ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9X839 | MTQQPFQLPHFYLPHPARLNPHLDEARAHSTTWAREMGMLEGSGVWEQSDLEAHDYGLLCAYTHPDCDGPALSLITDWYVWVFFFDDHFLEKYKRSQDRLAGKAHLDRLPLFMPLDDAAGMPEPRNPVEAGLADLWTRTVPAMSADWRRRFAVATEHLLNESMWELSNINEGRVANPVEYIEMRRKVGGAPWSAGLVEYATAEVPAAVAGTRPLRVLMETFSDAVHLRNDLFSYQREVEDEGELSNGVLVLETFFGCTTQEAADLVNDVLTSRLHQFEHTAFTEVPAVALEKGLTPLEVAAVGAYTKGLQDWQSGGHEWH... | Cofactor: Magnesium. Fe(2+) or Cu(2+) ions are very less efficient as cofactors.
Function: Tow-domain protein where the N-terminal domain catalyzes the cyclization of farnesyl diphosphate (FPP) to a 85:15 mixture of the sesquiterpene alcohol germacradienol and the sesquiterpene hydrocarbon germacrene D. The C-terminal ... |
P38909 | MLWKNYVLSSSRITRRLHKSPRKSSFSKNFFITGCLLTVGAVSSYLTYRYTSERENKHELSPSYFVKYKISHKRDIDSSHFLLEVTPLFKQKVNIWSLMTAENLWSVEIKQPEVMVVRNYTPLPLKFNPASKEIEILKDGDNADGKLSFYIKKYENGEVARWLHHLPKGHIIEIRGPFIDYEFPHLPNELKRSRDCLYMDNRNERGNNVRENSQFIYQPYDIMMFTAGTGIVTALQLLLTESPFRGTIKLFHTDKNIKQLGPLYPILLRLQASNRVQLKIFETDRQTKQDVLKSIQKSITKPYPYKGLLPFSNVNNKNIM... | Cofactor: Binds 1 FAD per monomer.
Function: Redox component that participates in c-type cytochrome biogenesis in the mitochondrial intermembrane space. May play a role in the reduction of heme prior to its ligation to apocytochrome c by cytochrome c heme lyase. Has oxidoreductase activity in vitro.
Location Topology: ... |
P81078 | ADSLTQFDGIKGRYSHEAFYEEKACDSCHLNK | Function: Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.
PTM: Binds 1 heme group per subunit.
Sequence Mass (Da): 3664
Sequence Length: 32
Subcellular Location: Periplasm
|
P00076 | GDAERGKKLFESRAAQCHSAQKGVNSTGPSLWGVYGRTSGSVPGYAYSNANKNAAIVWEEETLHKFLENPKKYVPGTKMAFAGIKAKKDRQDIIAYMKTLKD | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... |
P00004 | MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... |
P99999 | MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... |
Q2JUP0 | MKRIYLALCALLLLLGTGSRPAAAYPYYAQMAYDNPREATGKIVCANCHLNAMPARAEVPQAVTPGQVFTIKVGIPYDLSKQQVLADGSKGGLNVGAVVVLPEGFRLATEEEMTEEQRQETAETYITPYSDEKPNILLVGPLPGEQHQEIVFPVVAPDPKEDPSVAFMKYRVYIGANRGRGQINPDGSLSNNNVFRAPATGRLTSIATIESDLSDLPPELAALVPPEYELPGTRVLSFETEGGLKHLVVPPGPELVVNIGDSVQEGDPVTNNPNVGGFGQVERDLVLQNPERVKWLVAFLAAVAITQLLLVLKKKQVELI... | Cofactor: Binds 1 heme group covalently.
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 35284
Sequence ... |
A8NV38 | MTPAVSPAHTVLFEAKARKGISFEQIGKAIGRDEVWVASAFYGQAKFNEEELKKLSEVLEISSAQIVKELGDQWFPNRGLGPVPPSDPVIYRLFEGVLVYGHPIKAIIHEKFGDGIMSMIDCNINVERKPDPKGDRVVVTFDGKFLPYSKW | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 16876
Sequence Length: 151
EC: 4.2.1.104
|
P0CN03 | MFNLPYHCKALLTAKQERGLTFDDVAKAINKPEVWTTALFYGQASTDKSTAEAILKALGGEQFWTDYNDRLEAGQEKIDIRRVLNGLSGNGEENMGVKGMVTRGATFEVPPKDPVLYRLYEVLVVYGYSYKALIYEKFGDGIMSAIDFRTSLERKKDPKGDRVVITMDGKFLPYSDPSAWGTQ | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 20538
Sequence Length: 183
EC: 4.2.1.104
|
Q0K572 | MNRSDVTDLIIEAKVTRGIAWAQVAERVGRSKEWTTAACLGQMAFDAAGARAVMELFGLPPEAEPWLREVPYKGSLPTQVPADPLIYRFYELISVYGTTFKALIHEEFGDGIMSAIDFRMDLQREPDPNGDRVRIEMSGKFLPYKTY | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 16578
Sequence Length: 147
EC: 4.2.1.104
|
P58704 | MIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARQVGAKLDLDEDAILLLQMIPLRGCIDDRIPTDPTMYRFYEMLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPF | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 17048
Sequence Length: 156
EC: 4.2.1.104
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P0ABJ0 | MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT... | Cofactor: Binds 1 copper B ion per subunit.
Function: Cytochrome bo(3) ubiquinol oxidase is the terminal enzyme in the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Catalyzes the four-electron reduction of O2 to water, using a ubiquinol as a membrane soluble electron donor... |
Q9I426 | MFGKLTLSAVPYHEPIVMVTLAVVALLGLGVVGAITYYRKWTYLWTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLALAEGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEVYILILPAFGIFSEVTATFAGKRMFGYKSMVWAS... | Cofactor: Binds 1 copper B ion per subunit.
Function: Cytochrome bo(3) ubiquinol oxidase is the terminal enzyme in the aerobic respiratory chain. Catalyzes the four-electron reduction of O2 to water, using a ubiquinol as a membrane soluble electron donor for molecular oxygen reduction. Has proton pump activity across t... |
P57542 | MIENKFNNTILNSNSSTHDKISETKKLFGLWIYLMSDCIMFAVLFAVYAIVSSNISINLISNKIFNLSSILLETFLLLLSSLSCGFVVIAMNQKRIKMIYSFLTITFIFGLIFLLMEVHEFYELIIENFGPDKNAFFSIFFTLVATHGVHIFFGLILILSILYQIKKLGLTNSIRTRILCFSVFWHFLDIIWICVFTFVYLNGAI | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
Q89AA5 | MKKKYKIDTNIFSKELLGFWLYLMSDCIIFCTLFSVYFILVDNVAQGPSGHNIFQNNLIIIETFLLLFSSFSCNLVLFEMKNKNLYMVFLWLGITFLLGLLFVFLELFEFFHLINLGFGPTRSGFLSSFFVLIATHGIHVISGLIWIIVMIKYVYTFNITNLIYYRMLCLNLFWHFLDIVWVFIFSFVYLFGMV | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
Q9I425 | MSTAVLNKHLADAHEVGHDHDHAHDSGGNTVFGFWLYLMTDCVLFASVFATYAVLVHHTAGGPSGKDIFELPYVLVETAILLVSSCTYGLAMLSAHKGAKGQAIAWLGVTFLLGAAFIGMEINEFHHLIAEGFGPSRSAFLSSFFTLVGMHGLHVSAGLLWMLVLMAQIWTRGLTAQNNTRMMCLSLFWHFLDIVWICVFTVVYLMGAL | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
Q8K996 | MNKYKKIKNNFDKEKKSYIVGFLFSLFLTIIPFFCTLNHLFSRKINFFVILLCALSQIIIHFIYFLHLDFSKKNSWNIISLLFILIIVFIIVFGSIWIMYNLNHHVIL | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
Q89AA6 | MLKNRYLKYLFILILLSILSIMPIFAIIYRIFSRNYLYAFIIVCLFFQILAHIKFFLNLDFSLEQRWKLISVIFSLVVGLIILLGSIWVIKNLNNNLCIM | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
P0ABJ7 | MSHSTDHSGASHGSVKTYMTGFILSIILTVIPFWMVMTGAASPAVILGTILAMAVVQVLVHLVCFLHMNTKSDEGWNMTAFVFTVLIIAILVVGSIWIMWNLNYNMMMH | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
Q9I424 | MSSAAHDNHGAGHGSLGSYAIGFVLSVILTAIPFYMVMDGGFSRHATILTMVVLGLVQVVVHLICFLHMNMSSEGRWNVMAFIFTVIVILLVVGLSLWIIFSADMLMMPMP | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
Q9MUN1 | MSILIDNISKKFGNFQALNHINLEIKSGSIIALLGPSGSGKSTLLRIIAGLDTPDEGTIWISGKNASGYSIQSRNIGFVFQNYALFKNMTVYDNIAFGLELRRISFNDISRKVNKLLELVQLQNLGHRYPAQLSGGQRQRIALARALAIEPKVLLLDEPFGALDARVRKNLRAWLRDLHNKFSITTIIVTHDQQEAMEIADEIVVFNSGRIEQIGKPQDIYDQPATPFVFSLLGYVNKISFDNEIANFLLSSFPEKQSVLMQEKQFYIRPHQIVISKQSNESNYSAKIENLLYIGNWIHLDIYVASFNVNLKVHVSPKEF... | Function: Part of the ABC transporter complex involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Sequence Mass (Da): 39517
Sequence Length: 348
Subcellular Location: Plastid
EC: 7.3.2.3
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P0A4W3 | MTYAIVVADATKRYGDFVALDHVDFVVPTGSLTALLGPSGSGKSTLLRTIAGLDQPDTGTITINGRDVTRVPPQRRGIGFVFQHYAAFKHLTVRDNVAFGLKIRKRPKAEIKAKVDNLLQVVGLSGFQSRYPNQLSGGQRQRMALARALAVDPEVLLLDEPFGALDAKVREELRAWLRRLHDEVHVTTVLVTHDQAEALDVADRIAVLHKGRIEQVGSPTDVYDAPANAFVMSFLGAVSTLNGSLVRPHDIRVGRTPNMAVAAADGTAGSTGVLRAVVDRVVVLGFEVRVELTSAATGGAFTAQITRGDAEALALREGDT... | Function: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37444
Sequence Len... |
Q73XU8 | MIDAGTDRGDIAITVRDAYKRYGDFVALDHVDFVVPTGSLTALLGPSGSGKSTLLRTIAGLDQPDTGTVTIYGRDVTRVPPQRRGIGFVFQHYAAFKHLTVRDNVAYGLKVRKRPKAEIKAKVDNLLEVVGLSGFQGRYPNQLAGGQRQRMALARALAVDPQVLLLDEPFGALDAKVREDLRAWLRRLHDEVHVTTVLVTHDQAEALDVADRIAVLNQGRIEQIGSPTEVYDAPTNAFVMSFLGAVSTLNGTLVRPHDIRVGRTPEMAVAAEDGTAESTGVARAIVDRVVKLGFEVRVELTSAATGGPFTAQITRGDAEA... | Function: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38813
Sequence Len... |
Q5YZY9 | MITVTNARKNYGNFAALDDVTIEIPSGELTALLGPSGSGKSTLLRSIAGLEALDDGVVVIAGKDVTRVAPQKRDIGFVFQHYAAFKHMTVRDNVAFGLKIRKRPKAEITKRVDELLGIVGLDGFQHRYPAQLSGGQRQRMALARALAVDPQVLLLDEPFGALDAKVRADLRTWLRRLHEEVHVTTVLVTHDQEEALDVADRIAVMNKGRIEQVGTPEDVYDRPANEFVMSFLGDVARLNGHLVRPHDIRVGRDPSMALAAHEGTAESAGVTRATVERVVHLGFEVRVELRNAATGDLFSAQVTRGDAEALRLTDGETVYA... | Function: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36232
Sequence Len... |
Q8Z0H0 | MGIVVENVSKQFGSFRAVDQVNLEIQSGKLVALLGPSGSGKSTLLRLIAGLEKPDDGRIILTGKDATNQSVQERNIGFVFQHYALFKHLTVRQNIAFGLEIRKAPANKVKGRVEQLLELVQLSGLGDRYPSQLSGGQRQRVALARALAVEPSVLLLDEPFGALDAKVRKDLRAWLRRLHDEVHVTTVFVTHDQEEAMEVSDEVVVMNQGRVEQVGTPAEIYDNPATSFVMSFIGPVNVLPSSSRIFQSSQLEIEHPNVFLRPQDVVIEKSANGTTAPATVTRLIHLGWEIKVELTLDDGQVVNAHLTRDRYDELQLEPKQ... | Function: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37567
Sequence Len... |
Q9I6L0 | MSIEIRNVSKNFNAFKALDDINLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDAGNIVFHGEDVSQHDVRDRNVGFVFQHYALFRHMTVFDNVAFGLRMKPKGERPGESAIKAKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKILLLDEPFGALDAKVRKELRRWLARLHEEINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGEVYENPASDFVYHFLGDSNRLQLGNDQHLLFRPHEVSLSRSAVAEHRAAEVRDIRPLGAITRVTLKVDGQDELIEAEVVKDHDSLAGLARGETLYFKP... | Function: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36795
Sequence Len... |
Q12QM6 | MTDIVWHQHSIDQAARGAQKSQNPVLLWFTGLSGAGKSTLAGALERALFDAGFHTYLLDGDNVRHGLCKDLGFSLSDRDENLRRVGEVAKLMVDAGLVVLSAFISPTRAERDRVRALFPEGRFIEVHVSTPLSVCEARDPKGLYVKARSGEIKEFTGISSPYEAPTAAELTIDTSRGDLATQVQAMLAYLTAIEVIDANKLSALA | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 22214
Sequence Length: 205
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
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Q8EB13 | MSNIVWHQHSVDQAARARLKGQNPVLLWFTGLSGAGKSTLAGALERALFEAGFHTYLLDGDNVRHGLCKDLGFSVADRDENLRRVGEVAKLMVDAGLVVLSAFISPTREERDSIRARFPEGQFIEVHVSTPLSVCELRDPKGLYVKARKGEIAHFTGISSPYEAPLSAELTIDTSKGDLASQVHALIDYLTAIDVISSNRLASLA | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 22298
Sequence Length: 205
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
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P06106 | MPSHFDTVQLHAGQENPGDNAHRSRAVPIYATTSYVFENSKHGSQLFGLEVPGYVYSRFQNPTSNVLEERIAALEGGAAALAVSSGQAAQTLAIQGLAHTGDNIVSTSYLYGGTYNQFKISFKRFGIEARFVEGDNPEEFEKVFDERTKAVYLETIGNPKYNVPDFEKIVAIAHKHGIPVVVDNTFGAGGYFCQPIKYGADIVTHSATKWIGGHGTTIGGIIVDSGKFPWKDYPEKFPQFSQPAEGYHGTIYNEAYGNLAYIVHVRTELLRDLGPLMNPFASFLLLQGVETLSLRAERHGENALKLAKWLEQSPYVSWVS... | Function: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway . Required to efficiently reduce toxic levels of hydrogen sulfide generated when the sulfate assimilation pathway (SAP) is active . Also catalyzes the conversion of O-acetylserine (OAS) into cystei... |
O65039 | MQKFILLALSLALVLAITESFDFHEKELESEESLWGLYERWRSHHTVSRSLHEKQKRFNVFKHNAMHVHNANKMDKPYKLKLNKFADMTNHEFRNTYSGSKVKHHRMFRGGPRGNGTFMYEKVDTVPASVDWRKKGAVTSVKDQGQCGSCWAFSTIVAVEGINQIKTNKLVSLSEQELVDCDTDQNQGCNGGLMDYAFEFIKQRGGITTEANYPYEAYDGTCDVSKENAPAVSIDGHENVPENDENALLKAVANQPVSVAIDAGGSDFQFYSEGVFTGSCGTELDHGVAIVGYGTTIDGTKYWTVKNSWGPEWGEKGYIR... | Function: Involved in programmed cell death. Shows a pronounced preference for hydrophobic residues in the P2 position and no obvious preference in the P1 position of the cleavage site. Accepts proline at the P1 and P1' positions.
PTM: The potential N-glycosylation site at Asn-115 is not glycosylated.
Sequence Mass (Da... |
O06737 | MNETITYDTWNDMLSKQITDQLIDELDVLKWAYRTYGEKIVYACSFGAEGMVLLDLISKINKNAHIIFLDTGLHFQETYELIETVKERYPGFAIQMLEPELSLTEQGTKYGGELWKHNPNLCCQLRKIEPLKKHLSGMTAWISGLRRDQSPTRKHIQYVNLDQKFELIKICPLIHWTWDDVWTYIRLHNLPYNKLHDQHYPSIGCEMCTLPSPDPNDERAGRWAGREKTECGLHQE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
Catalytic Activity: [thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate
Sequence Mass (Da): 27671... |
Q5WKF5 | MAYVFEQMEATDYEKVNTKLKNRDSLDILRWANQTYGEKLVYACSFGAEAMVLLDLLSKIQKEAHILFLDTDFHFAETYELIERVKERYPTFRINMAKPALSPEEQAERYGDELWLKNPDQCCQIRKLDVLARELEPYDAWLSGLRREQSPTRANTEFVNQDKRFKKVKVCPLIHWTEEEIWMYIKLHQLPYNELHDQHYPSIGCTYCTKAVMPGEDARSGRWAGTGKTECGLHAPTKGDS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
Catalytic Activity: [thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate
Sequence Mass (Da): 28151... |
D3RNJ4 | MTERRQPSLSTDTLPTREAAAIELLSQVCRELDSIVFATSLGAEDMVLTEIIRRERLPIRIFTLDTGRLPTETLELIEVVERHYGTRIERYAPHPDAIADYVSRYGLDGFYDSVPARQACCRVRKLEPLKRALAGQSAWVTGLRAEQSVTRAELPAREWDAANGLEKINPLADWSEHEVWAFIRHHRVPYNPLHNQGYPSIGCAPCTRAITVGEDVRAGRWWWENPETKECGLHRREFAPRQPSAHPAIERDRSAA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
Catalytic Activity: [thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate
Sequence Mass (Da): 29144... |
B4RYS5 | MTNSTAEKQQPLTLDISKEALADINDMLEKTTAQQRVAWALNNLPDTHIVSSSFGAQSAVMLHMLTQVQPDIPVVLTDTGYLFPETYKFIDELVEKLNLNLHVYRADMSSAWQEARFGRLWEQGVEGIEKYNKLNKVEPMQRALRELNAGTWFAGLRRSQSDTRGKLPVLQKVGQQFKLYPIIDWSNKDLHYYLKDNELSYHPLWEQGYVSIGDWHTTQSLQEGMSEQDTRFFGLKRECGLHEFGDGI | Function: Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
Catalytic Activity: [thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol
Sequence Mass (Da): 28527
Sequence Length... |
O32213 | MVTKILKAPDGSPSDVERIKKESDYLRGTLKEVMLDRISAGIPDDDNRLMKHHGSYLQDDRDLRNERQKQKLEPAYQFMLRVRMPGGVSTPEQWLVMDDLSQKYGNGTLKLTTRETFQMHGILKWNMKKTIQTIHSALLDTIAACGDVNRNVMCASNPYQSEIHSEVYEWSKKLSDDLLPRTRAYHEIWLDEERVAGTPEEEVEPMYGPLYLPRKFKIGIAVPPSNDIDVFSQDLGFIAIVEDGKLIGFNVAIGGGMGMTHGDTATYPQLAKVIGFCRPEQMYDVAEKTITIQRDYGNRSVRKNARFKYTVDRLGLENVK... | Cofactor: Binds 1 siroheme per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate (Probable).
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 ... |
A9IT77 | MQSTDNDLSQSPPKLSADEQLKAASDQLRGTILRSLADPLTGAVSDSDAKLLKFHGIYQQDDREQRDERRRQKLEPAYQFMIRVRLPGGVCSAAQWLKLDELARAYGGDSLRLTTRQTFQFHWVLKHNLQATLQGLHEVLLDTIAACGDDARGVMCTADPRLSALHAAVYDIARQASDHAIPRMRAYHEIWWGEQRVASSDAGPEEPFYGQTYLPRKFKIGFVIPPVNDIDVYAQDLGFIAIAGDDGALQGFNVAIGGGMGRTDQAPATYPRLADVIGFVPPEAVIATCDAVMGVQRDYGNRKDRARARFKYTIDEHGLD... | Cofactor: Binds 1 siroheme per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NA... |
P0C0B2 | MKKDYKKVFLKNTKEERIKENSNYLRGTIIDDLKDEITNGFTGDNFSLIRFHGMYQDDRDLRLERNEQKLEPRYAMMLRCRLPRGIIKAKKWLKIDHFASKNTLYGTIRLNNLQTFQFHGILKKTLKDAHKMLNKIGLDSLGTANDVNRNVLCTSNPMESLIHQQCYEWVSKISNFLLPQTKAYAEIWLNQKKIATTDQEPILGKTYLPRKFKTTVVVPPYNDVDLYANDMNFIAITKNNKIVGFNVLIGGGLSINHGNKNTWPFLAVELGYITLEKTLSVAESIVTTQRDWGNRTDRKNAKTRYTIAKVGLSVFKKEVE... | Cofactor: Binds 1 siroheme per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NA... |
Q9JS45 | MSEHDMQNTNPPLPPLPPEITQLLSGLDAAQWAWLSGYAWAKAGNGASAGLPALQTALPAAEPFSVTVLSASQTGNAKSVADKAADSLEAAGIQVSRAELKDYKAKNIAGERRLLLVTSTQGEGEPPKEAVVLHKLLNGKKAPKLDKLQFAVLGLGDSSYPNFCQAGKDFDRRFEELGAKRLLERVDADLDFTASANAWTDNIAALLKEEAAKNRATPAPQTTPPAGLQTAPDGRYCKAAPFPAALLANQKITARQSDKDVRHIEIDLSGSDLHYLPGDALGVWFDNDPALVREILDLLGIDPATEIQAGGKMMPVARAL... | Cofactor: Binds 1 FAD per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> F... |
A1KU06 | MSEHDMQNTNPPLPPLPPEITQLLSGLDAAQWAWLSGYAWAKAGNGASAGLPALQTALPAAEPFSVTVLSASQTGNAKSVADKASDSLEAAGIQVRRAELKDYKAKNIADERRLLLVTSTQGEGEPPEEAVVLHKLLNGKKAPKLDKLQFAVLGLGDSSYPNFCRAGKDFDRRFEELGAKRLLERVDADLDFAAAADGWTGRIVARLKEEAAKNRATPAPQTTPPAGLQTAPDGRYCKADPFPAALLANQKITARQSDKDVRHIEIDLSGSDLHYLPGDALGVWFDNDPALVREILDLLGIDPATEIQAGGKTLPVASAL... | Cofactor: Binds 1 FAD per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> F... |
Q8EAZ9 | MLLKELSSLASPLSQSQVDKLKQLTAELNSVQLAWVSGYLAATANTSGSAIQVAASVTEAQAAQTVTILYGSQTGNGRGIAKALAEKAKTQGYSVNLASMGEYNVRQLKQETLLLLVVSTHGEGEAPDDAIELHKFLATKRAPQLNNLHYSVLALGDSSYEFFCQTGKDFDARLSALGAKALLPLVECDVDYEAAAGQWHADVLTAVKPLIQTTANVVALNEINSTSAQVASESEFTKQNPYRAEVLVSQKITGRDSDRDVRHVEIDLGESGLHYEVGDALGVWFSNSEILVGEILAGLGLAADAKVTVGSESISLKQAL... | Cofactor: Binds 1 FAD per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> F... |
P25779 | MSGWARALLLAAVLVVMACLVPAATASLHAEETLTSQFAEFKQKHGRVYESAAEEAFRLSVFRENLFLARLHAAANPHATFGVTPFSDLTREEFRSRYHNGAAHFAAAQERARVPVKVEVVGAPAAVDWRARGAVTAVKDQGQCGSCWAFSAIGNVECQWFLAGHPLTNLSEQMLVSCDKTDSGCSGGLMNNAFEWIVQENNGAVYTEDSYPYASGEGISPPCTTSGHTVGATITGHVELPQDEAQIAAWLAVNGPVAVAVDASSWMTYTGGVMTSCVSEQLDHGVLLVGYNDSAAVPYWIIKNSWTTQWGEEGYIRIAK... | Function: Hydrolyzes chromogenic peptides at the carboxyl Arg or Lys; requires at least one more amino acid, preferably Arg, Phe, Val or Leu, between the terminal Arg or Lys and the amino-blocking group.
Catalytic Activity: Broad endopeptidase specificity similar to that of cathepsin L.
Sequence Mass (Da): 49836
Sequen... |
Q8FAG5 | MLDQVCQLARNAGDAIMQVYDGTKPMDVVSKADNSPVTAADIAAHTVIMDGLRTLTPDIPVLSEEDPPGWEVRQHWQRYWLVDPLDGTKEFIKRNGEFTVNIALIDHGKPILGVVYAPVMNVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHADAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAAAAGAHVHDWQGKPLDYTPRESFLNPGFRVSIY | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27190
Sequence Length: 246
Subcellular Location: Cell inner membrane
EC: 3.1.3.7
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P22255 | MLDQVCQLARNAGDAIMQVYDGTKPMDVVSKADNSPVTAADIAAHTVIMDGLRTLTPDVPVLSEEDPPGWEVRQHWQRYWLVDPLDGTKEFIKRNGEFTVNIALIDHGKPILGVVYAPVMNVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHADAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAAAAGAHVHDWQGKPLDYTPRESFLNPGFRVSIY | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP. May also convert adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS). Has 10000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2).
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Loca... |
P44332 | MLTLNEHLLNQVLLIAYQSGKHLQQFYQKQVHVELKEDNTPVTEADLFVSQFLTEKLTALFPNVPVLSEENCHISFEERKNWKEYWLIDPLDGTQQFINRTDQFSVLITLVRKNKPVLSVIHAPILSTTYYAMCDFGTFKKQLDQVKKLTKNTTNFDRPLRIAVGATTSQEKVRSILPKDFPCEFVVVGSSSLKSGLVAEGAVDCYVRLGQTGEWDTAGAEVLLGETHGAIFDSHFEPLTYNQRETLINPHFVMVGDQSFDWRSIFQFN | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30723
Sequence Length: 269
Subcellular Location: Cell inner membrane
EC: 3.1.3.7
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P46726 | MASHDKRDYQAELTDAALAADLATAAGELLLEIREEIGFDQPRALGDAGDRLANSLLLSRLRAERPGDAVLSEEAHDDRVRLQAGRVWIIDPLDGTREFSTAGRTDWAVHIALWQRTTGGVADGRREITDAAVALPARGNRVYRSDTVTAGAVTGGVPNILRIAVSATRPPTILHRIRQKLAIEPVAIGSAGAKAMAVVDGDVDAYLHVGGQWEWDSAAPAGVVLAAGMHASRLDGSPLRYNQLDPYLPDFVMCRADIAPILLGVIREVWQ | Function: Phosphatase with a broad specificity. Its primary physiological function is to dephosphorylate 3'-phosphoadenosine 5'-phosphate (PAP) and 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Thus, plays a role in mycobacterial sulfur metabolism, since it can serve as a key regulator of the sulfate assimilation pathw... |
Q85AI0 | MSQLIFIPLLISLLVTKGKIRFLNNFESVLALSLHYGILVLALPIFILLYKAKKQPCSILLKVTTEPIILSAYATTFSTAFLAITINALFGLIIAWILVKYEFTGKETLDAIVDLPFALPASVGGLTLMTVYSDRGWMGPICSGLGLKIVFSRLGVPMATIFVSLPFVVRTIQPVLQDVEEELEEAAWCIGASPWTTFCQISLPLLTPSLLTGTALGFSRAIGEYGSIVLIACNIPMKDLVISVLIFQKLEQYDYQGAIVVATIVLIASFGGLLIINKVQLWKQNLSK | Function: Part of the ABC transporter complex cysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31474
Sequence Length: 288
Subcellular Location... |
A2CI71 | MSTNEMNQKKRLNRSGSLSSHLTRSWPWQLTLSYLFFMLILPVIALLSRASDELFKDFWQIAAEPVAISTYVVTLMTALFATLINGFFGVIIAWVLVRYNFPGKRIIDAAIDLPFALPTSVAGLTLATVYSDQGWIGHLFESIGIKVAFTRVGVAVAMIFVSFPFVVRTLQPVLVEIDQELEEAAWSLGASTWRTFWRVIFPPLTPAIVTGVALAFSRAIGEYGSVVIVASNIPFKDLTAPVLIFQRLEQYDYTGATIIGTVILSISLFLLFGINFIQSLNQLYVK | Function: Part of the ABC transporter complex cysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31812
Sequence Length: 286
Subcellular Location... |
C0HL14 | GVFCGEACAQASCSIAGCECIAGLCYKN | Function: Probably participates in a plant defense mechanism.
PTM: This is a cyclic peptide.
Sequence Mass (Da): 2772
Sequence Length: 28
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
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Q7XI14 | MARRAAAGLLRRHLGPLAAGETLQARGMYPKQYGAANHAFSRFYSIQGQQRSLYGFRTNVETDDTQQSARMNFEVQKRSFSSAAAHVQRNPAYSVLNSDDVSYFKSILGDSGVVQDEDRVSVANMDWMGKYKGSSQLLLLPKSTAEVSKILSYCNSRRLAVVPQGGNTGLVGGSVPVYDEVIISLGGMDKIITFDNVNGILTCEAGCVLENLSSYVENKGFIMPLDLGAKGSCHIGGNISTNAGGLRFIRYGSLHGSVLGLEVVLADGTVLDMLTTLRKDNTGYDLKHLFIGSEGSLGIVTKIAILTPAKLPSTNVAFLS... | Cofactor: Binds 1 FAD per monomer.
Function: Catalyzes the oxidation of D-2-hydroxyglutarate to alpha-ketoglutarate.
Catalytic Activity: (R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 61097
Sequence Length: 559
Subcellular Location: Mitochondrion
EC: 1.1.99.39
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Q88EH0 | MIAQLSTVAPSANYPEFLEALRNSGFRGQISADYATRTVLATDNSIYQRLPQAAVFPLDADDVARVATLMGEPRFQQVKLTPRGGGTGTNGQSLTDGIVVDLSRHMNNILEINVEERWVRVQAGTVKDQLNAALKPHGLFFAPELSTSNRATVGGMINTDASGQGSCTYGKTRDHVLELHSVLLGGERLHSLPIDDAALEQACAAPGRVGEVYRMAREIQETQAELIETTFPKLNRCLTGYDLAHLRDEQGRFNLNSVLCGAEGSLGYVVEAKLNVLPIPKYAVLVNVRYTSFMDALRDANALMAHKPLSIETVDSKVLM... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Catalyzes the oxidation of D-2-hydroxyglutarate (D-2-HGA) to 2-oxoglutarate (Probable). Is involved in a D-lysine catabolic pathway .
Catalytic Activity: (R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 110945
Sequence Length: 1006
Pathway: Amino-acid d... |
P84850 | MVLHLVPRWSASLFRASPRWKKTYSQRASAQLKWLGCPRSVYSPLACRAYSKVSGSPEVMLTPERYPVQRLPFSTVSEEDLAAFECIIPGRVITDPEQLQTCNVDWLRTVRGCSKVLLRPQTSEEVSQILRHCYKRNLAVNPQGGNTGMVGGSVPVFDEVILSTALMNQVISFHDVSGILVCQAGCVLEELSRYVQERDFIMPLDLGAKGSCHIGGNVATNAGGLRFLRYGSLRGTVLGLEVVLADGTILNCLTSLRKDNTGYDLKQMFIGSEGTLGVITAVSIVCPPRPKAVNVAFLGCPGFTEVLQTFRTCKGQLGEI... | Function: Catalyzes the oxidation of D-2-hydroxyglutarate (D-2-HG) to alpha-ketoglutarate . Also catalyzes the oxidation of other D-2-hydroxyacids, such as D-malate (D-MAL) and D-lactate (D-LAC) . Exhibits high activities towards D-2-HG and D-MAL but a very weak activity towards D-LAC (By similarity).
Catalytic Activit... |
A4VGK4 | MTDPALIDELKTLVEPGKVLTDADSLNAYGKDWTKHFAPAPSAIVFPKSIEQVQAIVRWANAHKVALVPSGGRTGLSAAAVAANGEVVVSFDYMNQILEFNEMDRTAVCQPGVVTAQLQQFAEDKGLYYPVDFASAGSSQIGGNIGTNAGGIKVIRYGMTRNWVAGMKVVTGKGDLLELNKDLIKNATGYDLRQLFIGAEGTLGFVVEATMRLERQPTNLTALVLGTPDFDSIMPVLHAFQDKLDLTAFEFFSDKALAKVLGRGDVPAPFETDCPFYALLEFEATTEERAEQALATFEHCVEQGWVLDGVMSQSEQQLQN... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the dehydrogenation of (R)-2-hydroxyglutarate (D-2-hydroxyglutarate or D-2-HG) to 2-oxoglutarate and of (R)-malate (D-malate) to oxaloacetate. Is functionally tied to L-serine biosynthesis, via its coupling with the D-3-phosphoglycerate dehydrogenase SerA, encoded ... |
P0DV35 | MTDPRILSLQQAVPALRLKTEPADLEHYGRDWTRRWTPNPLAIALPGSVEEVQAVVRWANAQAVAVVPSGGRTGLSGGAVAANGELVLSLERLNKPLDFNAVDRTLTVQAGMPLEAVHNAAREQGLVYPVDFAARGSCSIGGNIATNAGGIRVIRYGNTREWVAGLKVVTGSGELLELNNALVKNSSGYDFRHLMIGSEGTLGIVVEATLRLTDPPPPSNVMLLALPSFDVLMQVFAAFRAQLRLEAFEFFTDRALEHVLAHGAQAPFAEIHPYYVVTEFAAGDEAQEAAAMAAFETCMEQGWVSDGVISQSDAQAAQLW... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the dehydrogenation of (R)-2-hydroxyglutarate (D-2-hydroxyglutarate) to 2-oxoglutarate. Has also a low activity on D-malate in vitro . Is functionally tied to L-serine biosynthesis, via its coupling with the D-3-phosphoglycerate dehydrogenase SerA, encoded by the a... |
Q8MPP3 | MFSKYVLATLLALFAQSMCIQELSLPPEGSHSTAATRSKKAKTAISEDIMYNYLMQFDYLPKSDLETGALRTEDQLKEAIRSLQSFGNITVTGEIDSATARLIQKPRCGVGDRRSADSFSPDNLYHEIGSNVRVRRFALQGPKWSRTDLTWSMVNRSMPDASKVERMVQTALDVWANHSKLTFREVYSDQADIQILFARRAHGDGYKFDGPGQVLAHAFYPGEGRGGDAHFDADETWNFDGESDDSHGTNFLNVALHELGHSLGLAHSAIPDAVMFPWYQNNEVAGNLPDDDRYGIQQLYGTKEKTWGPYKPQTTTTTTT... | Function: Has metalloproteinase activity . Required for larval tissue histolysis during metamorphosis and is involved in pupal head eversion and fusion of the wing imaginal tissue . Required for growth of the dorsal air sac primordium and development of the dorsal air sacs . Promotes embryonic motor axon fasciculation ... |
O34688 | MGITSVLTKDNVKKIDTDIDVQERDLNVFITSASRVIAPLWPISTFAARNPWMGLENQPFDQVASWLKNTRDVDIYPSASMIRSAKNKGEIDEDFVEMGLQRWLDSHSYHIPRDVAERFCHAALKLDPLPSDLLSSHELEKLVSECSGLDHIENVFMQPLSSYIENQDGERLVNILDHHVIKWSKLYLDDSQAGWTMPNREEGFYRAWQHLIQYDPALSKKQRERVKGWPKEAHLALQEALFALEIPESEIQTYLEGHLLSLPGWAGMMLWRSQQSSHEHALLTEYLAVRISMEWALIKPYLPLTNERSKKTISIAPLIA... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 98767
Sequence Length: 871
Subcellular Location: Cell membrane
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A9WCK3 | MTMIETQLRSLLVTTKPIRDLTIDAVIAATKRAEQRIAPLWPLRYFVAVNPYLGLIDHTFADAAQLLARRTDARMTAPRDFYAQAIKSGRITDADLAAAIADEKLPSPAPASVAALKEFAFSKDPDPATTPLPTIADVATTVTGINWADFVTDAISTWAGAYFDLGQSYWRSPWAQLPAYAAWRAEAAHDRTAQARGVHGMRRALRELPETALETIVTAVKMLNIPEQGLEAYLHRLLLTIHGWASYARYLRWDAELYGGEDHTLTDLLAIRLVWEVALWHSFADRGVAEAWHKCKPELSNEQLTETARYALAGNILLQR... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 92482
Sequence Length: 838
Subcellular Location: Cell membrane
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Q7NT42 | MAAIAPAWPLDSLVASSPYWGLREQSFSQAADTLRLVADSPLHLPRGEYLAAWRRGEISAAALETALSETGWTGGAQAWLDAEPRDVDPVPPPRLLAACHREAAGPLSAQSWTDVVIQQISQYCAAWFDRDQANWHLDHERGFYAAWLEQMRHPYGLSALPERREQLRLRAERLPGDAEAMLAAGLAQLQAEPEWLKPWLQALLMRNNGWAAWCAYLGWQAGLKGETDGHLRQLLAIQMAWECLLDDGARGPDSAWAAWHRDWGLRLHGRADPRTLIWQRAHELSLHAPLAQALCRESAAEDGTRPAMQAVFCIDVRSEP... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84575
Sequence Length: 776
Subcellular Location: Cell inner membrane
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Q47IK9 | MSAAHELPIRERLAHWVEHLTHVLPAQAPIRDFVHHNTLHGFQHLPFTEALASAQALTGATTYWPESRFRECLASGRISPDDLSAALDDFGVGDLDQPVVRNLTRRDILLASLRFGCEAPNACRQAWLLDETSLADDPLFAYFCRSVELAPSKGASENWQVQALARWDALCGRVGRTWTWRALLEYLSGEDVLEWTRSILQRHLAAHLDLGVAAWRNPAQGQGFFAAWRASAGLDMAWEMDELPNARDEILHLPDSPLDVLLEELPRLVPDHSQWYGYLERLSLELPGWSGMFLWRDRNPGRGDGTPIAMLDYLTVRVLL... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 111281
Sequence Length: 1012
Subcellular Location: Cell inner membrane
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Q5L2V2 | MSRSVISLERSTEAKKAAACPLEVIVSEAAKVIAPLWPISAFIARHPWMGMEDKSFVDAADRLQEAYGIDLYPPMAVFHAALSKGEIDVSFIERRLQRWLDDEPLPAPRHEAERLCRALLWNDAVPEEALQMPKLIELAAAMPLRSVSIRTRSVRLGLEKRLDQQMIKWCKLFYDRGEAVWALPHREHGFYGSWRRLAPLDPSLSKEERKRLFDWPHHPEEALQRALEQLGVQDEEAVAYLEAHLLALPGWAGMMVWQSRRAGDEIGGLINYLAVRLSLEWVFTAPHLPLKEEENEDDRAVGPLLAAWIHWGGMTLDDWR... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 97317
Sequence Length: 870
Subcellular Location: Cell membrane
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Q18H12 | MTTESTSESKTKTETETETETEQRNDLSNSSNSSEDASCPGSSPVSTESDPDNDDTSVSANTIVRQYIESAAESVGALWPIHSFVTANPLSGFEDQPFHKAVAAGATRFGGDGYPDSDVFEHAWKTGQINQEILKKTLDEYETDHTPASAIAAIDSGTQATSGRDTGVRMGTGVDDEINNWDEIDKRVIKWLSAFLDAGSAEWEMPNRGSGFYTAFQSVATYDTMIPDTDLIEDPPADPIDAVSTVLASYPRSQWSEIIEAQITALPGWTGLICYRTENETAWQTAYPITLVGYLAARMMLADALSIPLDSISRPAHSVT... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 102008
Sequence Length: 931
Subcellular Location: Cell membrane
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Q31HC3 | MMLHNAKASDNNELDQAKPLIPQLSDKQKEALNDACGRIAPTWPLDELIAVNPWWEMRDQHISKVSAKLSALSQAQCVMPKSYFQEVWMETLQPQHVQQAIDEMEKDYTVDNLERYLLEEDEHTHWHNVSDFVDSGRDRKYKMAWRDEITHQISQFCADFFRLKDSQGTFSKTYQGLYHEWLATTRQDKGIEILMGEDGLTEHFMDLPESSESLLAEALVGLRVPDSQIADYAHALLLDANGWASWVAYLRWQDRLSNAENDLMMDFLAIRVAWEWVLWQHQKDSDRSVFNELKVMWHHQMSILPDLIATHEAAQAKSWI... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 93448
Sequence Length: 823
Subcellular Location: Cell inner membrane
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B4U7X3 | MVKAYLDNVRKYIPHYWPMTTFVHHNPLHGFEDMPFKEALKQASKLYKAKVYMDPDYYVELYKEGIIKRDILEKNLFEFLKSIGLQMYFAESKKFITEISQDWKYYKVKSSTTPDINLIDYFNQKIVKDEDTLFQELIEDMMLSEILDAILEDNTTDIIEKEILEFVARFLDEGQTTMSMPEREKGMFGAFKLYEGLNTSLNEEEYADTILHELSPKNVERYILNHLLKDFGWAAFIKYREDNEDYYFQQIHPASLLEYLAVRLHYEKKYLNHYPISNFVELQKAFEQNKTLFVLKLLKAKNILPSKYIDRLEEKDSPKA... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 112277
Sequence Length: 961
Subcellular Location: Cell inner membrane
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Q5R077 | MSTANRLATIAGQVSKAIAPQWPLSQWIAVNPFWHYRQQPVAGVAAHWRYSAGTRLLMSPDFYWQQWQQNRIDAALVTNKMVNELEQRSLLKAQLPQWRNLSRLVDKYTRRRRKMRWNDEVVLQISQTCGLFMQFPTRFQQAGKDSSLYQHWLTISRADRGIETLMDEAELTELFAQLPDDPHKLIQVCHDNFLSDASDYALRCYSQALISDLWGWAAAFSYQDARQDSQWVFELLCIRLAWEYILWQLAERTNTKVYQQLQQALSAQVENCEGQVAHIEQHNSLLWQWQAAYERSQLNRLQFKSDTVEESNAPDVQAVF... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 85144
Sequence Length: 757
Subcellular Location: Cell inner membrane
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Q28SY7 | MTTVHDLSSDTMTTAADRAARAIPPVWPLASSVAVNPFLGQTEEHLAQVSARLGRIGNVPVTMPPAHYAALIEDGTITDDDIASASAASRIDNAPDLAEIKRSAAVPFDRPEPHSTIADLAARMSGIDWPGILADRFGHWASGFFDQGQALWAAPRRRGAYDAWRQTATHDLTPEITGLTGFAQFVSETPDTAQEARLRAAKRLGLDDDMLETYLHQLLFSLGGWAQVARYHLWQAELSQTTDETIADLLTIRLLWEEALFLQYEDRIGDRWEATKTAHAQPVTPQRGEIINAILQEAWEHAVQRDLASTIAAPSPERGE... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 86623
Sequence Length: 801
Subcellular Location: Cell inner membrane
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Q9HTQ0 | MRVLVLGSGVIGTASAYYLARAGFEVVVVDRQDGPALETSFANAGQVSPGYASPWAAPGIPLKAMKWLLEKHAPLAIKLTSDPSQYAWMLQMLRNCTAERYAVNKERMVRLSEYSRDCLDELRAETGIAYEGRTLGTTQLFRTQAQLDAAGKDIAVLERSGVPYEVLDRDGIARVEPALAKVADKLVGALRLPNDQTGDCQLFTTRLAEMAKGLGVEFRFGQNIERLDFAGDRINGVLVNGELLTADHYVLALGSYSPQLLKPLGIKAPVYPLKGYSLTVPITNPEMAPTSTILDETYKVAITRFDQRIRVGGMAEIAGF... | Function: Catalyzes the oxidative deamination of D-amino acids. Has very broad substrate specificity; all the D-amino acids tested can be used as the substrate except D-Glu and D-Gln. Participates in the utilization of several D-amino acids as the sole source of nitrogen, i.e. D-alanine, D-histidine, D-phenylalanine, D... |
Q8TRA4 | MADIIIKNAYVLTMDPDAGDLKNGTVVIEDGKITEIGENTKENADTVIDAKGSVVMPGLANTHTHAAMTLFRGYADDLQLAEWLEKHIWPAEAQLKAEDVYKGSLLACLEMIKSGTTSFADMYFYMDETAKAVEASGLRASLSHGLIELWNEEKGEADLKEGKRFVRAWQGAADGRIKTMYGPHAPNTCSEEFLTKVKEEAHRDGAGLHIHVLETEAELNAMKERYGKCSVHLLEDIGFFGPDVLAAHCVWLSDGDIEILRQREVNVSHNPISNMKLASGIAPVYKMLEKGVNVTLGTDGCASNNNLDLFEEIKTAALLH... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine... |
Q2FRU6 | MADPKDISPCKNEDLFLKCRSTLITGVLLPDKTRSDIWYDETGTIRTCGPDIARNHRNEADIILDGSGFLAMPGLINTHTHAAMTLLRGYADDMHLQQWLSEKIWPLEAHLTGEHVYWGTKLACLEMIRSGTIAFNDMYFYMKDAARAVQESGIRAVLSHGIITFGDEAKMEAELKATEDLVHHVRSLNTSLITSAIAPHAPYTVPPQHLEVCADYSQKEKIIIHTHLAETKQEVDDCQKSYGMTPAALLDKTGCLTERTVAAHGCWLSEDDCRLLAERRVSVAHNPVSNMKLATGRAMPYHWLKDQGVNVCLGTDGCSS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine... |
Q58936 | MILIKNVFVNGKRQDILIEGNKIKKIGEVKKEEIENAEIIDGKNKIAIPGLINTHTHIPMTLFRGVADDLPLMEWLNNYIWPMEAKLNEEIVYWGTLLGCIEMIRSGTTTFNDMYFFLEGIAKAVDESGMRAVLAYGMIDLFDEERRERELKNAEKYINYINSLNNSRIMPALGPHAPYTCSKELLMEVNNLAKKYNVPIHIHLNETLDEIKMVKEKTGMEPFIYLNSFGFFDDVRAIAAHCVHLTDEEIKIMKQKNINVSHNPISNLKLASGVAPIPKLLAEGINVTLGTDGCGSNNNLNLFEEIKVSAILHKGVNLNP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine... |
Q8TYD4 | MRLAILGGIAVTPERVIEDAGILIDEDGRISFVDTREQLEECEDWEDEIELGEKDVIMPGLINTHTHGPMTLFRGVADDMPLMKWLREEIWPLEERLDAEKCRWGAALAAMEALKSGTTCLADMYFFMDAVAEAYAEVGIRAVISHGMIDLGEEDKREEELKESKRVYRKCQGMEGLIEFSLGPHAPYTCSEELLKEVRRLADEWGVKIQIHVAETEDEVKEVKRKHGKRPVEYLDEIGLLGDDVIAAHCVWLDDKEIEILSKRGVIVSHNPISNMKLASGISPVPEMLERGVNVTIGTDGCASNNNLDMLEEIKVAALL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine... |
Q18T09 | MAQINENYLKLPGSYLFSEIARRVNEFKVQNPDADIIRLGIGDVTRPLAPVVVEAMKQAVEEMGRAETFRGYGPEQGYDFLIEKIIANDYAPRGVQLGMDEVFVSDGAKSDTANFQEIFGVDNIMAVTDPVYPVYVDSNVMAGRTGNYDTEKGQYGRIIYLPCTEEGDMKPELPTAPVDMIYLCFPNNPTGMTLTKEELKVWVDYARENKAIILFDSAYEAFIREEGVPRSIYEVEGAREVAVEFRSFSKTAGFTGTRCAYTVVPKDIMIYDSTGEGHSLNKLWLRRQTTKFNGVSYPVQAGAAAVYTEEGKKQIQATID... | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate. Is also able to catalyze the reverse reaction in vitro, i.e. the transamination of LL-diaminopimelate w... |
Q6AL81 | MITINENYLKLQASYLFSDIAKRVATFQEENPEKEVIKLGIGDVTRGLTPSVIAAFHQAVDEMANDSTFHGYGPEQGYAFLREAIAENDFQSRGAGIVADEIFVSDGAKCDTSNIQEIFSAETKIAIPDPVYPVYLDTNVMAGRTGLFADGRYQNIVYLDSTKENNFVPELPTEKVDLIYLCFPNNPTGSTITKAGLKRWVDYAIENKALILFDAAYEAFIQDDTLPKSIYEIEGADKVAIEFRSFSKNAGFTGTRCAYTVVPKACMAYDSEGNSHSLHSMWNRRHCTKFNGVSYPIQRAAAATYTPEGKAECKELIDYY... | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolin... |
B8DJJ6 | MADFKLADRLATLPPYLFAGIDKVKAEVAARGVDIISLGIGDPDMPTPDFIIEAMKKAVERPANHQYPSYVGMLEFRQEVANWYGRRFGVSLDPKTEVIGLIGSKEGIAHFPLAFVNPGDLVLVCTPNYPVYHIATGFVGGEVQFIPLVEENDYLPDLDAIPAATWDRAKMIFVNYPNNPTAATAPRAFYEKLIGICRKHNVIIAHDTAYTEVYYDENDKPMSILEVEGAKDVTIEFHSLSKTYNMTGWRVGMAVGNASLVAGLGKVKENVDSGIFQAVQEASIVALRDGDDFCRELRGIYRKRRDVVVAALNKVGIACR... | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolin... |
Q7NDX4 | MKTAARLDRIPPYLFAEIDRRRDEAVARGVDIINMGIGDPDKPTPPVVLEAMHAAIDDPSTHNYPPYKGTKAYREAAAAWFERRFGVGGFHPDTEVISSIGSKEAIHNTFLAFVDPGDYTLIPDPAYPVYRTSTIFAGGEFFAMPLLPENQLLPDLEAVPETVARKAKLLWLNYPNNPTGAVASLEFFEKVVHFAKKHDILVCHDNAYSEMAYDGYKPPSILQVPGARDVAIEFLSCSKAYNMTGWRVGFVIGNRTGIAGLGQVKTNIDSGVFKAIQQAAIAAFGLDDERLHALMAVYQNRRNIIVEGLRSLGWPLEAPK... | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate. Can also use m-DAP instead of LL-DAP as the amino-group donor.
Catalytic Activity: (2S,6S)-2,6-diaminoh... |
B8CX89 | MENADRIKNLPPYLFAEIDKMIARAKKEGVDVISFGIGDPDQPTPDNIINKMIEAVKDPSTHSYPSYEGMYEYRKTVADWYKNNYGRELDPDKEVVSLIGSKEGIAHLPFCYINPGDIALVPDPGYPVYKTSVLLAGGKPVQVPLVEENNFLPDLKAIDEDIARKAKLFFINYPNNPTGAIAPEEFYEELIDFADKYDIIIAHDAAYSEIGLDGYNPPSFMQFEGAKKVGIEFNSLSKPFNMTGWRVGWAVGRSDVIESLGRIKTNIDSGIFEAIQYAGIEALTGPEDNIEKMTELYSKRRDLLVEGLRELGWEVPVNKA... | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolin... |
Q8KC06 | MSNRLISGSAVALVTPFHQDGSIDFEAMRRLVRFHREAGTDIVLPCGTTGESPTLTNEEEAEIIRVVCEEAGESMMVAAGAGNNDTRHAIELARNAEKAGAQAILSVAPYYNKPSQEGYYQHFRHVAEAVSIPVIIYNVPGRTGSNVNAQTILRLARDIENVVAVKEASDNFEQIMTLIDERPENFSVMTGEDGLMLPFMALGGDGVISVAANQVPKVVKGLIDAMKAGNLEEARAINRKYRKLFRLNFIESNPVPVKYALSLMGMIEEVYRLPLVPMADANKAILRAELEKLSLV | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32386
Sequence Length: 296
Pathway: Ami... |
Q0TP55 | MFKGSCVALITPFTEDGVNYEELRKLLEWHIKNHTDAILVCGTTGEGSTMTLEEKKEVIKFSVEVVNKRVPVIAGTGTNNTKASIELSKYAEEVGADMVLIITPYYNKTSQKGLYAHFNAINDAINIPIMLYNVPSRTGMNITPLMLDKLADLNNVVAIKEASGDLSQVAKMAELCGDRIAIYSGNDDQIVPILSLGGAGVVSVLANILPEETHNICEKYFLGEVIESRNLQLKYLSLANSLFIETNPIPVKTAMNLMNFNCGPLRLPLCEMEDSNLVILEENLKANGLIK | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31925
Sequence Length: 291
Pathway: Ami... |
Q8RQM8 | MSTGLTAKTGVEHFGTVGVAMVTPFTESGDLDVAAGREIAAHLVDNGVDALILAGTTGESPTVTTAEKLTLLKAVREEVGDRAKLIAGAGTNNTRSSVELAEAFAEVGADGLLVVTPYYSKPSQEGLVRHFTEIAQATDLPICLYDIPGRSGIPIESDTIRRLSELPTILAMKDAKGDVVAAAPLIEETGLAWYSGDDPLNLVWLALGGSGFISVIGHAAPNALRELYTSFEEGDLARAREINATLSPLVAAQGRLGGVSMAKAALRLQGINVGDPRLPIVAPNEQELEDLRADMKKAGVL | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31451
Sequence Length: 301
Pathway: Ami... |
A9KFS0 | MFNGSLVALVTPMQENGEIDYSNLKELVEWHLENDTDGLVILGTTGESPTITAEERHKIIRQVVDQVNKKIPIIVGTGANSTVHTIEMTQQAMELGADAALIVTPYYNKPTQEGLFQYFKTIAEAVPIAQILYNVPSRTACDLLPETVIRIAKCSNVVGLKEATGDIQRVKQLKAEDLDLLSGDDKTAMDFMLAGGKGVISVVANVVPKPYHAFCITAVSGNVELAKKENDQLSPLYDSLFVESNPIPVKWALSQMGVIPKGIRLPLTPLSERYHAKVRESLQQVGIKC | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31613
Sequence Length: 289
Pathway: Ami... |
C0QT41 | MFKGSIVALITPFKDGAIDRKSLKRLIDFHVEKGTDGIVIAGTTGESATLTFSEHEDLIKMAVEFADKRIPIIAGTGANATHEAIALTKSAEKAGADGSLQIVPYYNKPTQEGIYQHFKAIAEETSIPLILYNIPSRTGVDMLPETFARLYSDFPNVIGIKEATGNVARVSEMISLTNPDVVILSGDDALTLPMMAVGAKGVISVANNLVPEDIATMCRLALEGRFEEARQIHDRYWKLFKTLFIETNPIPVKTAAYLMGLIDDIEMRLPLYYMKPENEEKLKSVLKDYGLIR | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32295
Sequence Length: 293
Pathway: Ami... |
A6L5G7 | MIQTRLKGMGVALITPFKEDDSVDYDALLRLVDYQLQNGTDFLCVLGTTAETPTLTKEEKDKIKRLIIERVNGRIPILLGVSSNCTRAVVETLKNDDMTGVDAVLVAVPYYNKPSQEGIYQHYKAIAEATDLPVVLYNVPGRTGVNMTAETTLRLARDFKNIIAIKEASGNITQMDDIIKNKPANFDVISGDDGITFPLITLGAVGVISVIGNAFPREFSRMTRLALQGDFANALTIHHKFTELFSLLFVDGNPAGVKAMLNVMGLIENKLRLPLVPTRITTFEKMRAILNELKIKC | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32787
Sequence Length: 297
Pathway: Ami... |
A4SX51 | MTNKAHSQGSKKTIQGSMPAIVTPMFEDGSLDYPGLRALLDWHVSEGSDGIVIVGTSGESPTVSVEEHCELIRVTVEQIAGRIPVIAGTGGNSTQEAIELTHFAKKVGADASLQVVPYYNKPTQEGMYAHFKKIAESVDLPVILYNVPGRTVADMAGDTVVRLAGVPGIIGIKDATGSLERGTLLINDLKRAGHHEFSVFSGDDLTAAMLMLMGGHGNISVTANVAPRLMHELCVAAMSDDVKRTREIQYQLIAVHKAMFIEANPIPVKWALHEMGKITAGIRLPLTPLSSSLREPLKAALKQANLL | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32877
Sequence Length: 307
Pathway: Ami... |
B2RMB9 | MDRAQLRGMGVALITPFDEKGEVDHESLRLLADYQVAGGADYIVALGTTGESPTIEEAERSAILQTVREAVAGRCPIIVGAGGNYTERLVNRIQAMDKTGVDAILSVAPYYNKPTQEGIYRHYRTLAESTDTSIILYNVPGRTGVNIKSETTLRLATDCPNIIGIKEASGNVDQVRAIVLEKPDPFIVLSGDDHLSLSFIKEGAEGVISVIGNAYPELFSRLIHLCLENRFEEAETIQQRLEGMCYLMFVDGNPAGIKELLYQKGLIRHNILRLPLVSASDSTSTLIARVRNQIEQR | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32617
Sequence Length: 297
Pathway: Ami... |
A2BZ39 | MIPNNTQFSNPIFGRILTAMVTPFKENGGVDYELAIKLANHLCENGSDGIVLCGTTGESPTLSWDEQHNLFVAVKSSLNSRSKVIVGTGSNCTSEAIEATKKAYEFGADGALVVVPYYNKPPQEGLYNHFSSIATAASDLPLMLYNIPGRTGCNLLPTTVNKLMNFPNILSIKAASGRIEEVTELRAACGPKLFIYSGDDSLLLPMLSVGAVGVVSVASHIVGLQLKMMIESFQKGEFSIALDIHEKLQPLFKALFETTNPIPIKAALELTGWQVGSPRNPLTPLIKEKKDNLFQIIQNLSL | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32683
Sequence Length: 302
Pathway: Ami... |
P49423 | MSTVPEISSAPFGRLLTAMVTPFDTAGAVDFALAARLARYLVDQGSDGLIVCGTTGESPTLSWEEQYQLLETVRNAVNGSAKVLAGTGSNSTSEAIHATAKAAEAGADGALVVVPYYNKPPQAGLESHFRAVAQAAPDLPLMLYNIPGRTGCSISPITVQRLMNCSNIVSFKAASGTTNEVTDLRIRCGSRLAIYSGDDGLLLPMLSVGAVGVVSVASHIVGMRLKAMIEAYFAGENSLALSHHEQLQPLFKALFATTNPIPVKAALELIGWPVGAPRSPLLPLENQMKNELMKTISALLQT | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31764
Sequence Length: 302
Pathway: Ami... |
B9JYQ3 | MKLVVVGVSGRMGQALVRIICETQGAVLHAAVGRPGSASIGRDAGDLAGVGPLGVPVTDDALAAFVNADGVIDFTRPETSVEFSALAAQARIVHIIGTTGCSPADEARFEAAARHARIVKSGNMSLGVNLLSVLVAQAAKALEASGWDIEVLEMHHKHKVDAPSGTALLLGEAAAKGRGIDLTEKAVKVRDGHTGPREPGSIGFATLRGGSVIGEHSVLLAGEGEIVTLSHSAGDRSIFARGAVKAALWAQDKKPGLYSMLDVLGLSSPH | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 27636
Sequence Length: 270
Pathway: Amino-acid biosynthesis;... |
Q5PA93 | MKIGIVGCLGRMGRIIVQEVVGTGGVELSGGVVRRGNGLVGEDMGAVLGCGHGAKITDSKEFLFDCSDVVIDFSSPECMLECVGIASEKRVPLVSGTTGVDERDFRTHAEKVPLLWSCNMSLGVTLLLELVKMAAAGFRGYDVEIRELHHRAKKDAPSGTSLMLGKAVAQGMGVELESQQHTFGSGCRRSGAVGFSVARGGGVIGDHAVMFLGDDEIVELQHRAIDRRVFARGAIKAACWLVGKPAGLYTMSDVLRA | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 27190
Sequence Length: 257
Pathway: Amino-acid biosynthesis;... |
O67061 | MSVRVVVCGALGRMGRRIIELALQDKDVEVVGGVEHPDCVPSIDLGEALGKEELKGKPLTSRLEELLPYTDVVIEFSGNPTAAVGHAELTTLEKKAIVIGTTGFTKQEIEQIKEFSKNAPVLLSPNMSLGVNLLFKLAEIAAKVLKDKNFDAEIMEIHHRFKKDAPSGTAMKLAEILSETLEKKNLVFGRKGEAPRKEDEIGVMALRGGDVVGDHTVYFLGFGERIELTHRATSRDTFAKGAVEAAKWIKGKEPGFYTMFDVLGL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 28961
Sequence Length: 265
Pathway: Amino-acid biosynthesis;... |
O29353 | MRVAVSGAAGRMGRLVVKNAVAEGLKVVQAFDINEVGKDAGELAGVGKIGVPIEDDISKLDADVLIDFTTAEAAMKNAEVAAEKGVRVVMGTTGFTDEDRKRLAELAEKVPMIVSPNFSLGVNIFWKIVEYAAKMLYEWDAEIVELHHRHKRDSPSGTALKLAEIIRKVKEEKGIEADLKTCREGISPRESEIGVFGIRGGDVVGEHTVFFFGSGERIELTHRAMSRECFAIGAVRAAKWIAKVDKPGFYTMDDFLE | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 28096
Sequence Length: 257
Pathway: Amino-acid biosynthesis;... |
Q96VT7 | MSSPRPSTSSTSSDSGLSVDTTAYPEESKYTSTAPGAGGLSDENRYRDVEEGEAGADEPFLPSAKKQAASGSRTSRLIWGLVILCVAGWLWGLVLFVTQNRSAQQSVSEALQSHESGAISGSSSSGKPVTLEQVLTGQWLPRSHAVSWIAGPNGEDGLLVEQGEDQGKGYLRVDDIRSRKGDATSQESRVLMEKAIVQVDGRTIFPVSTWPSPNLNKVLLLSEREKNWRHSFTGKYWIFDVATQTAQPLDPSNPDGRVQLAIWSPTSDMVAFVRDNNLYLRRLSSKEVVPITKDGGADLFYGIPDWVYEEEVFSGNSVTW... | Function: Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Catalytic Activity: Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided ... |
Q3Z7V5 | MTPIKVVVHGASGKMGQEVLKTLCQENNLLPVGAVDIRAKSPALPLPDGSGSIPYSADLSSVLSQTKPDVMVDFTIAKASMPAIRIAAAHKVNLVIGTTGFSPEEISEIEQLAKTNDIGIIVAPNFALGAIIMVHLAQEASRFLASAEVIELHHDKKLDSPSGTALATAAAMLKTRGEAFNKPAKENMSDARGQEHDGIRVHSVRLPGLLAHQEVIFGAAGQSLTIRHDAFSRECYMPGVVLAIKEIVQTKGFVFGLDKLLKL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 27943
Sequence Length: 263
Pathway: Amino-acid biosynthesis;... |
Q6AR64 | MTKVIIAGASGRMGQRVAHMVEAHPELEYAAAFEAAGNPAIGKDIGRIVFGEENGVIVGEGLESVIADGDVIIDFTFHTATMEFARIAAKHGKAMVIGTTGLSVDELAELKDLSASFPCVQAPNMSVCVNVLFKLAKKTAAILGDDYDIEILEAHHNKKKDAPSGTALKLAEMAAEGVGRNLAEVGVYERNGIIGERDPKEIGIQTLRAADIVGEHTIYFAGAGERLEISHRAHSRDHFAKGAATAAAWLVGRENGIYDMFDVLGLQDL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 28623
Sequence Length: 269
Pathway: Amino-acid biosynthesis;... |
Q72BM6 | MSTPIIVMGAGGRMGSTICRLVQEEPQLCLAAVLERPDRASGVARDGCIAGSDPDVVFPQVPGGVIIDFTAPEASMATARAAARHGNAVVIGTTGFNEEQKAELAELARQIRLFWAPNMSVGVNVLLKVLPELVRLLGEKYDLEMVELHHNRKKDSPSGTALRLAECLAEARDWNLPDVACYHREGIIGERPQKEIGVQTIRGGDVVGVHTVYCLGPGERIEVTHQAHSRETFAQGALRAAAWLATQKPGKLYNMADIF | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 27984
Sequence Length: 259
Pathway: Amino-acid biosynthesis;... |
B8E2S7 | MIKTVLFGACGKMGKVIGKALIDATDIELVGAIDPYFKGEKYEKIIGIDKISLEVVESIDELQEDFDVAIDFTNAEAAYQNIKKVLQKGKRMVVGTTGLTQEMMEEFKDLAVKNKTAILIAPNFALGAVLMIQLAKQVVKYFPDVEIIELHHNEKADAPSGTAILTAEVLREEMKKYNLTHKDATKIEKLPGARGGKLDSINIHSVRLPGLVAHQEVIFGGLGQTLSIRHDALSRECYIPGVLMAVREIVKREGFFYGLESFLNREEA | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 29649
Sequence Length: 268
Pathway: Amino-acid biosynthesis;... |
Q3IKQ7 | MTKNKIGVFGANGRMGSALLEAASTKEHSELAAAYVRSSSPLLGINVNQLNSAADKTVTFSDEANITNVDVLIDFTLPAGMRTHLQTAVKQGVPMVIGTTGLNEADMTLLHEAANHIPIVFARNYSVGVNVLLNLVQTAATKFGDDMDIEIFEAHHRHKIDAPSGTALAIGEAIADAKGWDHDKVAVYDRSKVEQAKSQNEIGYSVLRGGDIVGEHTAYFATMGERLELTHKASSRMTFALGAIRAAGWLINKPAGLYDMQDVLDLK | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 28675
Sequence Length: 267
Pathway: Amino-acid biosynthesis;... |
Q7UJD7 | MADSTGPISLTVHGAAGRMGRRVVALGLADPNFQLVGAIDHAKSDHLGQDSGAVAGEAPSGIEISSHWPVLDDAATNQAVIDFSLPEAIDGCVEHCVKVGSPLVVATTGLSDEQKQNLSEAAASIPVVWAPSMSLAVNLSMKIAEQITAALKDVAGGLDVEILERHHRFKADAPSGTALKFGELIAGQLGESTSHVHGREGHTGARTREEIGYHAIRVGDNPGEHTIVFGMLGEKIELNVAASNRDCYASGALAAAKWLIHQKKGPGLYSMFDVLGMSDN | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 29223
Sequence Length: 280
Pathway: Amino-acid biosynthesis;... |
Q9X9V6 | MTDTTAPRTSGAVAAGLATIAADGTVLDTWFPAPELSDEPGPSGTERLTAEQAAELLGGGATAAVGPDARRGVEVVAVRTVISSLDEKPVDTHDVYLRLHLLSHRLVKPHGQSLDGIFAHLANVAWTSLGPVAVDDIEKVRLNARAEGLHLQVTSIDKFPRMTDYVAPKGVRIADADRVRLGAHLSAGTTVMHEGFVNFNAGTLGTSMVEGRISAGVVVGDGSDIGGGASTMGTLSGGGNVRIVIGERCLVGAEAGVGIALGDECVVEAGLYVTAGTRVTMPDGQVVKARELSGASNILFRRNSVTGTVEARPNNAVWGG... | Function: Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA
Sequence Mass (Da): 33932
Sequence Length: 329... |
Q30RL0 | MEIIQTTEAFKALVQDIKTSINGYKEPLAFGVCRVDMGQLNLEKTLQATYPVINWNENFGSAAIFIKALQEQGVEIDFTQSEVICNINKAFLKSCLNAFSPYSEEAYGDAHKNIQVISALYNQIATSGSKDGEFKVTFIFADEPLKSVEATYLKLYALSQAKVEIRSINLNGAFGALPNVAWSNGKPLELDYLREFEIELKLANEYPHIEFVDKFPRFLQHIIPADNTRILDTSKVRFGAQLAAGTTVMPGASYVNFNAGTTGAVMVEGRISSSAVVGAGSDIGGGASILGVLSGTDGNPITIGKNTLLGANSTCGIPLG... | Function: Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA
Sequence Mass (Da): 43231
Sequence Length: 398... |
P56220 | MQQLQNVIESAFERRADITPANVDTVTREAVNQVIGLLDSGALRVAEKIDGQWVTHQWLKKAVLLSFRINDNKVMDGAETRYYDKVPMKFADYDEARFQKEGFRVVPPATVRQGAFIARNTVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRETGEIHYGRVPAGSVVVSGNLPSKDGSYSLYCAVIVKKVDAKTRGKVGINELLRTID | Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA
Sequence Mass (Da): 29887
Sequence Length: 274
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): s... |
B6J929 | MSETLNLLKQLIERPSITPNDAGCQTILIDRLKSVGFQCEHLPFGEVHNFWAWHGHQSPFIIFAGHTDVVPPGDETQWHSPPFTPTEKNGYIYGRGAADMKSGLAAMVVAAENFVKQNPDHNGTIGFIVTSDEEGPAENGTQKVVDYLQQKNIKLDYCIVGEASSNEKLGDAIKIGRRGSMHGELTIIGKQGHIAYPHLADNPIHRSFQAFEALAKTKWDEGNEHFTPTSFQFYNVEAGAGAANVIPATLKAKFNFRFAPIHTTQQLQQKVERILNYYQLNYDIQWNVSSQPFFSGNGRLATFVRQAIQEICHLNTEPNT... | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacteria... |
A5G1F7 | MAAARPFLKMHGAGNDFVVLDARAHPLDLAPAAAARIADRHRGVGCDQIILIERDDGAAAFMRILNADGSESGACGNATRCVAALLAGETGARRLTIRTNAGLLPAEIKGPTLVEVDMGAPKLGWEDIPLAEPADTLSLRLALGPVQNPAACSMGNPHATFFVDDLTHLQIETIGPKLEHARLFPERANIGFARIDAPDRIRLRVWERGAGLTLACGSGACAALVNAHRRGLAARRAEIEMDGGTLTLTWRDDGHVLMEGPVALVFEGELDAAMLAP | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 29251
Sequ... |
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