWGIDGKVNYALEGSIFVAGSAIQWLRDGLR... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), including enzyme I, and histidine-containing protein (HPr) are required for the phosphorylat... |
Q6MJQ2 | MFMSSFIMAIDQGTTSSRTCIINQAGGLVAEAREAFKQIFPKPGWVEHDPEDIWYSTQRSMRLALEKAKIKGSQIRTIGITNQRETVMLWDAKSGKALHNAIVWQCRRTQDLCEKLKKNKKEKIITAKTGLVLDPYFSATKIQWLLKNVPNAAKKAKDGQALAGTVDSFLLWKLTAGHSHKTDVSNASRTMLMNIHTGWWDEDLLKIFGVPEAILPEICPSNSDFGVTQGLGFMPDGIPITGIVGDQQAALFGQTCFETGDSKCTFGTGSFLLLNTGKKAVKSKNKLLTTIAWKLKNQEMTYALEGGAFVCGAAVQWLRD... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 54309
Sequence Length: 495
Pathway: Polyol metabolism; glycerol degradation ... |
B2IE09 | MTKYVAVIDQGTTSTRCMVFNKQGEIVAQHQLEHEQICPQAGWVEHDPLEIWERTKDVIHGSVAKAGLVAADIAAIGITNQRETTMIWNRKTGQPYGNAIVWQDTRTDIVCNQMSAEGGQNRFQAKTGLPLATYFSGPKIRWMLDHYPGLRQDAEKGEALFGNMDSWLIWKLTGGPGPAAVHVTDVTNASRTMLMNLKTLDWDEELLSAFAIPRAMLPSIRPSSDPEFYGFTRQDGPFGGEIPICGDLGDQQAATVGQVCFDAGEAKNTYGTGCFMLMNTGTEMVHSNHGLLTTVCYQFGHEKPHYALEGSVAIAGALVQ... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 55758
Sequence Length: 507
Pathway: Polyol metabolism; glycerol degradation ... |
B2A2C4 | MQNYVISLDQGTTSSRAILYDQQGNIVKSAQKEITQHYPQSSWVEHDASEIWGTQSGVLREVLETAGIRPNQIAAIGIANQRETTVIWDKESGKPIHNAIVWQDRRTAPICEELEKQGLKEYIRQNTGLVIDAYFSATKVKWLLDNVNGAREKAKNGQLLFGTVDSWLIWNLTRGHVHVTDYTNASRTMMFNIHELDWDDKILDVLDIPREMLPEIKESSEIYGYTDEHTLGGAQIPISGIAGDQQSALFGQGCFERGMMKNTYGTGCFLLMNTGKDPVISKNGLLTTIAWAIDGEIYYALEGSIFIAGAAVQWLRDNLK... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 55707
Sequence Length: 498
Pathway: Polyol metabolism; glycerol degradation ... |
P08194 | MLSIFKPAPHKARLPAAEIDPTYRRLRWQIFLGIFFGYAAYYLVRKNFALAMPYLVEQGFSRGDLGFALSGISIAYGFSKFIMGSVSDRSNPRVFLPAGLILAAAVMLFMGFVPWATSSIAVMFVLLFLCGWFQGMGWPPCGRTMVHWWSQKERGGIVSVWNCAHNVGGGIPPLLFLLGMAWFNDWHAALYMPAFCAILVALFAFAMMRDTPQSCGLPPIEEYKNDYPDDYNEKAEQELTAKQIFMQYVLPNKLLWYIAIANVFVYLLRYGILDWSPTYLKEVKHFALDKSSWAYFLYEYAGIPGTLLCGWMSDKVFRGN... | Function: Responsible for glycerol-3-phosphate uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50310
Sequence Length: 452
Subcellular Location: Cell inner membrane
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P96335 | MFGPFKPAPHIAELPAEKIDSTYKRLRWQVFAGIFFGYAAYYFVRANFDLAQPGLIQAGLYSKAELGVIGSAAGLAYGLSKFVMAGMSDRSNPRVFLPFGLLLSGLCMTLMGLFPWATSGIAIMWVMIFLNGWFQGMGWPPCGRTMVHWWSKSERGTIVSIWNTAHNIGGMVPGAMVLLASAIFFSTHGIEAQAKDVWQQSLYFPGIAAMIFAIPVYFVMRDTPQSCGLPSIEKWRNDYPDDYNEKTYENDLTAKEIFVTYVLKNKLLWYIAIANVFVYLIRYGVLKWSPVYLSEVKHFNIKGTAWAYTIYELAAVPGTL... | Function: Responsible for glycerol-3-phosphate uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53045
Sequence Length: 480
Subcellular Location: Cell inner membrane
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P21437 | MMSLAWPLFRVTEQAALAAWPQTGCGDKNKIDGLAVTAMRQALNDVAFRGRVVIGEGEIDHAPMLWIGEEVGKGDGPEVDIAVDPIEGTRMVAMGQSNALAVMAFAPRDSLLHAPDMYMKKLVVNRLAAGAIDLSLPLTDNLRNVAKALGKPLDKLRMVTLDKPRLSAAIEEATQLGVKVFALPDGDVAASVLTCWQDNPYDVMYTIGGAPEGVISACAVKALGGDMQAELIDFCQAKGDYTENRQIAEQERKRCKAMGVDVNRVYSLDELVRGNDILFSATGVTGGELVNGIQQTANGVRTQTLLIGGADQTCNIIDSL... | Cofactor: Manganese. Mg(2+), Co(2+), Ni(2+), Ca(2+), Cu(2+) and Zn(2+) cannot support activity.
Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Also displays a low activity toward glucose 1,6-bisphosphate, and no activity against ribulose 1,5-bisphosphate, fructose 2,6-bisphosph... |
Q03224 | MERSLSMELVRVTEAAALASARWMGRGKKDEADEAATSAMRDVFDTVPMKGTVVIGEGEMDEAPMLYIGEKLGNGYGPRVDVAVDPLEGTNILASGGWNALTVIAVADHGTLLNAPDMYMQKIAVGPEAVGCIDIEAPVIDNLKAVAKAKNKDVEDVVATILNRERHAKIISELREAGARIKLINDGDVAGAINTAFDHTGVDILFGSGGAPEGVLSAVALKALGGEIIGKLLPQSEEEITRCHKMGLDLSKVLRMEDLVKGDDAIFAATGVTDGELLKGVQFKGSVGTTESLVIRAKSGTVRFVDGRHSLKKKPNLVIR... | Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Can functionally substitute for the FBPase class 3 (Fbp) of B.subtilis.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 33951
Sequence Length: 321
Pathway: Ca... |
Q6M6E7 | MNLKNPETPDRNLAMELVRVTEAAALASGRWVGRGMKNEGDGAAVDAMRQLINSVTMKGVVVIGEGEKDEAPMLYNGEEVGTGFGPEVDIAVDPVDGTTLMAEGRPNAISILAAAERGTMYDPSSVFYMKKIAVGPEAAGKIDIEAPVAHNINAVAKSKGINPSDVTVVVLDRPRHIELIADIRRAGAKVRLISDGDVAGAVAAAQDSNSVDIMMGTGGTPEGIITACAMKCMGGEIQGILAPMNDFERQKAHDAGLVLDQVLHTNDLVSSDNCYFVATGVTNGDMLRGVSYRANGATTRSLVMRAKSGTIRHIESVHQL... | Cofactor: Manganese. Mn(2+) can be replaced by Mg(2+).
Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Is essential for growth on gluconeogenic carbon sources. Also displays a low activity toward glucose 6-phosphate, and fructose 6-phosphate, glycerol 3-phosphate, ribulose 1,5-b... |
P0A9D0 | MRRELAIEFSRVTESAALAGYKWLGRGDKNTADGAAVNAMRIMLNQVNIDGTIVIGEGEIDEAPMLYIGEKVGTGRGDAVDIAVDPIEGTRMTAMGQANALAVLAVGDKGCFLNAPDMYMEKLIVGPGAKGTIDLNLPLADNLRNVAAALGKPLSELTVTILAKPRHDAVIAEMQQLGVRVFAIPDGDVAASILTCMPDSEVDVLYGIGGAPEGVVSAAVIRALDGDMNGRLLARHDVKGDNEENRRIGEQELARCKAMGIEAGKVLRLGDMARSDNVIFSATGITKGDLLEGISRKGNIATTETLLIRGKSRTIRRIQS... | Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 35852
Sequence Length: 336
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplas... |
P47871 | MPPCQPQRPLLLLLLLLACQPQVPSAQVMDFLFEKWKLYGDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPANTTANISCPWYLPWHHKVQHRFVFKRCGPDGQWVRGPRGQPWRDASQCQMDGEEIEVQKEVAKMYSSFQVMYTVGYSLSLGALLLALAILGGLSKLHCTRNAIHANLFASFVLKASSVLVIDGLLRTRYSQKIGDDLSVSTWLSDGAVAGCRVAAVFMQYGIVANYCWLLVEGLYLHNLLGLATLPERSFFSLYLGIGWGAPMLFVVPWAVVKCLFENVQCWTSNDNMGFWWILRFPVFLAILINFF... | Function: G-protein coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand bind... |
Q61606 | MPLTQLHCPHLLLLLLVLSCLPEAPSAQVMDFLFEKWKLYSDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPPNTTANISCPWYLPWYHKVQHRLVFKRCGPDGQWVRGPRGQPWRNASQCQLDDEEIEVQKGVAKMYSSQQVMYTVGYSLSLGALLLALVILLGLRKLHCTRNYIHGNLFASFVLKAGSVLVIDWLLKTRYSQKIGDDLSVSVWLSDGAMAGCRVATVIMQYGIIANYCWLLVEGVYLYSLLSLATFSERSFFSLYLGIGWGAPLLFVIPWVVVKCLFENVQCWTSNDNMGFWWILRIPVFLALLINF... | Function: G-protein coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand bind... |
P09832 | MSQNVYQFIDLQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQTNTLPEVCGRVCPQDRLCEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRPDMSGVKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSMRGGLENEDADGVYAALPFLIANTKQLMGFGETRDEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRR... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate.
Catalytic Activity: 2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine + NADPH
Sequence Mass (Da): 52015
Sequence Length: 472
Pathway: Amino-acid biosynthesis; L-glutama... |
E1V8I0 | MANRLNNDFQFIDVGRQDPEKKPARTRAKQFAEIYEPYKPQDAAAQAHRCLHCGNPYCEWKCPVHNYIPNWLQLVSEGNILEAAELSHRTNSLPEVCGRVCPQDRLCEGDCTLNDGFGAVTIGSVEKYITDTAFAMGWRPDMSKVTWTDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKYPEIGGLLTFGIPEFKLEKTVMERRRAVFEEMGVEFCLGVEIGRDMPFEQLLEEYDAVFLGMGTYKYMEGGFPGEDLPGVHKALDYLVANVNHCLGFETDPADYVSLEGQRVVVLGGGDTAMDCNRTAIRQGAASVTCAY... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate.
Catalytic Activity: 2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine + NADPH
Sequence Mass (Da): 51995
Sequence Length: 472
Pathway: Amino-acid biosynthesis; L-glutama... |
P9WN18 | MADPGGFLKYTHRKLPKRRPVPLRLRDWREVYEEFDNESLRQQATRCMDCGIPFCHNGCPLGNLIPEWNDLVRRGRWRDAIERLHATNNFPDFTGRLCPAPCEPACVLGINQDPVTIKQIELEIIDKAFDEGWVQPRPPRKLTGQTVAVVGSGPAGLAAAQQLTRAGHTVTVFEREDRIGGLLRYGIPEFKMEKRHLDRRLDQMRSEGTEFRPGVNVGVDISAEKLRADFDAVVLAGGATAWRELPIPGRELEGVHQAMEFLPWANRVQEGDDVLDEDGQPPITAKGKKVVIIGGGDTGADCLGTVHRQGAIAVHQFEIM... | Cofactor: Binds 1 [4Fe-4S] cluster.
Catalytic Activity: 2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine + NADPH
Sequence Mass (Da): 53452
Sequence Length: 488
Pathway: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+) route): step 1... |
P28721 | MFFKKNLTTAAICAALSVAAFSAMATDSTDTELTIIGEYTPGACTPVVTGGGIVDYGKHHNSALNPTGKSNKLVQLGRKNSTLNITCTAPTLIAVTSKDNRQSTIVALNDTSYIEKAYDTLVDMKGTKNAFGLGSAPNGQKIGAASIGIDRSNGGIHAADDTGEIPVDLIQTDHWSAATPTWKASSNGAFCSLTSCSAIERGYSVAKTGELTPVAITAVTFPLLIDAAVNDNTILGSDETIKLDGNVTISVQYL | Function: Involved in induction of the so-called NTR enzymes in response to nitrogen deprivation, as well as in glutamate biosynthesis. May mediate the glutamate-dependent repression of the GLT operon.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26352
Sequence Length: 254
Subcellular Location: C... |
P0AER4 | MSIDWNWGIFLQQAPFGNTTYLGWIWSGFQVTIALSICAWIIAFLVGSFFGILRTVPNRFLSGLGTLYVELFRNVPLIVQFFTWYLVIPELLPEKIGMWFKAELDPNIQFFLSSMLCLGLFTAARVCEQVRAAIQSLPRGQKNAALAMGLTLPQAYRYVLLPNAYRVIVPPMTSEMMNLVKNSAIASTIGLVDMAAQAGKLLDYSAHAWESFTAITLAYVLINAFIMLVMTLVERKVRLPGNMGGK | Function: Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27503
Sequence Length: 246
Subcellular Location: Cell inner membrane
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P0AER7 | MYEFDWSSIVPSLPYLLDGLVITLKITVTAVVIGILWGTMLAVMRLSSFAPVAWFAKAYVNVFRSIPLVMVLLWFYLIVPGFLQNVLGLSPKNDIRLISAMVAFSMFEAAYYSEIIRAGIQSISRGQSSAALALGMTHWQSMKLIILPQAFRAMVPLLLTQGIVLFQDTSLVYVLSLADFFRTASTIGERDGTQVEMILFAGFVYFVISLSASLLVSYLKRRTA | Function: Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24915
Sequence Length: 224
Subcellular Location: Cell inner membrane
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Q7Z4T8 | MRNAIIQGLFYGSLTFGIWTALLFIYLHHNHVSSWQKKSQEPLSAWSPGKKVHQQIIYGSEQIPKPHVIVKRTDEDKAKSMLGTDFNHTNPELHKELLKYGFNVIISRSLGIEREVPDTRSKMCLQKHYPARLPTASIVICFYNEECNALFQTMSSVTNLTPHYFLEEIILVDDMSKVDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGASHASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKPSPLVRGTFDWNLQFKWDNVFSYEMDGPEGSTKPIRSPAMSGGIFAIRRHYFN... | Function: Probable inactive glycosyltransferase required during spermatid development. May participate in protein loading into the acrosomes and accumulation of ubiquitin-proteasome systems around the head-tail coupling apparatus region.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 51427
... |
Q9D4M9 | MKSVIIQGLFCGFLAIGLWASMLLLFLHLEQEDMLENEKEELLKKRSLGKNAHQQTRHSEDVTHDEVNFSDPELIQGLRRYGLNAIMSRRLGIEREVPDSRDKICQQKHYPFNLPTASIIICFYNEEFNTLLRAVSSVVNLSPQHLLEEIILVDDMSEFDDLKDKLDYYLEIFRGKVKLIRNKKREGLIRSKMIGASRASGDILVFLDSHCEVNRVWLEPLLHAIAKDHKMVVCPIIDVINELTLDYMAAPIVRGAFDWNLNLRWDNVFAYELDGPEGPSTPIRSPAMTGGIFAINRHYFNELGQYDNGMDICGGENVEL... | Function: Probable inactive glycosyltransferase required during spermatid development. May participate in protein loading into the acrosomes and accumulation of ubiquitin-proteasome systems around the head-tail coupling apparatus region.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 49874
... |
Q49A17 | MKRKQKRFLQMTLLFTVALIFLPNVGLWSLYKDKHLVKSAEPGEQQTFPLGLGDGQFYSWTDGLRRKDWHDYESIQKEAMRSGKGEHGKPYPLTEEDHDDSAYRENGFNIFVSNNIALERSLPDIRHANCKHKMYLERLPNTSIIIPFHNEGWTSLLRTIHSIINRTPGSLIAEIILVDDFSEREHLKDKLEEYMARFSKVRIVRTKKREGLIRTRLLGASMARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMIDVIDHNHFGYEAQAGDAMRGAFDWEMYYKRIPIPPELQRADPSDPFESPVMAGGLFAVD... | Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Catalytic Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[pro... |
P0AAG4 | MITLKNVSKWYGHFQVLTDCSTEVKKGEVVVVCGPSGSGKSTLIKTVNGLEPVQQGEITVDGIVVNDKKTDLAKLRSRVGMVFQHFELFPHLSIIENLTLAQVKVLKRDKAPAREKALKLLERVGLSAHANKFPAQLSGGQQQRVAIARALCMDPIAMLFDEPTSALDPEMINEVLDVMVELANEGMTMMVVTHEMGFARKVANRVIFMDEGKIVEDSPKDAFFDDPKSDRAKDFLAKILH | Function: Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for energy coupling to the transport system.
Catalytic Activity: a polar amino acid(out) + ATP + H2O = a polar amino acid(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Seq... |
Q5GZ90 | MPSPSYLGRFAPSPTGPLHFGSLLAAFGSWLLARHAGGQWCVRIEDIDPPRAEPGASERQLRTLTAFGLHSDLPVIRQSERDAAYTAAINRLLETGQAFECSCSRADLAGMGGIHHACVAPLGARRAVRLRVPPQSPVGFDDALHGRVLQDVYADVGDVVLRRADGYWAYQLAVVVDDAAQGITDVVRGADLLDSTPRQMLLQRALGVPQPRYLHLPLMLDGDGRKLSKSHGAPALDDTDPLPALHAAWAGLGQRPDALPRRATVTTLLQQAVRHFSPQLLPRQRQRDRATCAYERQRD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC an... |
Q8ZBL1 | MVQQAVIQRSANQRATNQPTEYIGRFAPSPSGDLHFGSLIAALGSYLQARAQGGKWLVRIEDIDPPREVPGAASRILAALEHYGLHWDGPVIYQSQRHEAYRATLNWLEQQGLSYYCTCTRSRIHQLGGFYDGYCRDRHLPASGAAIRLRQTQPVYAFYDKLLGELHAHPALAQEDFIIRRRDGLFAYNLAVVVDDAFQGVTEIVRGADLIEPTVRQIALYQQLQHPVPGYIHLPLALNNQGNKLSKQNHAPPLPNGDPRPILIDALKFLRQPLPEYWQDLDLYLLLRYAVKHWTLVSIPLQGAITPQKTQRHSQSKYGE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC an... |
Q9XST2 | TSIFETAGVGQPAYATIGAGVVNTVFTLVSVFLVERAGRRTLHLLGLAGMCGCAILMTIALLLLERLPAMSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFCNWTSNFIIGMGFQYIAXAMGPYVFLLFAVLLLAFFIFTFLKVPETR | Function: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon... |
P14672 | MPSGFQQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNETWLGRQGPEGPSSIPPGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLVNNVLAVLGGSLMGLANAAASYEMLILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILIAQVLGLESLLGTASLWPLLLGLTVLPALLQLVLLPFCPESPRYLYIIQNLEGPARKSLKRLTGWADVSGVLAELKDEKRKLERERPLSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFETAGVG... | Function: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon... |
P14142 | MPSGFQQIGSDDGEPPRQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNATWLGRQGPGGPDSIPQGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLANNVLAVLGGALMGLANAAASYEILILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILVAQVLGLESMLGTATLWPLLLALTVLPALLQLILLPFCPESPRYLYIIRNLEGPARKSLKRLTGWADVSDALAELKDEKRKLERERPMSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFESAGVG... | Function: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation . Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells . Up... |
Q3E880 | MVSIRVICYLLVFSVLQVHAKVSNANFNSQAPQMKNSEGLGASNGTQIAKKHAEDVIENRKTLKHVNVKVEANEKNGLEIESKEMVKKRKNKKRLTKTESLTADYSNPGHHPPRHN | Function: Acts as a peptide hormone recognized by receptors (e.g. RGI1 and RGI2) to trigger signaling events including the regulation of RITF1 expression and leading to the production of reactive oxygen species (ROS) in roots to modulate meristem size . Signaling peptide (root growth factor) that maintains the postembr... |
O51547 | MRDDQIFNLIEKEKLREREHIELIASENFTSLEIRQAVGSILTNKYAEGYPLNRYYGGCSFIDEIETLAISRAKELFGAKYANVQPHSGSQANMAAIMALISPGDRILGMQLSHGGHLTHGSRVNFSGIFFNTYFYGVSRDSELIDYDEVLKIAKDCRPNLIIAGASSYSREIDFKKFREIADDVSAYLLCDIAHIAGLIVAGFHNSSIDVAHLTTSTTHKTLRGPRGGIILSGKDFDKLVNFNGKEKPLFNAVNSTVFPGTQGGPLVHVIAGKAIAFKEALQESFKEYIANVIKNTKVMAEYFKSEGFRIVSGGTDNHL... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
D3DKC4 | MRHLFNTDAEIYEAIVKEYERQFYHLELIASENFTSLAVMEAQGSVMTNKYAEGLPHKRYYGGCEFVDIAEDLAIERAKALFDAEHANVQPHSGTQANMAVYMAVLKPGDTIMGMDLSHGGHLTHGAKVNFSGKIYNAVYYGVHPETHLIDYDQLYRLAKEHKPKLIVGGASAYPRVIDWAKLREIADSVGAYLMVDMAHYAGLIAGGVYPNPVPYAHFVTSTTHKTLRGPRSGFILCKKEFAKDIDKSVFPGIQGGPLMHVIAAKAVAFKEAMSQEFKEYARQVVANARVLAEEFIKEGFKVVSGGTDSHIVLLDLRDT... | Function: Its primary function is to catalyze the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecu... |
B1L5K9 | MDPVEAYGRVKSSILEHHKWFDSSLPMIASENVTSPAVRKAMTSDFGHRYAEGWVGERVYAGTKYIDEVESIAMELVKRLFNVKFADVRPISGVVANLAVYTAFTNPGDVAMALPITKGGHISMGPLRGSEGQFIGGTAGAVRGLDVKYLAFDDHNMNVDVDKSIKRIEENKPKLVILGGSVILFPHPVKELSDVCKSVGALLHYDAAHVAGLIAGKQFQQPMEEGADVMTMSTHKTFFGPQHGAVITNDEEKFERIKLANFPGLLSNHHLHSVAALALAAAEMLAFGEEYARAVVRNAKALAQALHDEGFSVVAEHLGF... | Function: Catalyzes the reversible interconversion of serine and glycine with a modified folate serving as the one-carbon carrier. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Sequence Mass (Da): 47777
Sequence Leng... |
Q5FMC0 | MKYAEKSPALWDAIRQEEKRQQNTIELIASENIVSDAVREAQGSVLTNKYAEGYPGRRYYGGCQYIDQVEQLAIDYAKKLFNAKFANVQPHSGSQANMAVYQALLKPGDVILGMGMDAGGHLTHGAKVNFSGKEYKSYEYGLNVETEELDFDQIRKVALEVKPKLIVAGASAYSRIIDWQKFRDIADEVGAYLMVDMAHIAGLVATDQHPSPIPVADIVTTTTHKTLRGPRGGMILSNNLEIGKKINSALFPGIQGGPLEHVIAGKAQAFYEDLQPQFTDYIKQVVKNAKAMAEVFDESENIRVVSGGTDNHLMIIDITD... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
Q5LPA8 | MNASHQDTGFFTEALSERDPELFGAITSELGRQRDEIELIASENIVSAAVMQAQGSVMTNKYAEGYPGRRYYGGCQYVDIAENLAIERAKQLFGCGFANVQPNSGSQANQGVFQALIKPGDTILGMSLDAGGHLTHGAAPNQSGKWFNAVQYGVRQQDNLLDYDQVEALAKEHRPKLIIAGGSAIPRQIDFARMREIADMVGAYLHVDMAHFAGLVAAGEHPSPFPHAHVATTTTHKTLRGPRGGMILTNDEDIAKKVNSAIFPGIQGGPLMHVIAAKAVAFGEALRPEFKTYIQQVIANAQALSDQLIKGGLDTVTHGT... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
Q54Z26 | MGSVSGNTPLKEVDNEIFELMNREKDRQFKGLELIASENFTSRAVMEALGSHFTNKYAEGYPGSRYYGGTEVVDELETLCQKRALKAFRLDESKWGVNVQPYSGSPANFAVYTALLRPHDRIMGLDLPSGGHLTHGYQTDKKKISASSIFFESMPYQIGADGLIDYQRLEENALLFKPKLIISGASAYPREWDYKRMRAIADKVGAYLMCDMAHYSGLVAAQLLDSPFDYCDVVTSTTHKTLRGPRSGIIFFRRGKRVDGNGKEIEEYDIESKINFAVFPSLQGGPHENVIAGVAVALKEADSQEFKEYALQVKKNAAAI... | Function: Interconversion of serine and glycine.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 50688
Sequence Length: 457
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 2.1.2.1
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O23254 | MEPVSSWGNTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALEAFHCDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTSGGKKISATSIYFESLPYKVNFTTGYIDYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRGPRAGMIFYRKGPKPPKKGQPEGAVYDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKA... | Function: Catalyzes the interconversion of serine and glycine with the conversion of tetrahydrofolate (THF) into 5,10-methylene-THF.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 51718
Sequence Length: 471
Pathway: One-car... |
Q9SVM4 | MEPVYSWGNTHLDFVDPEIYDLIEKEKHRQCRGIELIAAENFTSVAVMEALGSCLTNKYSEGMPGNRYYGGTEFIDEIESLCRSRSLEAFHCNPEKWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHITHGYYSSGGKNISATSIYFENLPYKVDSKTGYIDYDKLEEKAMDFRPKLIICGGTSYPREWDYARFRAVADKVGAFLLCDMAHNSALVAAQEAADPFEYCDVVTTSTHKSLRGPRAGMIFYRKGPKPAKKGQPEGEVYDFDAKINSAVFPALQSGPHNNKIGALAVALKQVMAPSFKVYAKQVKA... | Function: Catalyzes the interconversion of serine and glycine.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 52261
Sequence Length: 470
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location... |
P03212 | MRAVGVFLAICLVTIFVLPTWGNWAYPCCHVTQLRAQHLLALENISDIYLVSNQTCDGFSLASLNSPKNGSNQLVISRCANGLNVVSFFISILKRSSSALTGHLRELLTTLETLYGSFSVEDLFGANLNRYAWHRGG | 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. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the vira... |
P28941 | MYQILIGCVWQKSPYINQCTEFQPPLSFVTPERMRRFMRCWARLELVYMLAWIVTTKLVKATRLDFTWGPGEPKRILEASCGSGPIMKGQLFTSPNIKNLLNRTTGIMVKAHCNPPEAILWVDTPPKPVWVNPFAVVQGLAEDVTNGNMPQDFKEKLLFALDDSLSQSQSSPDEILGPPPLGCFTGPFFLSPPKSKDIAEGLKDSCIPASYYANLQKT | 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. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the vira... |
Q66649 | MRSLDRYAIFILLACGLLWRPCLSSVPMPCCPIDSKKDVSGLPSVFEVKEIFFNYPQTCNYTNVAQFTYVPQGANVSTVVCANGFNLMSFILAVLQRVFEKPHNMGLLAENINKIRTDYALNFTAVNSESSRFNVVPVGRNGKVVTTTRVVKRSARSGSGAPPG | 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. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the vira... |
Q77MS8 | MKIYRVLVHLSFVLGMFTKTNTVLAWSKYDLVHGFMRVANISSIMRLDCLPNLLSSNAGYAALPSDDIPTGIFIKVNCSIPEFILWYEQKAMAAWINPIMGTVLMMNDVLKSGLENSVKVGLLTFLKRIAEKGPNGPLRNRGSGCINLIAPADISCYGSTRLDRFNRDFEDDSRGMPCRAKAMRRTTSGSRRANA | 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. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the vira... |
O92277 | MYECMFFSHRLTIGFYIPLIVLTTMSSLSESLGERQKTACTVAAISCANSDTYNRTTVSNHTFFYISDRWKYSELIRYEKPTGDLRHDKLIHVDREFLDIVSLLHNNENQLRTLLTIFRSDSAPPWVKFMRGYSQCLDHPIIYTCVEEKCQQYNLEELPYGKDIFLENVVGFDLGAPPHNMSVLIAVSNTKPKITKVLRITSTSLTLFDALYNTVLTFFRSIGARNVDVVRRLILYQASLSGPHRDAPIHNYLNRDLS | 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. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the vira... |
F5HCH8 | MCRRPDCGFSFSPGPVILLWCCLLLPIVSSAAVSVAPTAAEKVPAECPELTRRCLLGEVFEGDKYESWLRPLVNVTGRDGPLSQLIRYRPVTPEAANSVLLDEAFLDTLALLYNNPDQLRALLTLLSSDTAPRWMTVMRGYSECGDGSPAVYTCVDDLCRGYDLTRLSYGRSIFTEHVLGFELVPPSLFNVVVAIRNEATRTNRAVRLPVSTAAAPEGITLFYGLYNAVKEFCLRHQLDPPLLRHLDKYYAGLPPELKQTRVNLPAHSRYGPQAVDAR | 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. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the vira... |
P10185 | MGILGWVGLIAVGVLCVRGGLPSTEYVIRSRVAREVGDILKVPCVPLPSDDLDWRYETPSAINYALIDGIFLRYHCPGLDTVLWDRHAQKAYWVNPFLFVAGFLEDLSYPAFPANTQETETRLALYKEIRQALDSRKQAASHTPVKAGCVNFDYSRTRRCVGRQDLGPTNGTSGRTPVLPPDDEAGLQPKPLTTPPPIIATSDPTPRRDAATKSRRRRPHSRRL | 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. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the vira... |
Q72AV1 | MTEEARRIVIEHAVEGTRLRESYFNGNADKVVDGARRMAVTLAKGHKLLFCGNGGSAADAQHLAAEFVNRFQMERPPLPAIALTTDTSIITAIGNDYSFDQIFEKQVQALGNEGDMLVGISTSGNSPNVVRAMHAARERGLATMGLTGRGGGEMAGLCDILFDVDHGRTALVQEVHITIGHLLCGLTDHFLFENVLALQPWLKDATNA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
Catalytic Activity: 2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
Sequence Mass (Da): 22429
Sequ... |
O25531 | MNTNKALFLDRDGIINIDKGYVSQKEDFEFQKGIFELLKHAKSLGYKLLLITNQSGINRGYYTLKDFEQLTQYLQESLFKELGFNLDGIYFCRHAPEENCACRKPKPSLILQAAKEHQICLEQSFMIGDKESDMLAGLNAKVKNNLLLIQNPLKTPHSWIQCKDFKEMIDLIK | Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
Sequ... |
Q9JWE9 | MKLIILDRDGVINQDRDDFVKSVDEWIPVEGSMDAVAFLTQAGYTVAVATNQSGIGRKYFTVQNLTEMHAKMHRLVRQAGGEINGIWFCPHTDADNCNCRKPKPGMIEDIIGRFNAQASETWLVGDSLRDLQAIDAVGGKPALVLTGKGKKTLSQHGHELPEHTQVFDTLLDFSQYIMQENAAPQAD | Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
Sequ... |
Q9JXI5 | MKLIILDRDGVINQDRDDFVKSVDEWIPVEGSMDAVAFLTQAGYTVAVATNQSGIGRKYFTVQNLTEMHAKMHRLVRQAGGEINGIWFCPHTDADNCNCRKPKPGMIEDIIGRFNAQASETWLVGDSLRDLQAIDAVGGKPALVLTGKGKKTLSQHGHELPEHTQVFDTLLDFSQYIMQENTAPQAD | Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
Sequ... |
Q9CK98 | MKKAIFLDRDGTLNIDHGYVHEIDQFQFIDGSIEALQQLKAMGYLLVLVTNQSGIARGYFSEDQFLQLTEWMDWSLADRGVDLDGIYYCPHHTEGKGEYCQDCDCRKPKPGMLLQAIKELNIDPNTSFMVGDKVEDMLAGKGAKIKNTVLVKTGKPITEDGKKQANYVLESIADLPKLIKGLKS | Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
Sequ... |
Q9I7C0 | MSRSLLILDRDGVINLDSDDYIKTLDEWIPIPSSIEAIARLSQAGWTVAVATNQSGIARGYYDLAVLEAMHARLRELVAEQGGEVGLIVYCPHGPDDGCDCRKPKPGMLRQIGEHYGVDLSGIWFVGDSIGDLEAARAVDCQPVLVKTGKGVRTLGKPLPEGTLIFDDLAAVASALLQ | Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
Sequ... |
Q88RS0 | MKLLILDRDGVINYDSDAYIKTLEEWVPIPGSVDAIAQLSKAGWTVAVATNQSGIARGYYPLATLEAMHARLRALVAEQGGEVGHIVYCPHGPDEGCDCRKPKPGMLRAIAEHYQIGLEGVWFVGDSKGDLEAALAVGAQPVLVKTGKGERTLEKGVPETTLIFDDLAAIARELI | Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + pho... |
Q98I56 | MADKTGTPHPLTEPGVWIERIGGRVFPPHLPALFLDRDGTINVDTDYPSDPAEIVLRPQMLPAIATANRAGIPVVVVTNQSGIARGYFGWSAFAAVNGRVLELLREEGVFVDMVLACAYHEAGVGPLAIPDHPMRKPNPGMLVEAGKRLALDLQRSLIVGDKLADMQAGKRAGLAQGWLVDGEAAVQPGFAIRPLRDSSELGDLLAAIETLGRDNRS | Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + pho... |
Q6N2R1 | MTASAPRRPAAFLDRDGVINYNDHYVGTRERLRWMPGIAAAIRQLNAAGYYVFIITNQSGVARGMFSEDDVRALHRWMLDELNTQGARIDDVRFCPHHVEGTLDAYRVACEHRKPGPGMILDLAKTWPVDMTRSFVIGDSASDVEAAKAAGIPGFRFEGEDIDVFVKQVLIEMQRAAVSN | Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position. Also catalyzes the dephosphorylation of D-glycero-alpha-D-manno-heptose 1,7-bisphosphate in vitro.
Catalytic Activity: D-gly... |
Q8KAY7 | MESAKVLFLDRDGTINRDIGRYVSSREEFILIDRADEAIAIAREAGFRIVLITNQAGIARGIVTPQDVEDVNDYLNELLAERQTSFDRCYYCPAHPNYPHPEYDRFIDHRKPSPRMVEQAIADLREEGFEVDRSASFFIGDKLIDVECGQRAGLKTILVRTGHNEESLCEQHQIFPDHVADDLYQAVTGYILGQPTSRD | Function: Converts the D-glycero-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 2267... |
Q9HKQ2 | METVRIIYVRDNQTLKTVFVDRDGTINRDCPYCHELDDLQIYDDTVGILKHYQGKGYRIIIVTNQSGIGRGYFSMEEFRRFNDGVVNRLLDLGVKVSATYFCPHRPDEGCSCRKPGIGLINEALSDFRVDIGGSLVIGDRDDVDGQLARNLGLPFRIVSH | Function: Converts the D-glycero-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 1810... |
Q8DH26 | MPRPAVFLDRDGVLNQEVGYIHRLEDLQLIPGVAQAVRRLNDAGWFCCLASNQSGPARDYYSIDHVHALHHRLQELLAASAGAVLDAVYFCPDLSRPEGGVVADYAGWTTWRKPNTGMLVAAAWDHDLDLSRSVMVGDKATDIDLARNAGCYGILVQTGFGDRVLEGSYQHASQPDYIAEDLAAAVEWICTHLAPR | Function: Converts the D-glycero-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 2148... |
Q0P8I7 | MSKKVLITGGAGYIGSVLTPILLEKGYEVCVIDNLMFDQISLLSCFHNKNFTFINGDAMDENLIRQEVAKADIIIPLAALVGAPLCKRNPKLAKMINYEAVKMISDFASPSQIFIYPNTNSGYGIGEKDAMCTEESPLRPISEYGIDKVHAEQYLLDKGNCVTFRLATVFGISPRMRLDLLVNDFTYRAYRDKFIVLFEEHFRRNYIHVRDVVKGFIHGIENYDKMKGQAYNMGLSSANLTKRQLAETIKKYIPDFYIHSANIGEDPDKRDYLVSNTKLEATGWKPDNTLEDGIKELLRAFKMMKVNRFANFN | Function: NAD-dependent dehydrogenase involved in the biosynthesis of heptose moieties with a hydroxyl group at C6 found on the capsular polysaccharide (CPS) of C.jejuni. Catalyzes the initial oxidation of C4 of the GDP-D-glycero-alpha-D-manno-heptose to form GDP-D-glycero-4-keto-alpha-D-lyxo-heptose in the presence of... |
P59215 | MGCTLSAEERAALERSKAIEKNLKEDGISAAKDVKLLLLGAGESGKSTIVKQMKIIHEDGFSGEDVKQYKPVVYSNTIQSLAAIVRAMDTLGVEYGDKERKADSKMVCDVVSRMEDTEPFSAELLSAMMRLWGDSGIQECFNRSREYQLNDSAKYYLDSLDRIGAADYQPTEQDILRTRVKTTGIVETHFTFKNLHFRLFDVGGQRSERKKWIHCFEDVTAIIFCVALSGYDQVLHEDETTNRMHESLMLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYPGSNTYEDAAAYIQTQFESKNRSPNKEIY... | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14 (By similarity).
PTM: Deamidation of Asn-346 converts alpha-1 to alpha-3.
Location Topology: Lipid-anchor
Sequence ... |
P50148 | MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDS... | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Required for platelet activation. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutroph... |
P21279 | MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDS... | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems . Required for platelet activation . Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity . Regulates chemotaxis of BM-derived neutr... |
P82471 | MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMVRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDS... | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Required for platelet activation. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutroph... |
P38410 | MTLESIMACCLSEEAEEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFSAMQAMIRAMETLKIPYKYEHNKGHALLVREVDVEKVASFENPYVDAIKYLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRIATHGYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDS... | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
PTM: Palmitoylated. Palmitoylation occurs in the Golgi and participates in the localization of GNAQ to the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da):... |
Q6FQ15 | MRLVSRRRLKGLALVAFALIGITIFVRILMEFQLEREVSFYKKFFRLKKDGLHGVYNPIDIKQIPKQTIDDLYRAKMETVSASKPIDWSKYAYVNYVTEPNYLCNTLIMFHALIKKFGTKAKLELLISNELFKSEIQSRNEQVQRILKKIRELDSEQIVIKEVQNIVKPTDQSPWNESLTKLLVFGLTEYERIIYLDNDAILQDKMDELFFLPNDITFAAPLTYWFMSEKDLEKTYKEVQHDKMSINLNKYTKQLSNRIRNGKEIYNHLPALPQSLYLNSDRVAKEILDSTSSASPLFDADSLKKVGKVKFASNLMVIKP... | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 58333
Sequence Length: 501
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q6BUZ2 | MKLVLGNGLVNLSWEYMLSFSILLYFIFTQLIFVFEDHSLAKNLKVIPSEVINALFDNFNKNLNFDKYAYVQYATDFDYLNLAIINFIVLRRSSTKIPNLVVLFNRALQEDKNRFDGLRDLSLRYSVTLKPIPIIENVNAESPTWSKSFTKFHIFNEVKYDRIVYFDADSMLLHTQWNDNSSIVNNESNVPENLDELFTIPEIIDIALPQAYWLTKHTKASGKIKAPDGKGYQDEITALINEISKSVNDSLVFEKLPSLLVQSQKSNHRNNFFATHVMVVKPSNEIFNELKKYVHNPWLWSLHKRHALRNKSDYDMEVLN... | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 54445
Sequence Length: 464
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q8T1C6 | MNENSIFVSIISYRDSECQWTIKNLIELAKYKENIFIGVCLQYSMNDDSDNKCFQFNFEEEYGKNQIRIIRMNHTEAKGPCYARALVQQQLFKGEKYYLQIDSHMRFVKDWDIEMINQLLQCKKPNDDNGGMVIDEKAILTCYPMGYKLPNLIPTHRFPILLVASGFGENDGFLRLGGKIVSKKLIEPCSSLFWVSGFSFSRSDIINSVPYDPNLQYLFFGEEISMSARLFTHGYNFYSPTKTLIFHLWNRDYRSTFRENNSLEIQKLEENSKKRLLILFNQNNNNINDNDDNNNNNNNNNNNNNNNNNNNNNNNNNNNN... | Function: Catalyzes the attachment of N-acetylglucosamine (GlcNAc) in alpha-linkage onto the 'hydroxyPro-143' residue of Skp1 (fpaA/fpaB). Is the first glycosyltransferase in the Skp1 HyPro modification pathway, which results in a pentasaccharide-linked 'HyPro-143'.
Catalytic Activity: trans-4-hydroxy-L-prolyl-[Skp1 pr... |
Q4HVS2 | MGEASSFVAVRLMRIIPILAILGATYYIFLTCFASFQATDVPVPEEWRNHDAVVDEVDEITETLTHDPDSRPTPHKLTIAEIEDLENKGEFMGFEDEDEIDVFINLDDDGDWEEDDLKKELGDELEGDFEDEEDEDFGDDDDDDDNDDDVDWSRFAYIQYVTNEDYLCNSVMIFEQLHRLGSKADRLLMYPKEMLEPDAAYSNKRGGQLLIRARDEYNVTLQPIEIQHRDGQDETWADSFTKLLAFNQTQYDRVLSLDSDSMVLQHMDELFQLPPCPVAMPRAYWLYNENPPKRILSSQVMLIQPDDVEFERIVQKMNSI... | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 52390
Sequence Length: 450
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q12096 | MRLISKRRIRFIVFILFGVLTVFVVSRLVVHFQYNQEIKFYKKYFQQRKDGLHEIYNPLEIKQIPKETIDDLYTARLDKELKNGEVIEWSKFAYVNYVTNADYLCNTLIIFNDLKQEFETKAKLVLLISKDLLDPNTSSNVAYISSLLNKIQAIDEDQVVIKLIDNIVKPKDTTPWNESLTKLLVFNQTEFDRVIYLDNDAILRSSLDELFFLPNYIKFAAPLTYWFLSNSDLEKSYHETRHREKQPINLQSYTKVLTKRIGKGQMIYNHLPSLPHSLYLNSNNIAQDIISSTSSLSPLFDFQSSKKVGKLKFASNLMVI... | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 57578
Sequence Length: 491
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q8N0V5 | MMGSWKHCLFSASLISALIFVFVYNTELWENKRFLRAALSNASLLAEACHQIFEGKVFYPTENALKTTLDEATCYEYMVRSHYVTETLSEEEAGFPLAYTVTIHKDFGTFERLFRAIYMPQNVYCVHLDQKATDAFKGAVKQLLSCFPNAFLASKKESVVYGGISRLQADLNCLEDLVASEVPWKYVINTCGQDFPLKTNREIVQYLKGFKGKNITPGVLPPDHAVGRTKYVHQELLNHKNSYVIKTTKLKTPPPHDMVIYFGTAYVALTRDFANFVLQDQLALDLLSWSKDTYSPDEHFWVTLNRIPGVPGSMPNASWT... | Function: Branching enzyme that converts linear into branched poly-N-acetyllactosaminoglycans. Introduces the blood group I antigen during embryonic development. It is closely associated with the development and maturation of erythroid cells.
Catalytic Activity: a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4... |
Q330M9 | MAEQEPKELLEMSTDTERLLEENDLRPLWEVEKDFGNQFGGFEADIWKWEDIQASIDAIERDVPIADLPPGFQRRVAVPVNTGYRNAISNTIYVGVQTVSPGETAPAHRHGANALRFTIDGSEDMKTVVAGEEFPMRDNDLITTPQWEWHDHVNDGDETAAWLDVLDLPLVLDSLNARNTFENHELDRQPVTKSQGYWESQYGRARPFEDTKEDGIPGPFEGNCAATPPYRFSWKDTLQTLRQRAENDDPDPHDGYSLSYVNPATGQPPLFPTMSFRAQLLQEETDPHFHNAVDAYFVIEGEGATHVGDDVLEWSERDIF... | Function: Catalyzes the oxygen-dependent ring fission of gentisate between the carboxyl and proximal hydroxyl groups at positions 1 and 2 of the aromatic ring to form maleylpyruvate. No activity with cathechol and protecatechuate as substrates. Part of a 3-hydroxybenzoic acid-degradation pathway.
Catalytic Activity: 2,... |
Q9SLE0 | MSAKNDVTGKVIAIMGVSGAGKSTIGKMLGKALSCDFLDADDFHSLSNRDKMRQGIALSDEDRMPWLEKIQESLRKRLLDGETVVLACSSLRKQYREILRGSDPDYKPGSYTSCKVTFVLLEGNAEVIAARLQKRASEEEHFMPLTLLQSQFDLLQADECEKIFKISVVLSPEVIVNTILEMVANSLNP | Function: Phosphorylates gluconate to 6-phosphogluconate.
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Mass (Da): 20969
Sequence Length: 189
Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
|
P12011 | MTSYMLGIDIGTTSTKAVLFSENGDVVQKESIGYPLYTPDISTAEQNPEEIFQAVIHTTARITKQHPEKRISFISFSSAMHSVIAIDENDKPLTPCITWADNRSEGWAHKIKEELNGHEVYKRTGTPIHPMAPLSKIAWITNERKEIASKAKKYIGIKEYIFKQLFNEYVIDYSLASATGMMNLKGLDWDEEALRIAGITPDHLSKLVPTTEIFQHCSPEIAIQMGIDPETPFVIGASDGVLSNLGVNAIKKGEIAVTIGTSGAIRTIIDKPQTDEKGRIFCYALTDKHWVIGGPVNNGGIVLRWIRDEFASSEIETATR... | Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Mass (Da): 57169
Sequence Length: 513
Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
|
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