ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8ZY16 | MDVALRIIPCLDIDGKAGVVVKGVNFQGIREVGDPVEMAVRYEEEGADEIAILDITAAPEGRATFIDSVKRVAEAVSIPVLVGGGVRSLEDATTLFRAGADKVSVNTAAVRNPQLVALLAREFGSQSTVVAIDAKWNGEYYEVYVKGGREATGLDAVKWAKEVEELGAGEILLTSIDRDGTGLGYDVELIRRVADSVRIPVIASGGAGRVEHFYEAAAAGADAVLAASLFHFRVLSIAQVKRYLKERGVEVRI | Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-b... |
P34048 | MTTAPFVSPSLPRLHSARASPFPKPSVGSGGGVAFPARTYGSSLRLRSAVMSASGVGGNGSPMAPEESTVSSRLGEVKRVTKETNVHVKINLDGTGVANSSTGIPFLDHMLDQLASHGLFDVYVKATGDTHIDDHHSNEDIALAIGTALLQALGDRKGINRFGHFTAPLDEAAVEVILDLSGRPHLSCGLSIPTERVGTYDTQLVEHFFQSLVNTSGMTLHIRQLAGNNSHHIIEATFKAFARALRQATEYDLRRQGTIPSSKGVLSRS | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 28632
Sequence Length: 269
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosp... |
W5AWH5 | MTTAPVVSPSLSRLHSAPASPFPKAPVGSGAGVAFPARPYGPSLRLRSAVMAASGVGGNGSPMAPEESAVSSRLGEVKRVTKETNVHVKINLDGTGVANSSTGIPFLDHMLDQLASHGLFDVYVKATGDTHIDDHHSNEDIALAIGTALLQALGDRKGINRFGHFTAPLDEAAVEVILDLSGRPHLSCGLSIPTERVGTYDTQLVEHFFQSLVNTSGMTLHIRQLAGNNSHHIIEATFKAFARALRQATEYDLRRRGTIPSSKGVLSRS | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 28501
Sequence Length: 269
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosp... |
A3DJF3 | MDRKFEVSRKTGETDITLSINIDGSGKSNISTGVGFFDHMLNLFAKHGLFDLDVKAKGDLEIDAHHTVEDVGIVLGQAIKQALGEKKSIRRYGSSFVPMDEALVLVALDLSGRPYLVFDAELKCEKLGNMETELVEEFFRAVAFNAGITLHVKALYGSNTHHIIEAMFKAFGRALDDATRKDDRIEGVMSTKGML | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21510
Sequence Length: 195
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
Q6F7A8 | MRNVSMTERIIEVVRNTNETKIRVRLNLDGSGQGTLNTGVPFLDHMIDQIKRHGLFDIDIHCDGDLEIDDHHTVEDCGITLGQAFAQALGDKKGLRRYGHFYAPLDESLSRVVVDLSGRPGLFMDIPFTRARIGSFDVDLFSEFFQGFVNHALMTLHIDNLKGKNSHHQIESVFKAFARALRMACEIDPRAAGSIASTKGSL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 22539
Sequence Length: 202
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
A0LTS3 | MDPTASGRQAPRNPRQATVQRETKETSVSVALVVDGTGTVDIDTGVPFYDHMLAQLGKHAGFDLTVVTRGDLDVDAHHTVEDTALALGQAFREALGDKAGIRRFGDALVPLDEALCQVAVDLSGRPYLVHSEPEMVELIGTYETTLTRHVWESFVAQAHICLHIQVLAGRNAHHINEVQFKAVARALRDAVRLDGVAGVPSTKGAL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 22205
Sequence Length: 206
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
Q9RX91 | MPRTAAVTRTTKETDITVRLDLDAAPYEQPATGHGFFDHMLDALARHSRLGISISGTGDLHIEPHHLIEDTGITLGQALSQALGDRKGIERYGSAFVPMDETLAHVVLDLSGRAHLAFEPETLDVYGDAGGMTHYHLREFLRGFCNHAGATLHVRLLAGREAHHVIEAVMKAFARALRDAVAVTSDALPSTKGSL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21093
Sequence Length: 195
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
Q6ANL7 | MVVIEKNRKSAISRKTTETDIQLELNLDGAGQHLIDTGVPFLNHMLTLFSVHGFLDLSLRAEGDIDIDDHHTTEDIGIVLGQAIAQALGNKGGISRYASVYLPMDEALVRIVIDLSNRPYLHYNAPVIEQKLGTFDSCLVKEFFRAVSQQAGMTLHIDMIHGENGHHIVEAIFKGFGRALSLAIEPLGTDGALSSKGCL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21718
Sequence Length: 199
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
A1VEV3 | MQTVARKASVERVTNETTIALTLTIEGEGNVRVTTGFGMLDHMLTLTAFWAGFDLDLTCNGDMHIDAHHTAEDVALCLGQALATALDDRKGIARVGFARVPMDEALAEVTLDISGRPWLEWRGDEYLPPVIAGEEKDLWREFHKAFASAARMNLHVSYLYGKNGHHLLESASKGLGLALRQAVRRDRQTVLSTKGSLD | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21787
Sequence Length: 198
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
B8E2C5 | MRKSEIERETKETYVKILLNLDGSGSFLGDFPVPYYKHLFSAFCFYAEWDVEIMAKGDVEVDPHHLIEDTGIVWGKAFYSAVSNSNFLRFSSKIVPMDEALVMAVVDISGRPYLEIRDDKGILNGRLIKEFLRGFVNNSQITLHIWLLSGENLHHIEEAIFKALGLALGEASKEVPNLKSTKGKIW | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21094
Sequence Length: 186
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
Q9S5G5 | MSQKYLFIDRDGTLISEPPSDFQVDRFDKLAFEPGVIPQLLKLQKAGYKLVMITNQDGLGTQSFPQADFDGPHNLMMQIFTSQGVQFDEVLICPHLPADECDCRKPKVKLVERYLAEQAMDRANSYVIGDRATDIQLAENMGINGLRYDRETLNWPMIGEQLTRRDRYAHVVRNTKETQIDVQVWLDREGGSKINTGVGFFDHMLDQIATHGGFRMEINVKGDLYIDDHHTVEDTGLALGEALKIALGDKRGICRFGFVLPMDECLARCALDISGRPHLEYKAEFTYQRVGDLSTEMIEHFFRSLSYTMGVTLHLKTKGK... | Cofactor: Binds 2 Mg(2+) ions. Can also use Co(2+) and Mn(2+)ions.
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 40290
Sequence Length: 355
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alp... |
B1H0E9 | MKQRKAKITRKTKETNIVVEINLDNILLPSVSTTIGFLDHMLELFAVHSGIGFKIKASGDTHIDDHHLVEDAGITIGQALKEAVGDKKGIVRYGHFLLPMDETLSYVALDLAGRFYLSYEADIKFQKNGFNYDLIQEFFYALASNAGITLHIKMIKGRNNHHIAESIFKAFGRALRQAVSYSKSKKTVPSTKGIL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21781
Sequence Length: 195
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
A5VX72 | MVERKASVERNTLETQVKCSINLDGSGKARFDIGVPFLEHMLDQIARHGLIDLDIECKGDTHIDDHHTVEDVGITLGMAFAQAIGDKKGIFRYGHAYVPLDEALSRVVIDFSGRPGLQMHVPYTRASVGGFDVDLFQEFFQGFVNHALVTLHIDNLRGHNTHHQIETVFKAFGRALRMAITLDERMAGQMPSTKGCL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21943
Sequence Length: 197
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
Q8ZY15 | MPYVRKTLETEVAVELRRGGDLAVETPIPFLTHMLETLLKYAGLGGVVKAVELRKLDDGHHVIEDVAIAVGRALDALLEDRRGIARFGHAVVPMDESIVMAAVDLGGRAYWVVRAKLPDVTIGGYPLRMFPHFVRTLAVEAKATIHIYARGTDPHHKVEAAHKALGLALRQALSPGEGLSTKGVLG | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 20123
Sequence Length: 186
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
Q39CT7 | MSRYWSDIVQQLVPYVPGEQPALAHPVKLNTNENPYPPSPRVVAAIARELGETGDTLRRYPDPVARALRETVATHHRIKPEQVFVGNGSDEVLAHTFQALLKHDRPLRFPDITYSFYPTYARLYGVQTSNVPLADDFSIRVDDYLDDAGGVLFPNPNAPTGRALPLADVERIVAANPSSVVVIDEAYVDFGAQSAITLIDRYPNLLVVHTTSKARSLAGMRVGFAFGEAALIDALNRVKDSFNSYPLDRLAQVAAQAAYEDTDYFNATCRRVIDSRTRLTHALDALDFNIVPSAANFVFARHPAHDAGAIAAKLKEREIF... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39281
Sequence Length: 355
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q62FC0 | MSRYWSDIVRQLEPYVPGEQPALAHPVKLNTNENPYPPSPRALDAIRRELGDTGEALRRYPDPVARRLRETVAAYHGIAPEQVFAGNGSDEVLAHAFQALLQHDRPLRFPDITYSFYPTYARLYRVAYETVPLAGDFSIVVDDYLDDAGCVLFPNPNAPTGRALPLADIERIVAANPSSVVVIDEAYVDFGAESAVSLIARYPNLLVVHTVSKARSLAGMRVGFAFGDAALIDALTRVKDSFNSYPLDRLAQVATQASYEDEAWFQATRKQVIASRERLVGALAALGFDVVPSAANFVFARPRSHDAATLAAQLKQREIF... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39228
Sequence Length: 356
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q3AAT6 | MVRKALENLKPYVPGKPVEEVERELGITNIDKLASNENLWGISPKVAAAIKEAVDKVNYYPDGGAFRLKEKIAAKYGVTPDNIILGNGSDELVMFLAMALIDPGDEAIMPVPSFPRYEPVVTMMNGIAREIPLKEHRLDLKTMAEAVNEKTRLVYLCNPNNPTGTYITKGELEEFLERVPEEVVVVLDEAYFEFARLFNDYPDGLNFFKKRPNTVVLRTFSKAYGLAGLRVGYGFAPENLAKAINSLRPPFNVNFLAQMAAVAALDDEEYVREVVKNTDEGKKFLYQEIIRMGLSYIPSAANFLMIKTEKPSALVFRELL... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 40662
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q9A5B6 | MERGRMLVLDRKPLTPAWASPMRQALEGVQGYKAGMTLAEAARRTGLSAFSKLASNENLLGPSPKVAEAVMAAMAEPHIYPDPHSDVLRAAIGARLGVSPARVVVSPGSEALIDYVFRAVLHPGDSILLSSPTFPTYEIFGRCAEARIIDVPRLANFDIDVPAVCAAAALGPKLLVLCTPNNPTGNALKAADFQAILAATPRSTVVFVDEAYREYHEAFDTFAMLDAWGGPWVSARTFSKAYGLAGLRMGYGVASSPELVDYLDRIRPPFNVTAVSQAAALAAWEDQDYLKRTVDLTIAERGRVEAVLDDMGVEHTESHA... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 40386
Sequence Length: 378
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q46WL3 | MSVVDPSLIERIIRDDVRAMGAYHVPDSHGLVKLDAMENPYRLPPALRSELAARLGEVALNRYPVPSSEALRAKLKEVMQVPAGMEVLLGNGSDEIISMLALAAARPGAKVMAPVPGFVMYAMSAQFAGLEFVGVPLRADFTLDRGAMLAAMAEHQPAIVYLAYPNNPTGNLFDAADMEAIVRAAQGSVCRSLVVVDEAYQPFAQESWMSRLTDFGNLLVMRTVSKLGLAGIRLGYVAGDPQWLEQLDKVRPPYNVNVLTEATALFALEHVAVLDEQAAQLRAERSRVAEGMAAHGGVTVFPSAANFLLARVPDAAQTFD... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39607
Sequence Length: 366
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q31GD4 | MSQSLFCDEVLPHISDIQVYQPGKPISEVQREHNLLRISKLASNENPLGASPKAIKAVQSELINMGRYPDGNSFYLKQDLADFLQKQPTEIALGNGSNELLELVARIFAGKGDEIIYSQYAFAVYSISTQAVGATGIEVPAKEWGHDLEAMAEAITDKTKLIYLANPNNPTGTLFTQKEWEAFISKVPSNVIVVLDEAYTEYVTHDEYANGLNYLEQYPNLIVSRTFSKAYGLAALRIGYMVANEELIAYINRLRAPFNINHLAQVAAKAALKDPMFVKKTVDLNTQGMQTLTQFFEEKGLSYIPSQGNFVCVDLGPDSL... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 41389
Sequence Length: 373
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q5ZU10 | MSIDFQQLPHAGIRSLIPYVPGKSIEELAKEKGITDIIKLASNENPLGCSPLALSVIQTMSSHYIATYPSPWNHPLMSKLASYLKVKPEQLFLSNGSDYLFNILLNCFALHTDRHILTHDYAFSTYAIQANSLQIPINSVPIGHNWEVNITDIVNACNQQTGIIFIANPNNPTGVLIQQEEIKYLLEQIPKSTLLVLDEAYYEFAASQLTVNSLDWLEEHPNLVVTRTFSKIYGMAGLRLGYAIANPSIINILKRVQLPFIVNQVALAAAYAAIDDDDFIQSSLKMNNEGMLQLQAGFNELNIKYLPSSCNFLTFDCEED... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 41489
Sequence Length: 369
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q608S3 | MSITTLAVPGVRGLTPYQPGKPIGELEREFALKRIVKLASNENPLGASPKVLEVVRRILGGTHLYPDGSGFELKAALAEKLGVEPAQIVLGNGSNDVLDLVARAFLTAGRNAVYSEYAFAVYPIATQTAGATGKTAPAHDGSRGPRFGHDLETMLERVDPDTRVVFIANPNNPTGTLLGRGELYSFLAALPEHVIAVVDEAYFEYARRPDHPDALEWLGEFPGLIVTRTFSKAYGLAGLRVGYAVTGVEIADLLNRARQPFNVNTLGLAAAAAALEDTGFLEATVQANDAGRSQLEAGFRERGFDFIPSAGNFVSFDLGR... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39708
Sequence Length: 371
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
P55683 | MERTMSDAKLQRVLSSLTEVYRQLNSLPSSQPSDAGYVKLDTNENPFALPKAVMQSAVAALERQYLYPEDDNISLREAAAASYDLSADQVIAGNGSSELLSLIYKAFLGPGDSVAMLSPGFAYNRKLAQLQGARLLEIKWGESSLLPIHELLFGPAKQAKFILLANPNNPTGTFVPIADIESLVALSDQLVVLDEAYVDFAPDSALRLVNRYSNLLLLRTFSKSYAAAGIRVGFGFGHPEVIGRLRNIQNMFNMNVIGHAVGVSILAHRATYNENHRHIRHERERVRVALSRLGFSVTPSHANFLLARVPAGRDGVWWHA... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 40421
Sequence Length: 368
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q3AD53 | MKLILNKEELLDKYSRRKAVEEDIEQQVRKILNEVASSGDEALIEYAREFDGFKGDLSNLKVSEEEIDKAYREVDDGFLNSLRKAIQRVFDFHQKQLPRSWFTTEENGNILGQIYTPVEVAGIYVPGGTAAYPSSVVMNAVPAKVAGVKRIVMVSPQKGERMNPYVLVAAREAGVTEIYRVGGAHAIAALAFGTKTIPRVDVITGPGNIYVTIAKKLVYGTVNIDMLAGPSEVVVIADSSAKPEYLAADMLSQAEHDSLASGVVITWDGELARKTAQKVEEYLKLLPRREIILKALENCGGIVVVDDEEEALQLANQLAP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 46608
Sequence Length: 425
Pathway: Amino-acid biosynth... |
Q9A5V1 | MRRFLFSDPDFQTAFKAFLDERRGSPADVDAAVAGVLEAVRTQGIEALLDYSRRFDKVDLTAETIRVTAEEIEAGAAETPADVREAIAFAAARIRAYHSRQRPADQAWTDEAGVELGWRWTPLEAVGVYVPGGRAAYPSTVLMNAVPAQVAGVDRIAMVTPPGKLQPAVLAAAKEAGVTEIWRVGGAQAVAALAYGAGPIQPVDKIVGPGNAYVTAAKRRLYGVVGIDALAGPSEIVVVADNKNNPDWIAADLLSQAEHDPAAQSILITDDEAFAAAVEQAIAERLKTLATGEDAAASWRDHGAVIIAPLDESPALVDAI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 45154
Sequence Length: 428
Pathway: Amino-acid biosynth... |
Q3J079 | MPQFLDTRRPGFEADFTALLGMKREDSPDVDAVVAGIIADVRARGDAAVIELTARFDRLELTPERLAFSEAEIEAEIATVSAEDRAALELAAERIRAYHARQMPENARWTDAAGAELGWRWGPIASAGLYVPGGLASYPSSVLMNAIPARVAGVERLVVACPTPGGVVNPLVLLAARLAGVDAVYRIGGAQAVAALAYGTETIRPVDKITGPGNAYVAAAKRRVFGRVGIDMIAGPSEILVIAEGAVDPDWIALDLLSQAEHDESAQSILVTPDEALGRAVVQAVEARLETLERRAIAGASWRDYGAVIVTRDLEEAAAL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 45962
Sequence Length: 434
Pathway: Amino-acid biosynth... |
Q3B5E3 | MSPVHYRTSTSTIVAVLKLYRFLDDRDALFRQIGRSVDFDPEVQRAVTDILEAVRLRGDMAVLEYTERFQGAVLTSMQVPEEDILRAREEADPAFIRVLEEAWENILRFHRHEVENSFFYEGEGGVVLGQRVTPMDRAMLYVPGGKASYPSSVLMNAAPARVAGVGEIFMTTPCDASGAVSPHILAAASVAGVTSVYRLGGAQAVAAFAYGTQTIPKVDIITGPGNKYVALAKKQVFGHVAIDSIAGPSEVVVVADDDADAEFITMDLFAQAEHDPDASSVLITPSMRLAEEVRDLAAARVGSMLRGEVIAEALSNNGAI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 48062
Sequence Length: 443
Pathway: Amino-acid biosynth... |
Q8NNT5 | MLNVTDLRGQTPSKSDIRRALPRGGTDVWSVLPIVQPVVEDVQNRGAEAALDYGEKFDHIRPASVRVPAEVIAAAENTLDPLVRESIEESIRRVRKVHAEQKPSEHTTELSPGGTVTERFMPIDRVGLYVPGGNAVYPSSVIMNTVPAQEAGVNSLVVASPPQAEHGGWPHPTILAACSILGVDEVWAVGGGQAVALLAYGDDAAGLEPVDMITGPGNIFVTAAKRLVRGVVGTDSEAGPTEIAVLADASANAVNVAYDLISQAEHDVMAASVLITDSEQLAKDVNREIEARYSITRNAERVAEALRGAQSGIVLVDDIS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 46771
Sequence Length: 442
Pathway: Amino-acid biosynth... |
Q3Z878 | MEIIRGFAPAEKRLSRRDKAGFFLDETQRAELAKRLGVDPEKAVNGIIDDIRKQGDKAVLEYTLKFDRAAISKLEVSPAEIKQAAGEIPAELFEALKLAATQVRAYHHFQKEAVWKAAEIMQGKQLIRPLERVGLYVPGGKAFYPSTVLMTAIPAKEAGVDEIILVTPPGADGKIPAPTLAAAYIAGVDKVFACGGAQAVAALAFGTKSIPKVDKICGPGNIFVTLAKKAVFGVVDIDGLQGPSEVLILADQYANAEYCASDILAQAEHDVLASPIMVTTSAELAKRVNDIVETKAGSCARKDIIRQSLRDNGLIAVVDN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 46836
Sequence Length: 436
Pathway: Amino-acid biosynth... |
Q81G08 | MTKWKRANPNGTRDYLFEECTLIEEVEQKLRLTFLERGYEEIRTPTIEFYDVFAFQNRPIDEEKMYKFFDEKGRIIVLRPDMTIPLARVIGTQRWDTPLKVTYSGNVFRANESHSGKYNEIVQSGIEVIGIDNVRAEIECVISVIQALQKLKVQSFTIEIGQVQLYKCIVKKLSIQDEEERVLRTYIESKNYAALSNFIGEKKLDRCDETVRLLEKLPRLFGNLEVIEEAEKLASSNEMKMAIARVKEMYETIEMLGYGSYISIDLGMIQHLDYYTGVIFKGYIYEIGEEIVSGGRYDELIGNFGEMLPAVGLAVQVNQI... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 48859
Sequence Length: 420
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
O34459 | MFMFEKPHGMRDTLPGLYETKKKVRRSLTDLIDKWGYQFMETPTLEFYDTVGVQSAIEEQQLFKLLDQDGKTLVLRPDMTGPIARVAASKLLKHGHPLRVGYAANVFRAQEREGGRPAEFEQVGVELIGDGTTSADAEVIALVVGALKNAGLASFKIAIGHAGIADALFVEVLGNVERADVLRRFLYEKNYVGYREHVKSLPLSSIDKSRLLELLELRGGIEVCGRAEEIVDSAQGKSVVDELKALWDILEDYGCTENVRLDLNMVSHMSYYTGILFEVYAENVGFVIGSGGRYNKLLGHFDSPAPATGFGLRIDRLIEA... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity).
Sequence Mass (Da): 43505
Sequence Length: 391
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose ... |
Q7VWM0 | MGNWLLPEGLADVLPAEARRIEELRRELLDLYRTYGFELVAPPLVEYIDSLLSSTGSDLNLRTCKLVDQLSGRTLGVRADMTSQVTRIDAHLLNRAGVTRLCYCGSVLHARPADLLSSRELLQIGAEIYGHAGFEADLEIIQLVMDTLATAGVRNARLDLCHSGVMRAIFDADPQASRHAGDLCTLLREKDVPGLAELASRVDGLGEDTVRALQALATLYGGPEIIARARRELPAVPGMAQALDALQALVDAMPGVTLSVDLADVGGYGYHSGVTFAVYGEDWHDALVRGGRYDDVSCAFGRARPATGFSLDLRKLAAGL... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 41627
Sequence Length: 385
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
Q2YIH8 | MTMVGSRTSPIFNALRVELNAREAELVEIPLIQPADPFLDMAGEDLRRRIFLTENENGDSLCLRPEFTIPVCRNHIALNAATPKRYAYLGEVFRQRRDGAAEFLQAGIEDLGAADEAASDARSLADALSCVKAIAPDAPLEIVLGDQSVFAGMLKALGLPQGWRKKLLRSFGDAHSMDLALAELTGTQRRDPLPESLAVLVAEGDEIGLARMLEAEMLEAGISPGAGRTPVEIARRLIEKEDLAATHFPAAALDLLRQFLAIRVSLDMAAVTLRAFAADNALDLGAVLQKFEARADAIAQAGIEMKDIIYDASFGRPLDY... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 40921
Sequence Length: 378
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
C4LYI2 | MADSCIFCKIAQKQIPSTIVYEDDEIFAFKDINPIAPIHILVIPKQHIASLNEITEENEAFIGKVLYKVSLIGKKECPEGYRVVNNIGEDAGQTVKHIHFHILGGKKLAWDKL | Function: Hydrolyzes purine nucleotide phosphoramidates with a single phosphate group, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl... |
Q21882 | MNKFSLFFALTATLMTITESAVPTASISAHVLDISGGSPAGGVQILAYIQQNDDWTKIGSEFTQDNGRVDWVSPDFTLIPGTYRLVYITEPYYKAKNVESFYPYVEVVFNIRDATQHYHVPLTLSPWGYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 15129
Sequence Length: 135
EC: 3.5.2.17
|
Q92VB9 | MQVQDGTPGRLTTHVLDTASGRPASNLRIDLYRIEGERPELLSSTRTNDDGRCDAPLLNGSTMETGTYELRFHAGEYLGTAAERGANPFLDVIPIRFGIADRAAHYHVPLLLSPYGYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 13512
Sequence Length: 123
EC: 3.5.2.17
|
Q92UG5 | MSKSGRLTTHVLDTALGRPAHGLKIDLYRLEGDARHLIRTVHTNSDGRVDGPLMEGAGFATGTYELVFHAGDYFRSAGVKLPDPAFLELVPLRFGIADADSHYHVPLLLSPYGYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 13114
Sequence Length: 120
EC: 3.5.2.17
|
O32142 | MGKLTTHILDLTCGKPAANVKIGLKRLGESIMKEVYTNNDGRVDVPLLAGEELMSGEYVMEFHAGDYFASKNMNAADQPFLTIVTVRFQLADPDAHYHIPLLLSPFGYQVYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 12635
Sequence Length: 114
Pathway: Purine metabolism; urate deg... |
Q8YFU1 | MGKLSTHVLDTAHGTPAAAMRVELYRIAASGTPELLKRVVTNLDGRTDAPLLSGDEMRTGIYELQFHVAEYFEGRGAELAHEPFLDLIPIRFGIADEDGNYHVPLLVSPWSYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 13033
Sequence Length: 118
EC: 3.5.2.17
|
Q9A545 | MSGLTTHILDQASGKPAAGVGVRVSRRDGEQTQWLAELRTDADGRARLVAGEDLAVGGYRLEFAIGDHFKASGLPVSDPPFLDVVVIDFAVSNLDQHWHVPLLVSPYGYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 12394
Sequence Length: 115
EC: 3.5.2.17
|
Q06S87 | MNRLQHIRGHIVSADKHINMSATLLSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTGITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCFYPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 15486
Sequence Length: 138
Pathway: Purine metabolism; urate deg... |
Q9RV69 | MSGHPGLTTHVLDTARGKPAAGVRVQLCRVTGDTRTPVTEAVTNSDGRTDAPLIERGSLKQGTYELTFHVADYFKGFVAAADPPFLDVVTLRFTVGDTSGHYHVPLVMTPWSYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 12868
Sequence Length: 119
Pathway: Purine metabolism; urate deg... |
P76341 | MLKRYLVLSVATAAFSLPSLVNAAQQNILSVHILNQQTGKPAADVTVTLEKKADNGWLQLNTAKTDKDGRIKALWPEQTATTGDYRVVFKTGDYFKKQNLESFFPEIPVEFHINKVNEHYHVPLLLSQYGYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 15460
Sequence Length: 137
Subcellular Location: Periplasm
EC: 3... |
Q9KET9 | MSGKVTTHVLDTSCGKPAAGVVVELWRIVEGGESELLTKAVTNQDGRLDKPLLTENKMARGVYELRFQVGDYFLRNGFVNQAYPFLHVIPVRFGLEDVNEHYHVPLLVAPGGYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 13209
Sequence Length: 119
Pathway: Purine metabolism; urate deg... |
Q9CRB3 | MATESSPLTTHVLDTASGLPAQGLCLRLSRLEAPCQQWMELRTSYTNLDGRCPGLLTPSQIKPGTYKLFFDTERYWKERGQESFYPYVEVVFTITKETQKFHVPLLLSPWSYTTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 13559
Sequence Length: 118
Pathway: Purine metabolism; urate deg... |
Q8XXJ7 | MGRLTTHVLDTAAGTPGKDLAITLFKIVNNLRQPIKTVRTNHDGRCEAPLLEGEALQAGIYELDFAVGDYYRAAGVSLPDPAFLDVVTLRFGVADAGAHYHVPLLVSPWSYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 12673
Sequence Length: 117
EC: 3.5.2.17
|
Q98CI7 | MAETSKADGGRLTTHVLDTATGKPAAGLSIALYRLDGSARTHLKTVATNADGRCDAALLAGAEFRAGEYELVFAAGDYLRGQGTKLPEPAFLDSVPIRFGMAEAVHYHVPLLISPYGYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 13119
Sequence Length: 124
EC: 3.5.2.17
|
Q4VYA5 | MKRHILATVIASLVAAPAMALAAGNNILSVHILDQQTGKPAPGVEVVLEQKKDNGWTQLNTGHTDQDGRIKALWPEKAAAPGDYRVIFKTGQYFESKKLDTFFPEIPVEFHISKTNEHYHVPLLLSQYGYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Mass (Da): 15105
Sequence Length: 136
Subcellular Location: Periplasm
EC: 3... |
Q3J7X9 | MIIVTGGAGFIGSNIIKALNQGGREDILVVDDLTQGEKFSNLIDCEIWDYWDKQPFLQAIKAGEEFPHPVDAFIHQGACSATTEWNGRYMMENNFYYSKRLLHYCLERRIPFLYASSAAVYGCGLTFQEHREFEAPRNVYGYSKWLFDQYVRRYLPTASSQIVGLRYFNIYGPREAHKGAMASVAYHAHCQLKETGRIKLFEGCDGYEHGEQRRDFVSVADAAAVNLWFLEHPNQSGIFNVGTGQAQTFNEVAQAVLAFHGHGEIEYIPFPDHLRGRYQSFTQADIHALREAGYAEPFALVEKGVKTYLDWLGKNQD | Cofactor: Binds 1 NADP(+) per subunit.
Function: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Catalytic Activity: ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose
Sequence Mass (Da)... |
Q9HUG9 | MKLSMPRFDQAPVLVVGDVMLDRYWHGATSRISPEAPVPVVRVEQHEDRPGGAANVALNIAALGAQALLVGVTGRDEAADSLANSLKAAGVDARFQRIDSQPTIVKLRVMSRHQQLLRVDFEEPFRTDAAALAVDVESLLAKVKVLVLSDYGKGALQNHQVLIQAARARNIPVLADPKGKDFAIYRGASLITPNLSEFETIVGRCADEAELVAKGQALMSELDLGALLVTRGEHGMTLLRHGQPALHLPARAREVFDVTGAGDTVISTLAAALAAGEELPSAVGLANLAAGIVVGKLGTAAISAPELRRAVQREQGSERG... | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da)... |
Q4KJA9 | MKLSMPRFDQAPVLVVGDVMLDRYWHGGTSRISPEAPVPVVKVEQIEDRPGGAANVALNIAALGAPASLVGVTGDDEAADSLANSLQGAGVRALFQRIKHQPTIVKLRVMSRHQQLLRIDFEEPFATDALALAAEVDALLDGIKVLVLSDYGKGALRNHQVLIAAARARGIPVLADPKGKDFSIYRGASLITPNLSEFETIVGGCADEHELVSKGAQLMHDLELGALLVTRGEHGMTLLRPDHPAMHLPARAREVFDVTGAGDTVISTLAAAIAAGEELPHAVGLANLAAGIVVGKLGTAAISAPELRRAIQREEGSERG... | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da)... |
Q3IHX7 | MDLSLLKNLSAARILVVGDVMLDRYWYGDSGRISPEAPVPVVKVSKLEDKAGGAANVAKNIARLDGKVGLLGLIGEDEGGQILEGILEGEKINSQLVSVCDLPTISKMRVISRHQQVVRLDLEETFTEQHSQLLLNRLELVLDEYDFIVFSDYNKGSLSLIENMISLAKKAGKTVLVDPKSSDLHLYRGADYITPNLNEFKLAGGQTDSEEGLATSARKLISDAGIKAMLLTRSEQGMSLISATEKYDFAAQELEVSDVTGAGDTVIATLAVMLGAGMTPKNAVEIANLAAGIAVSKLGAATVSPEELSRKLGQYLHATG... | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da)... |
Q98I54 | MIKHNPPSPEPLHRAIARFGGVTVLVVGDLILDRFVNGVIERISPEAPIPVLHGRGETSAMGGAGNVVANIVSLGARAIPVSVIGTDTAGDSLVRMLAELGAETAGLSQQRGRMTSSKSRFSALNQQVLRFDEEEIKPLDETERAGLIRHFRAALAGAEIVILSDYGKGILLDGVAAELIAICREAGKPVLVDPKGRDYARYAGATAITPNRKELGEAVGHAVFADDEIVAAARELISAHGFDFVVATRSEKGMSVVGPDEARHIATQAREVFDVSGAGDTVIATFALALASGADPVAAASIANAAGGVVVGKRGTARLT... | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da)... |
P09983 | MPTITAAQIKSTLQSAKQSAANKLHSAGQSTKDALKKAAEQTRNAGNRLILLIPKDYKGQGSSLNDLVRTADELGIEVQYDEKNGTAITKQVFGTAEKLIGLTERGVTIFAPQLDKLLQKYQKAGNKLGGSAENIGDNLGKAGSVLSTFQNFLGTALSSMKIDELIKKQKSGGNVSSSELAKASIELINQLVDTAASLNNVNSFSQQLNKLGSVLSNTKHLNGVGNKLQNLPNLDNIGAGLDTVSGILSAISASFILSNADADTGTKAAAGVELTTKVLGNVGKGISQYIIAQRAAQGLSTSAAAAGLIASVVTLAISPL... | Function: Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by forming a pore.
PTM: Myristoylated by HlyC; the toxin only becomes active when modified . Mainly myristoylated, while a minor fraction is acylated with pentadecanoyl (C15:0; 26%) and heptadecanoyl (C17:0; 6%) fatty a... |
Q44066 | MASALSPGSRVLIALIRVYQRLISPLLGPHCRFTPTCSSYGIEALRRFGVIKGSWLTVKRVLKCHPLHPGGDDPVPPGPFDTREH | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 9345
Sequence Length: 85
Subcellular Location: Cell membrane
|
P09545 | MPKLNRCAIAIFTILSAISSPTLLANINEPSGEAADIISQVADSHAIKYYNAADWQAEDNALPSLAELRDLVINQQKRVLVDFSQISDAEGQAEMQAQFRKAYGVGFANQFIVITEHKGELLFTPFDQAEEVDPQLLEAPRTARLLARSGFASPAPANSETNTLPHVAFYISVNRAISDEECTFNNSWLWKNEKGSRPFCKDANISLIYRVNLERSLQYGIVGSATPDAKIVRISLDDDSTGAGIHLNDQLGYRQFGASYTTLDAYFREWSTDAIAQDYRFVFNASNNKAQILKTFPVDNINEKFERKEVSGFELGVTGG... | Function: Bacterial hemolysin that causes cytolysis by forming heptameric pores in target host membranes.
PTM: Proteolytical cleavage is required to convert the 80 kDa hemolysin precursor into the active 65 kDa hemolysin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81962
Sequence Length: 741
Doma... |
Q41438 | MDVRRRPVKPLYPSEHISSGEPLKPHNQDSSVKASDALPLPLYLTNGLFFTMFFSVMYFLLHRWREKIRNGIPLHVLNFSELVAMVSLIASVIYLLGFFGIGFVQSFVSKGNNDSWDVEDESPEQFIDRTVTPPPVRRNIPMKSVPVAEKTAQIITPFSSEDDEVVIKSVVEGRIPSYSLESKLGDCKRAAFIRKEALQRSSGKSLEGLPLDGFDYESILGQCCEMPIGYIQIPVGIAGPLLLNGKEFSVPMATTEGCLVASTNRGCKAIYVSGGATSVLFRDAMTRAPVVRFGSAKRAAELKFFVEDPMNFETLSVVFN... | Function: Catalyzes the synthesis of mevalonate. The specific precursor of all isoprenoid compounds present in plants.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62159
Sequence Length: 574... |
Q9YAS4 | MGSSSGQKPRRLEDLVDKLASGSLSHSRLEKELGNANEAALVRRLYLERLTGASLSSVASTILDFQELYGRNIENPIGAVQVPVGVAGPLRINGDYARGDFYIPLATTEGALVASVNRGAKAITLSGGARAKVIKDGMTRAPLLWTPSVYEAHRLAMWVEDRIEDLRSVVAGVTRHGRLQHIYPYIIGNLVWLRLSFSTGDAMGMNMVTISSDRICRYIEENYDGDAKCIALSGNMCTDKKPAAINKILGRGKYVVAEAVIKGEVVKNVLKTTPQNINLVNVTKNLLGSAAAGSHSFNAHFANIIAAIFIATGQDAAQVV... | Function: Converts HMG-CoA to mevalonate.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
Sequence Mass (Da): 44625
Sequence Length: 421
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
EC: 1.... |
O76819 | MKVWGAHGEFCARHQWEVIVATLALLACAASVERNGPGNRSEHCAGWARACPGLEAEYQAADAVIMTFVRCAALLYAYYQISNLHKIASKYLLIIAGVFSTFASFIFTSAVASLFWSELASIKDAPFLFLLVADVARGARMAKAGWSAGEDQGKRVGRALALLGPTATLDTLLAVLLVGVGALSGVPRLEHMCTFACLALLVDYLVFVTFYPACLSLVADFASGRKEMSPDSPFSEADLKPNPVVQRVKMIMAAGLLCVHLTSRWPWSSDNGIIEGPTDTLTPTSNDNILLHSYVKWFSVSADYIVIATLLCALIIKFVF... | Function: Synthesis of mevalonate for the production of non-sterol isoprenoids, which are essential for growth differentiation.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89790
Sequence Le... |
O28538 | MQVLRLDRRHYKSGKIRRAMSSRIPGFYKLSVEERLKKVAEFAGLSDEEVKAVLSQGLPLDVADRMIENVIGTFELPLGIATNFLIDGKDYLIPMAIEEPSVVAAASNAARMARESGGFTTDYTGSLMIGQIQVTKLLNPNAAKFEVLRQKDEIIERANECDPMLVNLGGGCKDIEARVIDTIMGKMLIVHLIVDVKDAMGANAVNTMCEKVAPFIERITGGKVYLRIISNLAAYRLARAKAVFDKDVIGGEEVVEGIMLAYAFAAADPFRCATHNKGIMNGISALMIATGNDFRAIEAGAHSYAAIGGYKPLTTYEVDR... | Function: Converts HMG-CoA to mevalonate.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
Sequence Mass (Da): 47146
Sequence Length: 436
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
EC: 1.... |
P54960 | MVGRLFRAHGQFCASHPWEVIVATLTLTVCMLTVDQRPLGLPPGWGHNCITLEEYNAADMIVMTLIRCVAVLYSYYQFCHLQKLGSKYILGIAGLFTVFSSFVFSSSVINFLGSDVSDLKDALFFFLLLIDLSKATVLAQFALSSRSQDEVKHNIARGIAMLGPTITLDTVVETLVIGVGMLSGVRRLEVLCCFACMSVIVNYVVFMTFYPACLSLILELSRSGESGRPAWHDKSLIIKALHEEDQKPNPVVQRVKVIMSAGLMLVHAHRWVRCLSIALWPDLTSLRYFCTHCDTGVSYSRWSFASEGEELPTVKLVTGD... | Function: Synthesis of mevalonate for the production of non-sterol isoprenoids, which are essential for growth differentiation.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93157
Sequence Le... |
O51628 | MNLESLSSFMELSKNFRHKSVLEKRQEIKSFLELSYKDFFYNNANEDFLFNMIENYIGYLSFPIGIVKNLKINGKYYSLPIATEESSVVAALNFAAKILENADLRYSLGEVLGISQIYIKSEKDLSKIFVDLGDKIKTWIEPLLTNMNQRGGGFRRLSTRHIKELGIQKLNIYVDTCDAMGANLLNSIAERVAEFIFLEFGYECVLKVLSNDISEFTAKARFVLDFKHLLPGKEDSWNLAKKIELISSIGFYEEERAVTNNKGIMNGITGVCLATFNDTRALEASVHKFASKSGKYFPLSKFYTTDNALVGEIEIPLQVG... | Function: Converts HMG-CoA to mevalonate.
Catalytic Activity: (R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH
Sequence Mass (Da): 48922
Sequence Length: 431
Pathway: Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonat... |
P14773 | MIGRLFRAHGEFCASHPWEVIVALLTITACMLTVDKNNTLDASSGLGTATASAAAAGGSGSGAGSGASGTIPPSSMGGSATSSRHRPCHGWSQSCDGLEAEYNAADVILMTIVRCTAVLYCYYQFCSLHRLGSKYVLGIAGLFTVFSSFIFTTAIIKFLGSDISELKDALFFLLLVIDLSNSGRLAQLALSGSNQAEVTQNIARGLELLGPAISLDTIVEVLLVGVGTLSGVQRLEVLCMFAVLSVLVNYVVFMTFYPACLSLIFDLSRSGVDMSVVREKAKGSLLLKSLTEEEQKANPVLQRVKLIMTTGLMAVHIYSR... | Function: Synthesis of mevalonate for the production of non-sterol isoprenoids, which are essential for growth differentiation. Provides spatial information during embryogenesis to guide migrating primordial germ cells (the pole cells) from the ectoderm to the mesoderm. Also required for association of the pole cells w... |
Q9YH06 | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSSKEKGKFEDMAKADKLRYEKEMKNYVPPKGETKKKFKDPNAPKRPPSAFFLFCSEFRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKVDAGKKVVAKAEKSKKKKEEEEDEDEDEEDEEDEEEEEEEEEDDDDDE | Function: Multifunctional redox sensitive protein with various roles in different cellular compartments. Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent struc... |
P09429 | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE | Function: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stabi... |
P63158 | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEDDEEDEEDEEEEEEEEDEDEEEDDDDE | Function: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stabi... |
P12682 | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKHPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEEEEEDDDDE | Function: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stabi... |
P26584 | MGKGDPNKPRGKMSSYAYFVQTCREEHKKKHPDSSVNFAEFSRKCSERWKTMSSKEKGKFEEMAKGDKARYDREMKNYVPPKGEKKGKKKDPNAPKRPPSAFFLFCSEHRPKIKNDHPGLSIGDTAKKLGEMWSEQLAKDKQPYEQKAAKLKEKYEKDIAAYRAKSKSDAGKKGPGRPAGSKKKAEPEEEEEEEEDEEEEEEEEDEE | Function: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner (By similarity). Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA . Can bent DNA and enhance DNA flexibility by looping thus p... |
P26583 | MGKGDPNKPRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDMAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSEHRPKIKSEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYRAKGKSEAGKKGPGRPTGSKKKNEPEDEEEEEEEEDEDEEEEDEDEE | Function: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes. Binds DNA with a pref... |
P30681 | MGKGDPNKPRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDLAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSENRPKIKIEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYRAKGKSEAGKKGPGRPTGSKKKNEPEDEEEEEEEEEEEDDEEEEEDEE | Function: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes. Binds DNA with a pref... |
P25466 | MEDYSNLSLKSIPKRTCRIIFRTATILGICTLIVLCSSILHEIIHLDVSSGLMDSDDSQQGIIQPIIESLKSLIALANQILYNVAIIIPLKIDSIETVIFSALKDMHTGSMSNTNCTPGNLLLHDAAYINGINKFLVLKSYNGTPKYGPLLNIPSFIPSATSPNGCTRIPSFSLIKTHWCYTHNVMLGDCLDFTTSNQYLAMGIIQQSAAAFPIFRTMKTIYLSDGINRKSCSVTAIPGGCVLYCYVATRSEKEDYATTDLAELRLAFYYYNDTFIERVISLPNTTGQWATINPAVGSGIYHLGFILFPVYGGLISGTPS... | Function: Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity).
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,... |
P08492 | MEYWKHTNHGKDAGNELETSMATHGNKITNKITYILWTIILVLLSIVFIIVLINSIKSEKAHESLLQDVNNEFMEVTEKIQMASDNINDLIQSGVNTRLLTIQSHVQNYIPISLTQQMSDLRKFISEITIRNDNQEVPPQRITHDVGIKPLNPDDFWRCTSGLPSLMKTPKIRLMPGPGLLAMPTTVDGCVRTPSLVINDLIYAYTSNLITRGCQDIGKSYQVLQIGIITVNSDLVPDLNPRISHTFNINDNRKSCSLALLNTDVYQLCSTPKVDERSDYASSGIEDIVLDIVNHDGSISTTRFKNNNISFDQPYAALYP... | Function: Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity).
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,... |
A9D857 | MNKVLAIVLTITVAGFAQTAFADDHAMSPDMKLLAGASNWVNQSGSVAQFVFTPSPTQPQTYEVSGNYINNAQGTGCKGTPYPLSGAYYSGNQIISFSVVWSNASANCQSATGWTGYFDFSGSQAVLKTDWNLAFYSGSTPAIQQGQDDFMQSVATVSESLLTE | Function: The exact role played by hoefavidin in the host organism is still obscure. Forms a strong non-covalent complex with biotin and 2-iminobiotin.
Sequence Mass (Da): 17412
Sequence Length: 164
Domain: The C-terminal segment plays a key role in the formation and stabilization of the octameric configuration, since ... |
P47124 | MAKTTKRASSFRRLMIFAIIALISLAFGVRYLFHNSNATDLQKILQNLPKEISQSINSANNIQSSDSDLVQHFESLAQEIRHQQEVQAKQFDKQRKILEKKIQDLKQTPPEATLRERIAMTFPYDSHVKFPAFIWQTWSNDEGPERVQDIKGMWESKNPGFAHEVLNHDVINALVHHYFYSIPEILETYEALPSIILKIDFFKYLILLVHGGVYADIDTFPVQPIPNWIPEELSPSDIGLIVGVEEDAQRADWRTKYIRRLQFGTWIIQAKPGHPVLREIISRIIETTLQRKRDDQLNVNLRNDLNIMSWTGSGLWTDTI... | Function: The M-Pol II complex possesses alpha-1,6-mannosyltransferase activity and is probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46297
Sequence Length: 396
Subcellular ... |
O31266 | MTDTYLHETLVFDNKLSYIDNQRDTDGPAILLLPGWCHDHRVYKYLIQELDADFRVIVPNWRGHGLSPCEVPDFGYQEQVKDALEILDQLGVETFLPVSHSHGGWVLVELLEQAGPERAPRGIIMDWLMWAPKPDFAKSLTLLKDPERWREGTHGLFDVWLDGHDEKRVRHHLLEEMADYGYDCWGRSGRVIEDAYGRNGSPMQMMANLTKTRPIRHIFSQPTEPEYEKINSDFAEQHPWFSYAKLGGPTHFPAIDVPDRAAVHIREFATAIRQGQ | Cofactor: None. Contrary to most other dioxygenases, this enzyme does not require a cofactor for catalysis.
Function: Ring-cleaving dioxygenase involved in quinaldine degradation and utilization.
Catalytic Activity: 3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = CO + H(+) + N-acetylanthranilate
Sequence Mass (Da): 31858
S... |
P64634 | MNPPINFLPWRQQRRTAFLRFWLLMFVAPLLLAVGITLILRLTGSAEARIDAVLLQAEQQLARSLQITKPRLLEQQQLREQRSQRQRQRQFTRDWQSALEALAALLPEHAWLTTISWQQGTLEIKGLTTSITALNALETSLRQDASFHLNQRGATQQDAQGRWQFEYQLTRKVSDEHVL | Function: Required for the use of extracellular DNA as a nutrient.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20796
Sequence Length: 179
Subcellular Location: Cell inner membrane
|
P45751 | MNMFFDWWFATSPRLRQLCWAFWLLMLVTLIFLSSTHHEERDALIRLRASHHQQWAALYRLVDTAPFSEEKTLPFSPLDFQLSGAQLVSWHPSAQGGELALKTLWEAVPSAFTRLAERNVSVSRFSLSVEGDDLLFTLQLETPHEG | Function: Required for the use of extracellular DNA as a nutrient.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16846
Sequence Length: 146
Subcellular Location: Cell inner membrane
|
Q7PWT9 | MENDKMEIYESLIRWLSELNLSAPHGTVQELSDGAALAQALNQIAPEVFTDSWLSKIKSDVGANWRLKVSNLRKIIEGIYVYYQDELSLNLSEELRPDALKIAEKGDPHELGRLLQLILGCAVNCLEKQKYITQIMELEESLQRNIMAALQDIEYIWQGASPSRNSINTAATSLDVKTLQEDRDTLAQKCHETNKKMLGLIEEKAALQQEIVKLQAIVGRYENPNLIGDDGTSLGPIQLGSSRYNDLRKLVDSLKDELLQAETARDDLKMKSMIQEKEIGELQVKIDELHAATAEIAQLKDEIDILKEANEKLKICETQL... | Function: Involved in endocytic trafficking. Probably acts as a cytoskeletal linker protein that tethers endosome vesicles to the cytoskeleton.
Sequence Mass (Da): 77381
Sequence Length: 690
Domain: The coiled coil domain mediates homodimerization.
Subcellular Location: Cytoplasm
|
Q23529 | MLDLTNKESESSDNGNSKYEDSIDGREVGTSKPFKEERSLEDLQADLADMAVWMEGLDATKLPLNDPQLLCNGRAFSEVLHNVDKNFFTDGWLETMPENRTTNIMVFRSCTRKLWRKMFDYVNHINRTVVSSRWTDIHERIDGIYESDLPAMVNLGMAVVTLAHIGKNAKRFVDYSKALTSTHKSMMSNVAKMVTTVIDEMPENPCFHEISELHGSQSELNSLSESSGKLNGNGSSERRSNADQILVDAELEIERLRTETENQRKEIERLTKSFETAQHDMSSNSESGDISILEKQNEELRQKRRELEEKNLELDAAVDQ... | Function: Cytoskeletal linker protein, which is essential for attachment of the centrosome to the nucleus . Required for dynein localization to the nuclear envelope . Forms a LINC (LInker of Nucleoskeleton and Cytoskeleton) complex together with unc-84, that may be involved in DNA damage repair .
Sequence Mass (Da): 88... |
Q54IK9 | MIETSFIKWINSFKDLSNSIEDLKELSNGTIFNEICCQIAPKYFDIDSLRKDGLDNWIFREENIKNIVERVDEFYIEEMGLNDQISSINCEEIANENIDEIILLIEAILGMAMESENNEAVIENILSLDQDTQNDLMVVVAKIQQSHQPNTVDNSKSFDKDGSILSQSPSQSNNSISNNNNNNNIDSSNISKSNISSNNNNNNSSNNNKEEILNLQNEIEKLKREKQEIQNDLDESNIQLSNVTMDRDRITIDKQKTEEVCSSLHESIIGLQKQLDETMAQTTTMNALNDETYKTEINDLHMQVESKEKQLSELKKKVDE... | Function: Cytoskeletal linker protein involved in tethering membrane bound organelles to the cytoskeleton.
Sequence Mass (Da): 84236
Sequence Length: 734
Domain: The large coiled coil domain may mediate homodimerization.
Subcellular Location: Cytoplasm
|
P37352 | MKGTIFAVALNHRSQLDAWQEAFQQSPIKAPPKTAVWFIKPRNTVIGCGEPIPFPQGENLLSGATVALIVGKTATKVREEDAAEYIAGYALANDVSLPEESFYRPAIKAKCRDGFCPIGETVALSNVDNLTIYTEINGRPADHWNTSDLQRNAAQLLSALSEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPVVDEREVTTRKSFPTLPHPHGTLFALGLNYADHASELEFKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDYVAGYTVCNDYAIRDYLENYYRP... | Function: Decarboxylates OPET (5-oxo-pent-3-ene-1,2,5-tricarboxylic acid) into HHDD (2-hydroxy-hept-2,4-diene-1,7-dioate) and isomerizes it to OHED (2-oxo-hept-3-ene-1,7-dioate).
Catalytic Activity: (2E,4Z)-5-hydroxypenta-2,4-diene-1,2,5-tricarboxylate = (3E,5R)-5-carboxy-2-oxohept-3-enedioate
Sequence Mass (Da): 46878... |
P42270 | MFDKHTHTLIAQRLDQAEKQREQIRAISLDYPEITIEDAYAVQREWVRLKIAEGRTLKGHKIGLTSKAMQASSQISEPDYGALLDDMFFHDGSDIPTDRFIVPRIEVELAFVLAKPLRGPNCTLFDVYNATDYVIPALELIDARCHNIDPETQRPRKVFDTISDNAANAGVILGGRPIKPDELDLRWISALMYRNGVIEETGVAAGVLNHPANGVAWLANKLAPYDVQLEAGQIILGGSFTRPVPARKGDTFHVDYGNMGSISCRFV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Transforms 2-oxo-hept-4-ene-1,7-dioate (OHED) into 4-hydroxy-2-oxoheptanedioate, a step in the 4-hydroxyphenylacetic acid (4-HPA) degradation pathway.
Catalytic Activity: (4Z)-2-oxohept-4-enedioate + H2O = (4S)-4-hydroxy-2-oxoheptanedioate
Sequence Mass (Da): 29715
Se... |
Q47098 | MENSFKAALKAGRPQIGLWLGLSSSYSAELLAGAGFDWLLIDGEHAPNNVQTVLTQLQAIAPYPSQPVVRPSWNDPVQIKQLLDVGTQTLLVPMVQNADEAREAVRATRYPPAGIRGVGSALARASRWNRIPDYLQKANDQMCVLVQIETREAMKNLPQILDVEGVDGVFIGPADLSADMGYAGNPQHPEVQAAIEQAIVQIRESGKAPGILIANEQLAKRYLELGALFVAVGVDTTLLARAAEALAARFGAQATAVKPGVY | Cofactor: Binds 1 divalent metal cation per subunit. Has the highest activity with Co(2+) and Mn(2+), but can also use Zn(2+), Fe(2+) and Mg(2+).
Function: Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) to pyruvate and succinate semialdehyde. Is also able to catalyze the aldo... |
Q93AR8 | AIGSAGLGALVLFAAYSNDLSYFAANGDKYPYFANIGEISFDLSNPYVVAGLIFGGLIPYLFGGIAMTAVGRAAGSIVEEVRRQFKEKPGIMQGKDKPNYGRAVDLLTKAAIREMIVPSLLPVLAPLVVYFGVLLISGSKASAFAALGASLLGVIVNGLFVAISMTSGGGAWDNAKKSFEDGFVDKDGQRHMKGSEAHKASVTGDTVGDPYKDTAGPAVNPAIKI | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force (By similarity).
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence M... |
Q93AS0 | GSAGLGALVLFAAYANDLSYFAANGDTYPYFKDIGEISFSLANPYVVAGLLFGGLIPYLFGGIAMTAVGKAASAIVEEVRRQFREKPGIMAGTEKPDYGRAVDLLTKAAIREMVIPSLLPVLAPLVVYFGVLLISGSKAFAFAALGAYLLAVIMNRVLVAICMTLVGSS | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force (By similarity).
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence M... |
Q8TJA8 | MESLIFIAPLAGVISLVFAAFFAKSILKEDAGNKRMKEIAGAIQEGAMAYLNRQYKTIAVVSIILSFLILFLLDDGLKIAIGFLAGAISSAAAGYIGMSVSVRANIRTAHAASSGLEKAMSVAFRGGAVTGLAVVGLALLGTSSFYILYGDVDLVVGFGFGASLISLFARVGGGIFTKAADVGADLVGKVEAGIPEDDPRNAGVIADNVGDNVGDCAGMGADLFETYVVTSLAAMLLGSLIIGTYENAILYPLVLGSVAIFASIISVFFVKIGKEGKIMQALYKGVGGSAIISLIAFYFVTNSLMGDIRLFYATVVGIII... | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69017
... |
Q2RLE0 | MELFPIIPAGGILALLVALYMTSSVLKEDTGPKEMQTIAAAIREGAMAFLNRQYRTIAGLALIVAVLLALLTRQYHTAVAFITGAFASALSGYIGMYVAVNANLRVAAGARNSLNKALTVAFRGGAVTGLAVTALSLLGVTSLFYAFGGATNPTRAPLDIVGFGFGASFVALFAQLSGGIYTKAADVGADLVGKVEAGIPEDDPRNPAVIADLVGDNVGDCAGRGADLFESTAAENIGAMILGIALVPFFGVKGIVFPLVARAAGIIASIIGMFFVRAEENQDPMAALNRGYIVTSILAIIFLYPISRYMLSGPGVNFIY... | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70892
... |
Q93AR9 | MVLAAIFFGGTPILATAMAYPLAICAACVITSIIGTFFVKLGTNNSIMGALYKGLIVTGALSILGLGAATSFTIGWGSIGTVGGIEVRGGNLFVCGLIGLVVTALIVVITEYYTGTNKRPVNSIAQASVTGHGTNVIQGLAVSLESTALPAIVIVGGIIATYQLAGLFGTAIAVTAMLGLAGMIVALDAFGPVTDNAGGIAEMSHLSP | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force (By similarity).
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence M... |
Q8UG67 | MRMTVIPIVILCGVLSVVYAVWTTKSVLDADQGNERMREIAGYIREGAQAYLTRQYLTIAIVGLIVAVLAWYLLSAIAAIGFVIGAVLSGVAGFVGMHVSVRANLRTAQAASHSLGAGLDIAFKSGAITGMLVAGLALLGVSIYYFVLTSVLGHPPGSRAVIDALVSLGFGASLISIFARLGGGIFTKGADVGGDLVGKVEAGIPEDDPRNPATIADNVGDNVGDCAGMAADLFETYAVSVVATMVLAAIFFAGTPILESAMVYPLAICGACILTSIAGTFFVKLGTNNSIMGALYKGLIATGVFSVAGLAVATYATVGW... | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72792
... |
Q8VNU8 | AGGIAEMSGLPEDVRKTTDALDAVGNTTKAVTKGYAIGSAGLAALVLFADYTHNLEVAGKMQVFSLSDPAVIIGLFIGGLVPYLFGAMAMEAVGRAAGSVVIEVRRQFREIKGIMEGTAKPDYSRAVDLLTKAAIKEMVVPSLLPILVPVAVAIGMNILMGDGAGIRALGGMLIGTIVTGLFVAISMCTGGGAWDNA | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force (By similarity).
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence M... |
Q8VRZ1 | NGSIMGALYKGLIATGLLSIVGLGVANTLTVGWGEIGTVAGKSITGTNLFVCGLIGLIVTGLIVVITEYYTGTNKRPVNSXAQASVTGHGTNVIQGLAVSLESTALPAIVIVGGIIXTYQLAGLFGTAIAVTAMLGIAGMI | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force (By similarity).
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence M... |
Q8A294 | MDSILFWLVPVASVLALCFAYYFHKQMMKESEGTPQMIKIAAAVRKGAMSYLKQQYKIVGCVFLGLVILFSIMAYGFHVQNVWVPIAFLTGGFFSGLSGFLGMKTATYASARTANAARNSLNSGLRIAFRSGAVMGLVVVGLGLLDISFWYLLLNAVIPADALTPTHKLCVITTTMLTFGMGASTQALFARVGGGIYTKAADVGADLVGKVEAGIPEDDPRNPATIADNVGDNVGDVAGMGADLYESYCGSILATAALGAAAFIHSADTVMQFKAVIAPMLIAAVGILLSIIGIFSVRTKENATVKDLLGSLAFGTNLSS... | Function: Sodium pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for Na(+) movement across the membrane.
Catalytic Activity: diphosphate + H2O + Na(+)(in) = H(+) + Na(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76538
Sequence Length: 734
Subcel... |
Q89K83 | MTALWLIVLCGVLSVVYAIWATSSVLSADAGSPRMQEIAAAVREGAQAYLRRQYTTIGIVGIVIFVLLVYFLGFYVAIGFAIGAILSGAAGFIGMNVSVRANVRTAQAATTSLAGGLELAFKAGAITGMLVAGLALLGVTLYFGFLVYSLKLAPDSRVVVDAMVALGFGASLISIFARLGGGIFTKGADVGGDLVGKVEAGIPEDDPRNPATIADNVGDNVGDCAGMAADLFETYAVTAVATMVLAAIFFAKTPILMSMMTLPLAIGGICIITSIIGTFFVKLGPSQSIMGALYKGLIATGVLSLIGIAVVIYTLIGFGK... | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72442
... |
Q8RCX1 | MGAYLTLIYGVIVIAALVIIGLIKFIFAQDKGNEKMQQISDAIKEGAMAFLNRQYKTIASLALIVAVIIVVANYYGHLSEGSSQALSFALHVGFAFITGAFCSALSGYIGMYMAVNSNIRAAAGARSGLNRALQIALKGGAVTGLAVTALSLFGVATLFLAYGGLSGQDELIKEAPSLIVGFGFGASFVALFAQLGGGIYTKAADVGADLVGKVEAGIPEDDPRNPAVIADLVGDNVGDCAGRGADLFESTAAENIGAMILGVGLYPIFGWKGILFPLVARAIGIIASIIGIFFVNTKDESKDPMIALNKGYFVTTVVNL... | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74381
... |
Q3AFC6 | MENGMTLAYYGLGAGILAILFALYLFSSVLKEDMGNEKMREISQAIFEGAMAYLNRQYKTLIPFALVVFVLLVVGFGYKEGDFGYGLKVGVSFLVGAIASALAGYAGMTSTTKANARTTQAARKSLNAALNVAFRAGGVMGMSVAGLGLLGVSALYIIFKDVHVIDSFAFGASAIAFFARVGGGIYTKAADVGADLVGKVEAGIPEDDPRNPAVIADNVGDNVGDTAGMGADLFESYGATTMAAMLLGLTFAKNHGFSEVLGATFPLLLGAAGIVAAIISTFFVRTSEDGNPQMALNIGLWSTNFITAIFTYIIAQYVFG... | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for Na(+) movement across the membrane.
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71063
Sequence Length: 686
Subcellular L... |
Q9A8J0 | MSLWLYLAIGAGLLAVLYGAVQTASLMRASAGNARMQEIAAAIQEGAQAYLKRQYTTISIVGVVVIAALAFFFKSWEQPVGFALGAILSGAAGFAGMLISVRANVRTAQASSESLAKGLSMAFTSGAVTGMLVAGFALLGVAGYYYVLLATGHEATGRVVIDSLVALGFGASLISIFARLGGGIFTKGADVGGDLVGKVEAGIPEDDPRNAATIADNVGDNVGDCAGMAADLFETYAVTTVATMVLAAIFFRGTEAVSAMMLLPLAICAVCIVTSIIGAFFVRLGKSQNIMGALYQGLIVTGVLSIPAVWYVIHQLVPTA... | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72944
... |
Q8VNW3 | MQDLNAVQSLAVWAVLVISLLGIGYAFFIRSQILAQDTGTPKMREVWGFIKTGANAYLSQQFRTISILIVILTFVLAASVFIIPPTTEAVERFGSKEAATIWVAIGRAVAFLMGSLFSYAVGFVGMNVAVEGNVRVAAAARKGYNPALQVAYKSGSVTGMLTVGLGLLGGTLIFMVFGIAAPDALLGFGFGGSLIALFMRVGGGIYTKAADVGADLVGKVEAGIPEDDPRNAAVIADLVGDNVGDCAGMAADVFESFEVTLVSALILGLVLGDAVVGTIGDGAYDLRFIIFPLVLRAIGVVASVIGNLFVTTDERKRNAM... | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80486
... |
Q8KDT8 | MYGLVVCLFGMIFGLIQYQGINKLPVHAAMKEISDLIYETCKTYLITQGKFIIILWALVAAIIVAYFGGLNHLAPDKVVFILACSLLGIAGSYTVAWFGMRINTFANSRTAFASLGGKPFPTYAIPLRAGMSIGMLLISIELFAMLCILLFIPVDYAGPCFIGFAIGESLGASVLRIAGGIFTKIADIGSDLMKIVFKIKEDDARNPGVIADCTGDNAGDSVGPTADGFETYGVTGVALISFILLAIKDPSIQVSLLVWIFAMRLVMIVASAVSYWVNDALAKMKYGNADEMNFEKPLITLVWLTSIVSIVLTYIASYML... | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80370
... |
B3QY08 | MDFKKKPIKKKSITVAYFYEHLSSRLSIKLKKLNQVDEEKRKIYERDIHRPGLALAGFTNLFTYRRVQVFGNTETWFLNHLGTEERKQAFSNITRYKVPCIIVTNNNKLDPELVEMATEAGIPLYRTSHTTTKFIYLITDFLDDQFCHYQHYHGSMVDVYGVGMFITGRSGIGKSEVALDLIERGHRLVADDLVVITRKGESVLMASGTELVRHFMEIRGLGIIDVEAMFGIRAIRHQKRVEIVVELLEFEPGKEFDRTGLENKSVDILGVEVPLVQLPIYPGKNITVIAEVVALNYLLKHYGYDAAEEFDRRIQQQIAT... | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation... |
Q8KBZ7 | MNFDQKGLKKRSITVAYFFEHIQKRFDIKFRRLNELDEQKCRIHERDLHRPGLAIAGFTKLFTYKRVQILGNTETRYLNHLSDEERKTAFANFVSFRMPCIILTSNNKLDQELVDMATGAGIPVFITRCSSTKTIYYITDFLDEEFSLYQQYHGSMIDVYGVGVLLTGKSGLGKSEVALDLIERGHGLVADDVVVVKRKGETKTLVASRNNIIDHFMEIRGLGVVDVRQNFGIRAIRDRKEVQVVVELLEWSKESEYERLGLDQKMVKLLGVDLPLVQLPIFPGKNITAIIEVVALNFLLKHYAGYVPAEALTERIRNVI... | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation... |
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