ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8EEN5 | MSSSLFAPTIETIDYPFPPKPVPLSDAQKADYKARIKQLLIEKDAVLVAHYYTDPEIQALAEETGGCVSDSLEMARFGRDHPAKTLIVAGVKFMGETAKILSPEKTILMPTLEATCSLDLGCPIDKFSAFCDAHPDHTVVVYANTSAAVKARADWVVTSSIALEIVEHLDSEGKKIIWGPDRHLGSYIAKQTGAEMLMWQGDCIVHDEFKANALRDLKSVYPDAAILVHPESPASVVAMADAVGSTSQLIKAAQTMPNERFIVATDRGIFYKMQQAAPGKTLIEAPTGGNGATCKSCAHCPWMAMNGLKAIEASLSNSDK... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 38709
Sequence Length: 357
Pathway: Cof... |
Q97JL2 | MKKKAIFGGTFNPIHNAHLNIAAKSIEKLQLDELIFVPSGNPPHKSEKGIAPAELRYEMVKEAIKDNCKFRIDDYEIKKKGISYTYETLEHFSRSQKDVDWFFIAGLDSLMDLDKWRNVNTILSLCKFIVFNRSGYNKSQVLEQKEYLEKKYINNIVFLDIKPIDISSTIIRQKIRENEYIGDLVPEKIYDIIKKNKLYV | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23412
Sequence Length: 200
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
A6LQS1 | MKRFGIIGGTFDPIHNAHLYIAYEAKEKLSLDEVIFMPAGIQPLKANNIITDPGLRYSMVKAAIEHFSEFSVSDYEIEKGGLSFTHETLEYFKNKISDRDKDNELFFITGADCLFSMEKWKEVKKIFSLATLVVFSRGGINKSDMINRKHMIEEKYNGKIIVLDLKELEISSTDIRNRVHENKRIDFFVPERVSDIIYKNRLYR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23739
Sequence Length: 204
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
C1FVW3 | MINKAILGGTFDPIHNAHINVAYEALERFNLEEVIFIPAGNPPHKIKLKKTPAHIRYEMVKLAIEKETRFSISDFEIKSKGLSYTYRTLKHFKEKEPETNWYFITGEDCLSYLEHWKYIDEIFNICNFVIFSREGFKEKEEIIKKKKSILLKYGKEILFMDASILDISSTKIRNRIKEGKEVSFYMPDKVYKFILQNNLYK | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23847
Sequence Length: 201
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
A0Q1T2 | MKKKGIFGGTFDPIHNGHLHIAYEALYKLNLDRVIFIPSGNPPHKTDKVITDANIRYKLVKDVIQNEEKFEVSDYELKNQGLSYTYKTLKHFNEKHKDTEWYFITGADCLMQLDSWKNINEVLSLCNFVVFRRSGYSMEDMLKQKERIEKKFNKKIIFLDIPVIDISSTTIRNKIKNRENISYLVPEKARCMVNKMNLYK | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23619
Sequence Length: 200
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
B5Y804 | MIKPLKSSRTGLLAGVFDPVHIGHLFMAHLAMEAANLDRVWFVPTHIPPHKDSAKVPYFHRVNMLEMALKEEPKFVLMELEREARPTYSYETILSVKHVLGEKPYFILGSDEWEELHNWRRYDLLVKNAIFIVVPRKPITVARPEAEAIFTDMTPINVSSTYIRQRVAKGKPITYLVPKTVETYIHENHLYYP | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22451
Sequence Length: 193
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q7UFN6 | MSASETTPQSNHGIGILGGSFDPVHVGHLWMAESALEQLPIEHVRWIPAATSPLKPHGPVASNEHRLQMLRLALSGQSGLVIDDWELRQDSVSYTLLTLEYLQEQFPDRPLYLIIGADSLASFDRWREPEQILKRCHLAVIARGGDPPPDYSILDGMTDETQIQRIRESQIQMPQIEISSSDLRNRIATGRSIRFRVPHPVATLIDNEKMYRVR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24192
Sequence Length: 214
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
A7NPC0 | MTSGRTGILGGSFDPIHYGHLAIAEEVRVLLRLNRVLIIPAREQPLKPGGSVASPAHRLAMARLACADNPFFEVSRIEIDRPDPSYTSVTLQLLHEQGLNDLYLILGIDSVADLPRWREVRRILELAHIVGVARPGAAVDLSHLSQVLPQLPARLIEIDGPRLDISSTDLRQRVAQGRPIRYQTPDAVVAYIEANGLYR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21985
Sequence Length: 199
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q1AVU4 | MRVGIFGGTFDPIHVGHMIVAEQVMDELGMERVVFVPSGIPPHKEASSVRAPAEDRYEMVLAAIAGNERFSADRIEIDAGRPMHTVETVPLLKERLPGEEWFFITGADEVSNLLSWKDPDRLLEEVVMVAATRPGYDLSRLGHLEARLKNFDRIFPVECTRVDVSATGIRRRILQGKSIRYLVPEGVREIILSRGLYRADARRTRGELLKEERS | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24178
Sequence Length: 214
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q5LW93 | MRQGFPYARPGQVIGLFGGSFDPPHAGHVHVTREALKMFGLDRVWWLVTPGNPLKAHGPAPLDRRMEAARAMMRHPRVDVTDIEAHLGTRVTADTIAALRRIYPRVRFVWLMGADNLAQLHRWKDWRQIIETVPVGVLARPGDRISARMSPAARAYAPYRIDGQARHLLGRAEAPAWCFVNVPMVDVSSTRIRAAGGWSAAQQGRGQTGTQDQ | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23709
Sequence Length: 213
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q1GEC6 | MTVGLLGGSFDPPHEGHVQISRAALKRFDLDQLWWLVTPGNPLKENPPASMTRRIKAAREIMDHPRVRISDIEARLNTRYTAQTLRELRKLYPQVRFVWLMGADNLAHFHRWKNWRGIMESVPVGVLARPGDRISARLSRAARIYSQHRIPAGQSHLLARASSPAWCFLNVPMTKASSTEIRKRGAWTG | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21549
Sequence Length: 189
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q21FD0 | MGKAHATPQLLFGGTFNPVHNGHLVSAMAAREALGVDSVTLLPCYVPPHKTAPTIAAEHRLAMLQHVVQENNHLCIDTCELDAGESIFTVDTLAAKRELWGASASIIWLIGWDSLHNLSRWHRWQSLLTFANLAVVERPFAQSDDINSLPPAVRNWLQQHRVSAKQLTQQANGGVALLHTPRIELSSSDVRQRLGAQKSIQYMVPACVETYIRAHKLYTH | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24416
Sequence Length: 220
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q2S0V3 | MTVGLFGGSFNPPHVAHLVVAEVVRDQFGLDEVWWIPNATPPHKPNDELAAVQHRLAMTERTVEGNPAFRVCGVEVERDGVSYTVETLRVLQDQHPDTDFALILGSDSLDHFADWHRPDEIAERVPFIVYKRPGAIESVADPRFVNDVRYAAAPVMEISGTEVRARRRAGRSIRYLVPEAVRAYIDTHDLYRPTD | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21981
Sequence Length: 195
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
B0R6W9 | MSAPDTVSPLDLRFSAAELAERRDRIQSFIRDTVAAAGAERCVLGLSGGIDSTTVAHLTVDELGADALHGLVMPGAVSRDQNMSDAERVAEDLGIEYDVVEIDPFVTQLTDVFPDAAGDEVAVGNARARTRAVINYFVANHGDGVVLGTGNRAEAMTGYYTKYGDQAVDCNPIGNLYKMQVRQLARDLGVPEDLVTKAPTAELWADQTDAGELGVDYDTIDAVLAVHVDGGLPASATATHLDIDPSVVETVRDLYGASKHKRAMPPAP | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28408
Sequence Length: 268
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
Q7VHF9 | MKHFVNPCIHFIQKQLQERGFKKVVLGLSGGIDSAVVATLATLALGSENVRALLMPSLSSNEEHFNDAFNLAHNLELESKIIQLAPFQENFAKQEGMDLSGKYMEKLDMNQKMRMGNFCARIRMTMLYDCASADNALVLGTSNKSEILLGYGTIFGDLAYAINPIGGLYKTQIFAFARALNVPQEIIAKKPSADLFANQSDETDLGYNYADIDTFLEAFEKLGGVEATQNKEREHIKEKLKNAGFECNMIESLSTRVWNNTFKRTKPTILEYKV | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 30669
Sequence Length: 274
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
O25096 | MQKDYQKLIVYLCDFLEKEVQKRGFKKVVYGLSGGLDSAVVGVLCQKVFKENAHALLMPSSVSMPENKTDALNLCEKFSIPYTEYSIAPYDAIFSSHFKDASLTRKGNFCARLRMAFLYDYSLKSDSLVIGTSNKSERMLGYGTLFGDLACAINPIGELFKTEVYELARRLNIPKKILNKPPSADLFVGQSDEKDLGYPYSVIDPLLKDIEALFQTKPIDTETLAQLGYDEILVKNITSRIQKNAFKLELPAIAKRFNPE | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 29269
Sequence Length: 260
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
Q6IA69 | MGRKVTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYESDTLLHSFQVLAALVESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSRHTEEYFLPRMIQDLTKQETVPFGDAVLVTWDTCIGSEICEELWTPHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIYLLANQKGCDGDRLYYDGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPRVKVDFALSCHEDLLAPISEP... | Function: Catalyzes the final step of the nicotinamide adenine dinucleotide (NAD) de novo synthesis pathway, the ATP-dependent amidation of deamido-NAD using L-glutamine as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da... |
A2BLB9 | MRITLNELLDLDYEGVARSIEEFIKGYVESSGAKGVVVGLSGGVDSTTTLYLLVRALGPERVLVLVMPDSDVTPEEDVHDAVGIAERLGVRYKLIDIKPIVASYLVAMGEAPDRRSKGNLRARVRMTLLYLYANMEGLLVAGTGDRSELLIGYFTKYGDGAVDFLPIGCLYKSQVRRLALHLGVPEKIALKPSSPRLWPGQLAEDELGMKYEEIDLILYALFDKGLSPEEAAKATGLPIEKVRRVLELHRASEHKRSLPPAPDPAATVWRFRRRKG | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 30514
Sequence Length: 276
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
Q9YD08 | MSGAVGLVVKRRSGIAEDVARLVVKELVESGVEVLVDETVDYPSLSGFPRFSISRDPPGRVVVVGGDGTLLRTFLRLGERESPLFMTIKAGKKGFLLDVERYEAVERLRDFLEGRFREVVYPRYRVYLEGEARACMFNDTAVTANNAKMARVHVFVDGDLAMNIDGDGVVVSTTAGSTAYSLSGGGPIIDPRLDVIVLTPLNPVQLFLRSIVVPSGSRVTVEASVYSNPLVVNIDGQYVYELEPGGIVDIERCGSGVRIARFRWWEDYYERLYTRLLAYW | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31067
Se... |
C4ZCY4 | MKHFVVIANAYKDRDFALTNKIVAYIEQKGGTAKGLMSNVEAISDNEFELEDIPQDTQCILVLGGDGTLIRAATRVETLEIPLMGVNLGTLGYLCEVEEATVFDAIDSLMADKYMTEDRIMLIGHKRGSETSRVALNDIVIHRKGNLQILSLNVYVNGEFLNNYHADGIIVATPTGSTGYSMSAGGPIVDPKGDMILLTPNNAHNLTSKSIVLSGDDEIEIEILSRREQNDELACVSYDGDTTAELAVGDRFVISRAANHTKICKLHQRSFLEILRKKMGNYS | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31056
Se... |
Q21XX2 | MKSKFRHVALIGKYQTVASGASGASSRRVLEDIAHFLGAQGCEVVFEHDTAHNMGISGYPVLDVDAIGAKCDLGLVVGGDGTMLGIGRQLAKFGVPLIGINQGRLGFITDIPLDGYASALAPMLRGEFEEDHRSLMHARVMRDGRCVYDALAMNDVVVNRAATSGMVELRVEVDGHFVANQRADGLIIATPTGSTAYSLSAGGPLLHPSIPGWVLVPIAPHTLSNRPIVLANITEIAIEIISGRDASASFDTQSLASLLRGDRIVVTRSEHNVRFLHPRGWSYFDTLRQKLHWNEGVA | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 32015
Se... |
O67055 | MRKVLVFLKNSKKAFETFKRVERVLKDLNLSYKKFINRKELFKVLKPKDYELFLVIGGDGTFLSAARIASRFGVPLVGVNEGRFGFLTEIKKEEIKKVLPLVLEGRAKLQERLMIDVYLRSRNRLRYLGNYLNDAVISKSSIARIIRTKVFINGEEVLEVFGDGVILSTPTGSTAYALSAGGPIVYPESQNLLFVPICPHTLSNRPLVLPSKFEVKFKVVSENMEAFLTLDGQEGFHLKKGDEVIVKRSRYVCRMYSHPRKSFFGILKEKLRWG | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31327
Se... |
O30297 | MRAAVVYKTDGHVKRIEEALKRLEVEVELFNQPSEELENFDFIVSVGGDGTILRILQKLKRCPPIFGINTGRVGLLTHASPENFEVELKKAVEKFEVERFPRVSCSAMPDVLALNEIAVLSRKPAKMIDVALRVDGVEVDRIRCDGFIVATQIGSTGYAFSAGGPVVEPYLECFILIPIAPFRFGWKPYVVSMERKIEVIAEKAIVVADGQKSVDFDGEITIEKSEFPAVFFKNEKRFRNLFGKVRSIG | Function: Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da... |
A1K8P2 | MSAHFRSVALIGKYQSADVAESVFAIANHLRQRGLVVWIEQGTASSIGGAADFTVASYEEIGSRAELAVVIGGDGTMLNAARRLAEHQVPLVGVNLGRLGFLTDVARSDALQRLEEIVDGRYSEESRFMLDAEVLRSGERVFQTLALNDVVVNKGDLGRMIEFDLSIDGEFVYTQRSDGMIISTPTGSTAYALSANGPILHPGVGGIALVPLCPHALTARPVTLPDTCRIEIRLLPPHDASIHFDGQARFDARAGDCVRLGRSPLAVRLLHPEGYNYYAMLREKLHWSAVPRHN | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31956
Se... |
Q8A0V4 | MPILQPKLMKQLMKFAIFGNTYQPKKSLHALRLFELLKKQGAEICMCREFYQFLTADLKMEVPVDALLEGNDFTADMVISIGGDGTFLKAARRVGRKQIPILGINTGRLGFLADVSPEEMEVTFEEIQAGRYSVEERSVLQLICNDRNLQESPYALNEIAVLKRDSSSMISIRTAINGAYLNTYQADGLVIATPTGSTAYSLSVGGPIIVPHSNTIAITPVAPHSLNVRPIVIRDDWEITLDVESRSHNFLVAIDGSSETCKETTQLTIRRADYSIKVVKRFNHIFFDTLRSKMMWGADGRR | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 33777
Se... |
Q6MII5 | MKKSSMDKEHKQSKLVLKENGSIGLVYRLETAQAVSLAKKVAEFLKERGFEVFTCPDQKVVAGTKAAKTKKHMDDLKLVIVLGGDGTYLRAVRLLEGRSVPILGFNMGSLGFLTAHSADSCFDIIEKTLEGKMVQRPRSMIYSKILRKGKVRAEYHALNDMVIERGSMSQLINTAIYSEKFLVSQVKADGFIVASPSGSTAYNLAAGGPICHPESPVFVVTPVAPHSLTSRPLLFPDDRELSFRLEGKTQKAHFIVDGQKMTELTADDEVIVSRSCYDHWMVREANHNYFHLLREKLKFGDRN | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 33807
Se... |
B7GTM7 | MAKRNAVVVTHTRLRQTGTVVAEAVSQLRVAGFEVTIIDNTEAPDFGVQPPCVSDDTEIVVVLGGDGTILRAAELVHCTQVPILGVNMGHVGFLAEFESFQIDEAIRRVATHDYSIDERMIAHVDVWLPGATKPIEDWALNDITLERADRGKMVELSIRVDDVEMNSFGADGVIVSTPTGSTAYAFSAGGPVMWPNVKALQLIPLAAHALFARPLIIGSGSTFTIDILDDSMSEGWICCDGRRQRALPQGTRVMVRESRDTLRLARLSGMPFTNRLVSKFDLPVVGWREHARNEASSQPLHHGHTFPAAAYAAGVAGDAG... | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 36342
Se... |
Q74BH6 | MKKIAIFAKVHDPRCQGVASELIAWLEARGLIPLVEAHLARHLGGRQGIVPEDIPVLADMAVVLGGDGTLISAARLIGSRQIPILGVNLGSLGFLTEITLDELYPVLESCLSGDFQVTERMMLTVSVERNGEEICSHRVLNDVVINKGALARIIDMETEVSGIRLTTYKADGLIISTPTGSTGYSLSANGPIVHPSLECITITPICPHTLTNRPIVLESSSGVTVWLRSKDEDVYLTLDGQVGMELKCGDAVHVRRAAHRTRLVMSRSRNYFEVLRTKLKWGER | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 30999
Se... |
P44497 | MNHLYRSFKTIALVGKPRNDINLQMHKNLFHWLMERGYQVLVEKEVAITLELPFEHLATLEEIGHRAQLAIVIGGDGNMLGRARVLAKYDIPLIGINRGNLGFLTDIDPKNAYSQLEACLERGEFFVEERFLLEAKIERASEIVSTSNAVNEAVIHPAKIAHMIDFHVYINDKFAFSQRSDGLIVSTPTGSTAYSLSAGGPILTPNLNAIALVPMFPHTLTSRPLVVDGDSKISIRFAEHNTSQLEVGCDSQITLPFTPDDVVHIQKSEHKLRLLHLKIIIITMC | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31828
Se... |
A1WX34 | MDEHPPPPFPTVGIIGKPGDPAIAGLVERLLPMLEARGCTALLDEQSMPETGDDRHPQRVSRETLLDACDLIIAIGGDGTLIHIARAVAGRRDVALMGINRGRLGFLVDIAPEHLDEVAQILDGQHVVDERLLLHAEIRSNEDDTLLREDVAINEVVLHRWNTARMIELVTRIDGEPLSDHRSDGLILATPTGSTAYAMAGGGPIVHPNLHAMLLVPVCPHTLSNRPLVVDGSSRIEIDVHPRFIEHVRVSCDSQNDLTLQAGSRLVVRAHPSPVRLVHPPGYSYFNLLRAKLGWGGPLCNIEPFGA | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 33397
Se... |
Q5UXD1 | MTVGIVAQRDNDRAMSLASTLCDRLRATSAAVVVDETTAGALGDHDAWEAAVPDSAPVDEMSACNLVVSIGGDGTFLYAARGAGSTPILGVNLGEVGFLNAIAPEEAVETVVAEVEHIQKTGSARTRAKPRLQASGDNWELSPALNEVVVQGERRGHGGGATVDVYVDDSLYTSGHADGVLVATPTGSTAYNLSERGPLVHPDVAGLIITGMADEMGTPPLVVDVDSEIVVELTDADSGVVVSDGRVRKDVVPPERITVSRAGEPVRLAGPPLDFFTALDKLA | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 29263
Se... |
Q7VGM5 | MKSHNAPITKVGVILRPSSPELKTTFLQIKEELNNAGIEVILESISGGMIELLGRDFHQLATQCDALFSLGGDGTLISMLRRAFEYELPCMGINTGRLGFLTALMPQNLHTFTSHLKSGDYTLQKHLVLQARIYSTLNTAYENNLDNKNQTPTQTLIAINEFLISKHELSGMVHIDASIDRKYFNTYRCDGLIIGTPAGSTAYNISAGGSVIYPYCRNILLTPIAPHSLTQRPLVLSDEFMLEFYAKERAKLIIDGQEMIDIMPSDRVQIQALPQSAMLMYPPTRDYFSVLKEKFKWGEEH | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 33777
Se... |
B0TEJ8 | MPTVGVVLNDDKPQALEVARRMADWLSQREVPMGIPLTRVAELVHSPSPELRDRLRQLDLIVVLGGDGTLLNTARLAAPHGIPVVGVNLGRLGFLTEVEVSDLFPALERIIAGDYRIEERMMLEARLIRDGLEQPSYFALNDVVVTKGDHPRMIRVEAAVGDEVVWTYSADGLIVSSPTGSTAYSLSAGGPIVSPELHALLLTPISPHALDARPLVIPQDQAVRLTVISSHSHAVVTVDGQPGQPMVCGDSVLVRKASVACRLIRLGERTFFRILREKMQQGR | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 30816
Se... |
C3PJW6 | MEILIRSTPADVAVAAADILASYANTSATLGLATGSTPVATYKELIARHERGEVSFAGSRAFLLDEYLGLAPEHEQSYYATIRRDFTSHVDFDDALVKSPEGSAADPVAATAAYDQAIRNAGGIDVQLLGIGANGHIGFNEPSSSLTSRTRVVALHPQTVQDNSRFFDNLEEVPRHALTQGLGTISEARHLLLIATGTNKANAVQAMVEGPLSARCPGSVLQLHPRATVIVDEAAAALLEDREYYLFADQNRLH | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 27151
Sequence Length: 254
Pathway: Amino-sugar met... |
Q6NJ91 | MEIVITPTKDDAARIAADILEEYAREGKTLGLATGSTPLGTYQELIRRHNEEGLSFAECQAFTLDEYVGLPREHEQSYYSTIRREFTSHIDIPDEKVFNPDGTAEHPGQAAQEYDRLIVEKGGVDIQILGIGTDGHIAFNEPTSSMASRTRIKTLHPDTVRDNSRFFNGNESQVPHHVMTQGIGTIREARHLLMLCFGENKADAVKAMVEGPVAAVCPASVLQLHEHATVIVDEAAAAKLEHTQYYRYALENKPDWQRF | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 28904
Sequence Length: 259
Pathway: Amino-sugar met... |
Q8FMI6 | MDIIIRADAQEVGKEAAAIMAPFIKQGRTIGLATGSSPLTTYRELIRMYESGELTFKTIQAFLLDEYVGLARDDKNSYFRTIRDEFTAHVDFVDANVHSPDSTDPDPYHAAALYEQKIIDTGVAIQLLGVGVNGHIGFNEPTSALQGPTKVQALHPQTIKDNARFFNDCIENVPTHAMTQGLGTITRAENIIMVATGEAKADAIHRIVEGPLTALCPGSVLQLHADVTIVVDEAAASKLEHADYYRTMERIRL | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 27694
Sequence Length: 253
Pathway: Amino-sugar met... |
P0AF25 | MTIKNVICDIDGVLMHDNVAVPGAAEFLHGIMDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQEGKKAYVVGEGALIHELYKAGFTITDVNPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGRGFYPACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSSLDDIDSMPFRPSWIYPSVAEIDVI | Cofactor: Magnesium. Can also use other divalent metal cations as manganese, cobalt or zinc.
Function: Catalyzes the dephosphorylation of an unusually broad range of substrate including deoxyribo- and ribonucleoside tri-, di-, and monophosphates, as well as polyphosphate and glucose-1-P (Glu1P).
Catalytic Activity: a r... |
O52379 | MSEPQRLKPVFPQDPKWPGEGSSRVPFWAYTREDLYKRELERLFYANHWCYVGLEAEIPNPGDFKRTVIGERSVIMVRDPDGGINVVENVCAHRGMRFCRERHGNAKDFFCPYHQWNYSLKGDLQGVPFRRGVKQDGKVNGGMPKDFKLEEHGLTKLKVAARGGAVFASFDHDVEPFEEFLGPTILHYFDRVFNGRKLKILGYRRQRIPGNWKLMQENIKDPYHPGLLHTWFSTFGLWRADNKSELKMDAKFRHAAMISTRGQGGKNEEVVSGVDSFKEQMKVNDPRLLDIVPEPWWGGPTAVMTTIFPSVIIQQQVNSV... | Cofactor: Binds 1 Fe cation per subunit.
Function: Oxygenase component of the salicylate 5-hydroxylase (S5H) multicomponent enzyme system which catalyzes the 5-hydroxylation of salicylate to gentisate. Active only on substrates with a ring-substituted carboxylate group with an adjacent hydroxyl group. Primarily active ... |
Q31G32 | MEKLLGQAMPLGCIMVDLESTTLQPHEKERLLDPLVAGVILFSRNYESIEQLQALTTEIHQLRHPKLLIAVDHEGGRVQRFKEGFSMLPAMGQLGKCFRANEKEGLELAQQVGWLMATELLAVGVDFSFAPVVDLDYGDSRVIGDRAFDSDPVIVGKLGKALVQGMRDAGMASVAKHFPGHGYIQADTHLEVAVDHREFQEIAHKDIQPFLKLIENGLDAVMPAHVRYPKVDDLPAGFSKVWLQEVLRQQCYFDGAIISDDMSMHAATEFGDAPTRVTAALKAGCDLVLVCNDPVAADEVLSQVTWETGPLSHARLIRLH... | Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-r... |
Q5QUZ5 | MAQLMIDIAGTELTAEDKKLLAAPAVNGLILFTRNFASLEQLQELIREARAAAAKPLLIAVDHEGGRVQRFREGFSAIPSMGSLQKIENEDERQRAARDLGWLMAAEVQAVGIDISFAPVLDVDDCSDVIGDRAFSAVPSEISKLASSFIEGMHEAGMACTGKHFPGHGSVQADSHIAIPEDDRTLEQIRAHDLKPFLSLIQKLDGIMPAHVIYPQIDPQPAGFSEFWLQQILRSELQFNGTIFSDDLSMQGATVAGDMEQRAVAALKAGCDMILVCNDRAGAVQVLDADLPATEPESAQRVNRMLMSSNAVSLEELKRT... | Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-r... |
Q606N2 | MFDLVGPRLSADEREFLCHPAAGGLILFSRNYASPDQMLALVSEVRSLRPDMLIAVDHEGGRVQRFREGFTRLPPASAYLEVAGEAGLAAAETAGWLMAAELRAVGVDFSFAPVLDVDSGISTVIGDRAFARTPEEVTAAARAFATGMRRAGMAAVGKHFPGHGGVAGDSHLVLPEDRRELEELLARDLLPFSALIRENLEGIMPAHVLYSRIDARPPCFSPFWLQTILRERMNFDGAIFSDDLSMAGAAVAGDYAARALAALEAGCDMLVVCNTPEATASILEALENRTASPGSTRRLAAMCGRSRIDRDALLASSEWR... | Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-r... |
Q97E86 | MKIFEAYTIKNMCLKNRIVMPPMCMYSSDNTGNINDFHLVHYTTRSIGGVGFIIVEATGITPNGRISDKDLGIWSEKHAEGLSFLVKEVKKYGSKIAIQLNHSGRKYEGTSGEPVAPSALAFDENSKTPKELTKNEIKEIILAFKAAAKRAEKAGFDAIEIHGAHGYLINQFLSPLSNFRDDEYGGSTENRTRFLKEVLEAVREVWPKEKPILLRVSAEDYRGGSGITPNEMVNIINIVKDLIDVVDVSSGGVAPAHINLYPGYQVKLSEVIKNECNVPTIAVGLICDINMVEEILSNNRADLVALGRELLRNPYFVLSS... | Function: Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes.
Catalytic Activity: A + H(+) + NADPH = AH2 + NADP(+)
Sequence Mass (Da): 37677
Se... |
Q5KXG9 | MNTMLFSPYTIRGLTLKNRIVMSPMCMYSCDTKDGAVRTWHKIHYPARAVGQVGLIIVEATGVTPQGRISERDLGIWSDDHIAGLRELVGLVKEHGAAIGIQLAHAGRKSQVPGEIIAPSAVPFDDSSPTPKEMTKADIEETVQAFQNGARRAKEAGFDVIEIHAAHGYLINEFLSPLSNRRQDEYGGSPENRYRFLGEVIDAVREVWDGPLFVRISASDYHPDGLTAKDYVPYAKRMKEQGVDLVDVSSGAIVPARMNVYPGYQVPFAELIRREADIPTGAVGLITSGWQAEEILQNGRADLVFLGRELLRNPYWPYAA... | Function: Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes.
Catalytic Activity: A + H(+) + NADPH = AH2 + NADP(+)
Sequence Mass (Da): 37680
Se... |
Q928C2 | MSKLFSEYKLKDVTLKNRIVMSPMCMYSVENKDGIATDFHFAHYVSRAAGGTGLVILEATAVQEVGRISEFDLGLWNDEQVPALKRLVDGLHYHGAKAGIQLAHAGRKAVLPGEIVAPSAIPFDEKSAKPVELTKEAIKEVVADFKRAAYRAKEAGFDVIEIHAAHGYLIHQFLSPISNRREDNYGGPAGNRYKILSDIIKAVKEVWDGPIIVRVSATDYAHGGLQLEDHIPFAKWMKADGVELIDVSTGGLVNVEPPVFPGYQVPFADEIRRGAGIATGALGLITRGEQAEEILCNERADLIIIGRELLRNPYFAKEAA... | Function: Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes.
Catalytic Activity: A + H(+) + NADPH = AH2 + NADP(+)
Sequence Mass (Da): 37120
Se... |
Q6FDK2 | MSFRINPLNAIDFYKADHRRQYPEGTEYVYANFTPRSSRLANMLHDFDDKIVFFGLQGFIQHFLIETWNEGFFNQDKATVVSHYKRRMDTSLGEGAVSVEHIEALHDLGYLPLKIKALPEGSRVNMRVPVLTVINTQAEFFWLTNYIETVLSAELWKSSTTATIAFEYKRLLTQYAVKTGASIENVVVQGHDFSSRGMSGIYDAAQSGVGHLTSFIGTDAVTAIDYAEQYYAASGVVGVSVPATEHSVMCMGSEENELETFRRLICELYPSGIVSIVSDTWDFWRVLSEFSVKLKQDILNRTPNALGLAKVVFRPDSGDP... | Function: Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD . Functions in the nondeamidating salvage pathway for production of NAD from nicotinamide . Displays a strict preference for nicotinamide over nicot... |
P43490 | MNPAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKLRKVKYEETVFYGLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKGWNYILEKYDGHLPIEIKAVPEGFVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETSGNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGLALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIVSRSTQAPLIIRPDSGNPLDT... | Function: Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating pro... |
P75067 | MVQTPSEINTHLKHLLACDAYKLSHRLMYPNDTTNLYSCLTARGGRGGFPNFVWNHEFAKKIILEVFGNFCDSVLAVQNDPGLAQALTDKVTTVFGDPQFGLEFTQHICYLANFLKQHHQLPLTVKIHQSSEGLAFRTPLVTITGSDQMVPELVWLVNYFETVLLENIWLYQTTLTVAQSLKLLLERYANETADNTEFTHFQCHDFSMRGMSSLQSALYVANAHLQYFSGSDTILGGVAAKSILASEHSVMCADGQEGELNTFKRLLEQFPNKNLSLVIDSYDMWHVLDNILPQLKDLVLQRQEKLYLRPDSGNFETLIC... | Function: Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD.
Catalytic Activity: beta-nicotinamide D-ribonucleotide + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + H(+) + nicotinamide
Sequence Mass (... |
P31206 | MKKAVILFSLFCFLCAIPVVQAADTIFVRETRIPILIERQDNVLFYLRLDAKESQTLNDVVLNLGEGVNLSEIQSIKLYYGGTEALQDSGKKRFAPVGYISSNTPGKTLAANPSYSIKKSEVTNPGNQVVLKGDQKLFPGINYFWISLQMKPGTSLTSKVTADIASITLDGKKALLDVVSENGIEHRMGVGVRHAGDDNSAAFRIPGLVTTNKGTLLGVYDVRYNSSVDLQEHVDVGLSRSTDGGKTWEKMRLPLAFGEFGGLPAGQNGVGDPSILVDTKTNNVWVVAAWTHGMGNQRAWWSSHPGMDMNHTAQLVLAKS... | Function: Sialidases have been suggested to be pathogenic factors in microbial infections.
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Sequence... |
P29767 | MNKKKIMSILVSAFLITNLSSNIIFADIKENVYINQYSEGNRSQPIAEKLVPRSEIQASATSALTGEGPEKAIDGNTSTLWHTPWAGVDIQINPQSLTLKLGKTRNISSICVTPRQEGTNGMITDYKIYSGDDVIAEGKWKSDSSDKYVVFDNPISTDNIRIEAISTVGDENNKHASIAEVEVYELADTPVKLAESNNKVINNGNGGNYEGDISEISLLEEGTAIIRFTNNGSSLFSISNNERTNEHFHVYINGGAIGYELRKQSGNLATGSVNKALNAGINTIAFKAEKGKGYSIYLNGEKILTSSSITANFLSTLEGL... | Function: Sialidases have been suggested to be pathogenic factors in microbial infections.
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Sequence... |
Q02834 | MTANPYLRRLPRRRAVSFLLAPALAAATVAGASPAQAIAGAPVPPGGEPLYTEQDLAVNGREGFPNYRIPALTVTPDGDLLASYDGRPTGIDAPGPNSILQRRSTDGGRTWGEQQVVSAGQTTAPIKGFSDPSYLVDRETGTIFNFHVYSQRQGFAGSRPGTDPADPNVLHANVATSTDGGLTWSHRTITADITPDPGWRSRFAASGEGIQLRYGPHAGRLIQQYTIINAAGAFQAVSVYSDDHGRTWRAGEAVGVGMDENKTVELSDGRVLLNSRDSARSGYRKVAVSTDGGHSYGPVTIDRDLPDPTNNASIIRAFPD... | Function: To release sialic acids for use as carbon and energy sources for this non-pathogenic bacterium while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors.
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid ... |
P15698 | MKKFIKILKVLSMAIVLSACNINGIFASNLNTTNEPQKTTVFNKNDNTWNAQYFRIPSLQTLADGTMLAFSDIRYNGAEDHAYIDIGAAKSTDNGQTWDYKTVMENDRIDSTFSRVMDSTTVVTDTGRIILIAGSWNKNGNWASSTTSLRSDWSVQMVYSDDNGETWSDKVDLTTNKARIKNQPSNTIGWLAGVGSGIVMSDGTIVMPIQIALRENNANNYYSSVIYSKDNGETWTMGNKVPDPKTSENMVIELDGALIMSSRNDGKNYRASYISYDMGSTWEVYDPLHNKISTGNGSGCQGSFIKVTAKDGHRLGFISA... | Function: Sialidases have been suggested to be pathogenic factors in microbial infections.
PTM: It is possible that the sialidase is cleaved in front of a cysteine within the leader peptide, forming a glyceride thioether bond which links the protein to the membrane. A second proteolytic cleavage releases the mature ext... |
P29768 | MTVEKSVVFKAEGEHFTDQKGNTIVGSGSGGTTKYFRIPAMCTTSKGTIVVFADARHNTASDQSFIDTAAARSTDGGKTWNKKIAIYNDRVNSKLSRVMDPTCIVANIQGRETILVMVGKWNNNDKTWGAYRDKAPDTDWDLVLYKSTDDGVTFSKVETNIHDIVTKNGTISAMLGGVGSGLQLNDGKLVFPVQMVRTKNITTVLNTSFIYSTDGITWSLPSGYCEGFGSENNIIEFNASLVNNIRNSGLRRSFETKDFGKTWTEFPPMDKKVDNRNHGVQGSTITIPSGNKLVAAHSSAQNKNNDYTRSDISLYAHNLY... | Function: Cleaves the terminal sialic acid (N-acetyl neuraminic acid) from carbohydrate chains in glycoproteins providing free sialic acid which can be used as carbon and energy sources. Sialidases have been suggested to be pathogenic factors in microbial infections.
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alp... |
A5F7A4 | MRFKNVKKTALMLAMFGMATSSNAALFDYNATGDTEFDSPAKQGWMQDNTNNGSGVLTNADGMPAWLVQGIGGRAQWTYSLSTNQHAQASSFGWRMTTEMKVLSGGMITNYYANGTQRVLPIISLDSSGNLVVEFEGQTGRTVLATGTAATEYHKFELVFLPGSNPSASFYFDGKLIRDNIQPTASKQNMIVWGNGSSNTDGVAAYRDIKFEIQGDVIFRGPDRIPSIVASSVTPGVVTAFAEKRVGGGDPGALSNTNDIITRTSRDGGITWDTELNLTEQINVSDEFDFSDPRPIYDPSSNTVLVSYARWPTDAAQNGD... | Function: Cleaves the terminal sialic acid (N-acetyl neuraminic acid) from carbohydrate chains in glycoproteins providing free sialic acid which can be used as carbon and energy sources. Sialidases have been suggested to be pathogenic factors in microbial infections. Facilitates cholera toxin binding to host intestinal... |
Q8FDU8 | MITLAVDIGGTKISAALISDDGSFLLKKQISTPHERCPDEMTGALRLLVSEMKGTAERFAVASTGIINNGVLTALNPDNLGGLKEYPLKNIMEDITGLNGSVINDAQAAAWAEYTVLPKEICDMVFITVSTGVGGGIVVNRKLLTGVSGLAGHVGHILSGVTDTECGCGRRGCVEAVSSGRAIMGAAKNKLAGYSTKYIFELARQGYKEAEFLTERSASTIAELIVSLKLLLDCQVVVVGGSVGLADGYVQKVSKHLSIYSEICNVMLFPAYFRSDSGLIGATLWDRDCIT | Function: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P.
Catalytic Activity: an N-acyl-D-mannosamine + ATP = ADP + an N-acyl-D-mannosamine 6-phosphate + H(+)
Sequence Mass (Da): 30744
Sequence Length: 291
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosph... |
Q8X9H0 | MTTLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPLQAHAQRVAIASTGIIRDGSLLALNPHNLGGLLHFPLVKTLGQLTDLPTIAINDAQAAAWAEYQALEGDITDMVFITVSTGVGGGVVSGGKLLTGPGGLAGHIGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQGELAGADAKTIFMRAGQGDEQAQQLIHRSAHVLARLIADIKATTDCQCVVVGGSVGLAEGYLALVETYLAQEPAAFHVDLLAAHYRHDAGLLGAALLAQGEKL | Function: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P.
Catalytic Activity: an N-acyl-D-mannosamine + ATP = ADP + an N-acyl-D-mannosamine 6-phosphate + H(+)
Sequence Mass (Da): 29566
Sequence Length: 291
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosph... |
P37061 | MKVVVVGCTHAGTSAVKSILANHPEAEVTVYERNDNISFLSCGIALYVGGVVKNAADLFYSNPEELASLGATVKMEHNVEEINVDDKTVTAKNLQTGATETVSYDKLVMTTGSWPIIPPIPGIDAENILLCKNYSQANVIIEKAKDAKRVVVVGGGYIGIELVEAFVESGKQVTLVDGLDRILNKYLDKPFTDVLEKELVDRGVNLALGENVQQFVADEQGKVAKVITPSQEFEADMVIMCVGFRPNTELLKDKVDMLPNGAIEVNEYMQTSNPDIFAAGDSAVVHYNPSQTKNYIPLATNAVRQGMLVGRNLTEQKLAY... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the four-electron reduction of molecular oxygen to water.
PTM: The N-terminus is blocked.
Catalytic Activity: 2 H(+) + 2 NADH + O2 = 2 H2O + 2 NAD(+)
Sequence Mass (Da): 48915
Sequence Length: 446
EC: 1.6.3.4
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A2RIB7 | MKIVVIGTNHAGIATANTLLEQYPGHEIVMIDRNSNMSYLGCGTAIWVGRQIEKPDELFYAKAEDFEAKGVKILTETEVSEIDFANKKVYAKTKSDDEIIEAYDKLVLATGSRPIIPNLPGKDLKGIHFLKLFQEGQAIDAEFAKEKVKRIAVIGAGYIGTEIAEAAKRRGKEVLLFDAENTSLASYYDEEFAKGMDENLAQHGIELHFGELAKEFKANEEGYVSQIVTNKATYDVDLVINCIGFTANSALASDKLATFKNGAIKVDKHQQSSDPDVYAVGDVATIYSNALQDFTYIALASNAVRSGIVAGHNIGGKELE... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the four-electron reduction of molecular oxygen to water. Active on beta-NADH, but not on alpha-NADH, beta-NADPH or alpha-NADPH. Under aerobic conditions, oxygen acts as the electron acceptor. Under anaerobic conditions, DCIP and MB can replace oxygen as the electr... |
Q7M963 | MKTSKLNFLTLVASTGLALAFLSGCTSNTGTTQSAKLYSEEELGLRKATIYNENKTLVKEFEYSKEPAGASKVYERSFENAPPMIPHDVEGMMDMSREINMCTSCHLPEVAEAAAATPMPKSHFFNMRTGEDLKGAMDEARYNCSQCHTPQANVTPLVDNRFRPEFRGEDAKNRSNLIDTLNEGVK | Function: Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Transfers electrons to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor.
PTM: Binds 2 heme C groups per subunit.
Seq... |
Q53178 | MRLPSFLRRFWSIATSPSSFLSVGFLTLGGFVGGVLFWGGFNTALEATNTEAFCTSCHEMQSNVFEELTRTVHYTNRSGVRAGCPDCHVPHEWTDKIARKMQASKEVWGHLFGTIDTRRKFLDNRLRLAEHEWARLKANDSLECRNCHSEVAMDFTRQTDRAAQIHTQYLIQTEGYTCIDCHKGIAHELPDMRGIDPGWLPPADLRASLPDHGSSFDLEGARAYVAD | Function: Mediates electron flow from quinones to the NapAB complex.
PTM: Binds 4 heme groups per subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25637
Sequence Length: 227
Subcellular Location: Cell inner membrane
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P0ABL7 | MGNSDRKPGLIKRLWKWWRTPSRLALGTLLLIGFVGGIVFWGGFNTGMEKANTEEFCISCHEMRNTVYQEYMDSVHYNNRSGVRATCPDCHVPHEFVPKMIRKLKASKELYGKIFGVIDTPQKFEAHRLTMAQNEWRRMKDNNSQECRNCHNFEYMDTTAQKSVAAKMHDQAVKDGQTCIDCHKGIAHKLPDMREVEPGF | Function: Mediates electron flow from quinones to the NapAB complex.
PTM: Binds 4 heme groups per subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23101
Sequence Length: 200
Subcellular Location: Cell inner membrane
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P44655 | MSEKKPNILKRFWQWFRKPSRMAIGTIIILSAIGGILSWVGFNYGLEKTNTEQFCASCHMQDAYPEYLHSVHYQTRTGVGASCPDCHVPHEFGAKMKRKIIAAKEVYAHYTGKVDTLEKFNAHRLEMAQNEWARMKANDSKECRNCHNVDRMTFNDQRSVAARMHQKMKTEGKTCIDCHKGIAHQLPDMSGVESGFKDEK | Function: Mediates electron flow from quinones to the NapAB complex.
PTM: Binds 4 heme groups per subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22957
Sequence Length: 200
Subcellular Location: Cell inner membrane
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Q965X9 | MSAPTTSSSTDEDFAKPVKNGKTFANPKSFTNWGGIPGISDGFKFAFTETNHENVPCDKKILDVEIPVHNITADDFHSESDLFATWLGHATVLVDLEGVKFVTDPVWADRASFTSFAGPKRYRPPPMKLEDLPDLDFAVVSHDHYDHLDADAVKKITDRNPQIKWFVPLGMKKWMEGQGIGVDGSSTAVTELNWGESSEFVKNGKTYTIWCLPAQHWGQRGLFDRNHRLWSGWAVIGENRRFYYSGDTGHCDGEFKKFGEKLGPFDLAAIPIGAYEPRWFMKSQHINPEEAIEVHKLIRAKNSIGIHWGTYHMGSTEYYL... | Cofactor: Binds 2 zinc divalent cations per subunit.
Function: D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid. NAEs are bioactive lipids that are involved in diverse physiological processes... |
Q6IQ20 | MDENESNQSLMTSSQYPKEAVRKRQNSARNSGASDSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNPSIPNVLRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGVREAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQ... | Cofactor: Binds 2 zinc divalent cations per subunit.
Function: D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid . Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, pr... |
Q8BH82 | MDEYEDSQSPAPSYQYPKETLRKRQNSVQNSGGSVSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNISIPNVLRWLIMEKNHSGVPGSKEELDKELPVLKPYFVSDPEDAGVREAGLRVTWLGHATLMVEMDELIFLTDPMFSSRASPSQYMGPKRFRRPPCTISELPTIDAVLISHNHYDHLDYGSVLALNERFGSELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWSRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQ... | Cofactor: Binds 2 zinc divalent cations per subunit.
Function: D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid . Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, pr... |
Q769K2 | MDENENSQSPAPSHQYPKETLRKRQNSVQNSGGSESSRLSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNVSIPNVLRWLIMEKDHSSVPGSKEELDKELPVLKPYFISDPEEAGVREAGLRVTWLGHATLMVEMDELILLTDPMFSSRASPSQYMGPKRFRRPPCTISELPPIDAVLISHNHYDHLDYGSVLALNERFGSELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQ... | Cofactor: Binds 2 zinc divalent cations per subunit.
Function: D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid . Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, pr... |
Q9XGI7 | MVCPNSNPVVEKVCELYEQISRLENLSPSKDVNVLFTDLVHTCMPPNPIDVSKLCQKIQEIRSHLIKLCGQAEGLLESHFSKILSSYENPLQHLHIFPYFDNYIKLSLLEYNILTKNTTNIPKKIAFIGSGPLPLTSLVLATKHLKTTCFHNYDIDVDANFMASALVAADPDMSSRMTFHTADVMDVTCALKDYDVVFLAALVGMDKEDKVKVVDHLAKYMSPGATLMLRSAHGARAFLYPVLDPRDLRGFEVLSVYHPTDEVINSVIIARKLPVPSVPLLDGLGAYVLPSKCACAEIHAFNPLNKMNLVEEFALEE | Function: Synthesizes nicotianamine, a polyamine that serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Catalytic Activity: 3 S-adenosyl-L-methionine = 3 H(+) + nicotianamine + 3 S-methyl-5'-thioadenosine
Sequence Mass (Da): 35303
Sequence Length: ... |
P54008 | IHGDNKTRKGERKLHEERWQAASAAAHQHLSTPQTAAGGGRVLREVTLEMPIRYAPSDAVEKWLNNLLCLDCGSTPNRIIGGTPHPRECELYYVDRDSLFSYHKLSESFLQRIMALYVASHYKNQPNDLQLLSDAPAHHIFVLLGPQAEGQGNAGQLPDVLCVVQVALEGEISKESVAAQLSRGQRASGDLIPWTVAQQFQDNEFAGLSGARVVRIATHPDVTGMGYGSRAVELLTKYYQGELASGEFEEENEAAKPADEESDDESNLLKEKVKPRKALPPLLLPLTDRPAERLHWFGTSFGLTLQLYTFWQRSGFRSVY... | Function: RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tR... |
Q9W3C1 | MVKKKIDNRIRVMIENGVKLGHRTMFIVIGDKARDQVPILYDILTKSTVKARPTVLWCYKNKDEAISNHGKKRAKKIAVGKVDVNEADLFDSFRVATTIHGRYYSETHAVLGRTYGVCVLQDFEALTPNLLARTVETVEGGGLIILLLKTLQSLKQLYTMSMDVHKRFRTEAHQTVTCRFNERLILSLADCKRCLVVNDDLTVLPLSSKTINVEPVNPAGAGRSPNEASLKELKESLLTVQPAGALVNLCKTYDQANAVAQFIEALVDKQLKPPMSLTAARGRGKSAALGLSIAAAVAFGYVNIYVTSPHPENLITLFEF... | Function: RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tR... |
Q3MHZ1 | MAPSHLSVREMREDEKPLVLEMLKAGVKDTENRVALHALTRPPALLLLAAASSGLRFVLASFALALLLPVFLAVAAMKLGLRARWGSLPPPGGLGGPWVAVRGSGDVCGVLALAPGSSAGDGARVTRLSVSRWHRRRGVGRRLLAFAESRARAWAGGMGEPRARLVVPVAVAAWGVAGMLEGCGYQAEGSWGCMGYTLVREFSKEL | Function: Probable acetyltransferase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21734
Sequence Length: 206
Subcellular Location: Membrane
EC: 2.3.1.-
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Q0P4A4 | MVRLDLADVVLRRMQEKDIEAVKALIKEGCEGTENRLILHLLTRPLALLLLAILSSILRCVLHSFVLALVIPVFISVIYLKLTIPRSAGILGSCRPYWDYIGSSYHADTEPDLPNPHLGRAKLTTNQEKTRRRKKAKEKEKMNESEQVDEDELKQRAKVAGEVWVADSDGEIVGCVARDGWSRDGVCRVCRLVVQCWYRREGLGRLLVQGLESRTKQKGVCRVYAHVPIPSKVGEAFFRRLGYRLQGETAGIEEEEEDDYEDPEKGWLGYPLTKVFVKDL | Function: Probable acetyltransferase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31818
Sequence Length: 280
Subcellular Location: Membrane
EC: 2.3.1.-
|
Q8WUY8 | MAPSHLSVREMREDEKPLVLEMLKAGVKDTENRVALHALTRPPALLLLAAASSGLRFVLASFALALLLPVFLAVAAVKLGLRARWGSLPPPGGLGGPWVAVRGSGDVCGVLALAPGTNAGDGARVTRLSVSRWHRRRGVGRRLLAFAEARARAWAGGMGEPRARLVVPVAVAAWGVGGMLEGCGYQAEGGWGCLGYTLVREFSKDL | Function: Probable acetyltransferase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21650
Sequence Length: 206
Subcellular Location: Membrane
EC: 2.3.1.-
|
Q8BVG8 | MAPNHLSVREMREDEKPLVLEMLKAGVKDTENRVALHALTRPPALLLLAAASSGLRFILASFALALLLPVFLAVAAVKLGLRARWGSLPPPGGLGGPWVAVRGSGDVCGVLALAPGANVGDGARVTRLSVSRWHRRRGVGRRLLAFAEARARAWAGSMGEPRARLVVPVAVAAWGVAGLLEACGYQAEGGWGCMGYMLVREFSKDL | Function: Probable acetyltransferase that binds the 5'-GGACTACAG-3' sequence of coproporphyrinogen oxidase promoter. Able to activate transcription of a reporter construct in vitro (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21778
Sequence Length: 206
Subcellular Location: Membr... |
Q28DI5 | MPFIDENQLSVREMREEEAPVVLEMLKDGFKDTENRLILYILTRPMTLLLMAVASSGLRFILNSFSVALVIPVLLTIVGLKLLLWRSPDLKQIYSYYSIGQRKIWVAVYDQDDICGCVALEPTQDHQTVELKRMSVSRWYRRSGVGTHLLKFFEDHAKKKGFRGIVLYTSVVAKAAIGLFKNCGYKVTGGWNWLGYTIVQEFRKDI | Function: Probable acetyltransferase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23672
Sequence Length: 206
Subcellular Location: Membrane
EC: 2.3.1.-
|
Q8H1Q2 | MENGDIPEDANEHCPGPQSESAGKSDSCAGCPNQEACATAPKGPDPDLVAIAERMSTVKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIHQSNLGWSPVYVEDNLGVMSIGFMLPNSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLLPTGIDGAIIVTTPQEVSLIDVRKEVSFCKKVGVPVLGVVENMSGLSQPLKDVKFMKLATETGSSINVTEDVIACLRKNAPELLDIVACSEVFDSSGGGAERMCREMGVPFLGKVPMDPQLCKAAEQGK... | Cofactor: Binds 3 [4Fe-4S] clusters per homodimer. Contains two stable clusters in the N-termini and one labile, bridging cluster between subunits of the homodimer.
Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. Func... |
Q754X6 | MQTSAEMGGIIEAMPALAQDGYALEQAPPEHCPGPASENAGKGDACQGCANKDICESLPKGPDPDVALITQNLAPVRHKVLVLSGKGGVGKSTFSAMLGWALSADEALQVGVMDLDICGPSLPHMLGCVNETVHESSVGWTPVYVADNLAAMSIQFMLPEDDSAVIWRGAKKNALIKRFLKDVYWDELDYLVVDTPPGTSDEHITINTLLKESGIDGALVVTTPQEVALLDVRKELDFCRKAGIRVLGLVENMSGFVCPSCENESTIFKPTTGGGRALCEELGIKFLGAVPIDPRIGRCCDSGESFLDAYPDSPASTAIM... | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NBP35 and two labile, bridging clusters between subunits of the NBP35-CFD1 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extrami... |
Q59MP1 | MSPSQTQIEKSQLAAPEPEHCPGPESELAGQGDACKGCANQEICSSQTVKGPDPDLPIITERLSAIDHKILVLSGKGGVGKSTFTSMLAWAIAADEEIEVGAMDLDICGPSLPRMLGAEGESVHQSNSGWSPVYVADNLGLMSISFMLPDPDSAIIWRGAKKNGLIKQFLKDVNWGEKLDYLVVDTPPGTSDEHLSVTTYMKEVGIDGALIVTTPQEVALLDVRKEIDFCRKANIKILGLVENMSGFVCPNCKGESQIFKATTGGGKRLCEELGIPFLGSVPLDPRIGKACDMGECFFDSYPDSPAATAILDVVDALRDQ... | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NBP35 and two labile, bridging clusters between subunits of the NBP35-CFD1 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extrami... |
Q1EAU8 | MAPSFEEPTVALGAASKAAPKLVAPEPEHCPGPESEQAGKGDACAGCPNQSICASAPKGPDPDIPIITARLSSIRHKILVLSGKGGVGKSTFTSLLANAFASNPDSTVGVMDTDICGPSIPKMMDVETETIHVSNAGWNPVWVSDNLAVMSVQFMLPNRDDAVIWRGPKKNGLIKQFLKDVEWGELDYLIVDTPPGTSDEHLSVNSFLKESGVDGAVLVTTPQEVSLLDVRKEIDFCRKAGIRILGLVENMSGFVCPKCTHESQIFKPTTGGGGRLAADMGIPFLGSVPLDPRVGMACDYGENFMDRYPESPASMALRKV... | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NBP35 and two labile, bridging clusters between subunits of the NBP35-CFD1 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extrami... |
P0CO89 | MIATQRPFPIPSPVPLAPSSTVLPTTVPENAPEHCPGVESSQAGKADACEGCPNQSVCAEGPKGPDPDLPLIRERMSSVRRKILVLSGKGGVGKSTFTAGLSWALAADEECQAGIMDIDICGPSIPLLMGLESSTIHTSASGWSPAYALDNLAVMSIGFLLPSSSDAVIWRGPKKNGLIKQFLKDVEWGDLDYMVVDTPPGTSDEHLSIVQYLKEAGIDGAVLVTTPQEVALQDVRKEIDFCKKVGIPILGLVENMSGFVCPNCKNESQIFAPTTGGAEAMGKELGIELLGKVPLDPRIGMTCDQGMSFLDEYPESPATM... | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NBP35 and two labile, bridging clusters between subunits of the NBP35-CFD1 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extrami... |
Q6BTZ6 | MAPSQVEDISKTELETPEHCPGPESEQAGKEDACNGCPNQSICSSQLPQGPDPDLPLINKRLSQIDHKILVLSGKGGVGKSTFTSMLSWALAADEDIEVGAMDLDICGPSLPRMLGAEGESIHQSNSGWSPVYVADNLGLMSISFMLPDADSAVIWRGAKKNGLIKQFLKDVNWGEHLDYLVVDTPPGTSDEHLSVTTYMKEVGIDGALIVTTPQEVALLDVRKEIDFCRKANIKILGLVENMSGFVCPNCKGESQIFRPTTGGGKKLCEDLKLPYLGAVPLDPRIGKACDAGESFFDSYADSPASSAILDVVDALRDQI... | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NBP35 and two labile, bridging clusters between subunits of the NBP35-CFD1 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extrami... |
Q5BBC5 | MAPSFTETTSTYLEAPSKAPPNLVAPEPEHCPGPESDQAGQGDACAGCPNQSICASAPKGPDPDIPLITARLASVRHKILVLSGKGGVGKSTFSSLLAHGFASNPDSTVGIMDTDICGPSIPKMMGVESETIHISNAGWSPVWVSDNLGVMSVQFMLPNRDDAVIWRGPKKNGLIKQFLKDVDWGEMDYLIVDTPPGTSDEHLSVNSLLKESGVDGAVVVTTPQEVSLLDVRKEIDFCRKAGIRILGLVENMSGFVCPSCDHESKIFRATTGGGKRLAKKMGIPFLGAVPLDPRVGMACDYGESFVENFPDSPASLAIKQ... | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of nbp35 and two labile, bridging clusters between subunits of the nbp35-cfd1 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extrami... |
Q4HZ34 | MAPSLETPESIDDVFANPIKQKPQLVAPEPQNCVGPDSQQAGKADSCAGCPNQAICASAPKGPDPDIPVISARLENVKHKILVLSGKGGVGKSTFTSLLAHAFATNPDSNVGIMDTDICGPSIPKMMGVEGETVHVSGTGWSPIWVMDNLAVMSIQFLLPNRDDAVIWRGPKKNGLIKQFLKDVEWGDLDFLLVDTPPGTSDEHLSVNSFLKGSGIDGAVMVTTPQEVSLLDVRKEIDFCRKAGIKILGLAENMSGFVCPKCSNESQIFKASTGGGRALAEEMDIPFLGSVPLDPRIRMACDYGESYFDSFPDSPACLAF... | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NBP35 and two labile, bridging clusters between subunits of the NBP35-CFD1 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extrami... |
P22677 | MALSKVKLNDTFNKDQLLSTSKYTIQRSTGDNIDIPNYDVQKHLNKLCGMLLITEDANHKFTGLIGILYAMSRLGREDTLKILKDAGYQVRANGVDVITHRQDVNGKEMKFEVLTLVSLTSEVQGNIEIESRKSYKKMLKEMGEVAPEYRHDSPDCGMIVLCVAALVITKLAAGDRSGLTAVIRRANNVLRNEMKRYKGLIPKDIANSFYEVIEKYPHYIDVFVHFGIAQSSTRGGSRVEGIFAGLFMNAYGAGQVMLRWGVLAKSVKNIMLGHASVQAEMEQVVEVYEYAQKLGGEAGFYHILNNPKASLLSLTQFPNF... | Function: Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases (Probable). RNA replication depends on the availability of soluble nucleoprotein (By similarity). The encapsidated genomic RNA is termed the NC and serves as template for transcription and repl... |
P89522 | MENKIEVNNKDEMNRWFEEFKKGNGLVDTFTNSYSFCESVPNLDRFVFQMASATDDAQKDSIYASALVEATKFCAPIYECAWVSSTGIVKKGLEWFEKNAGTIKSWDESYTELKVDVPKIEQLTGYQQAALKWRKDIGFRVNANTAALSNKVLAEYKVPGEIVMSVKEMLSDMIRRRNLILNRGGDENPRGPVSHEHVDWCREFVKGKYIMAFNPPWGDINKSGRSGIALVATGLAKLAETEGKGIFDEAKKTVEALNGYLDKHKDEVDRASADSMITNLLKHIAKAQELYKNSSALRAQSAQIDTAFSSYYWLYKAGVT... | Cofactor: Endonuclease activity is stimulated by divalent cations such as Mn2+, Co2+, and Mg2+.
Function: Binds dsRNA and ssRNA and probably participates in the packaging of viral genome. In the dsRNA binding mode, the nucleocapsid protein specifically binds to the vRNA panhandle secondary structure formed at the termi... |
Q9WS40 | MADLFSKVNDFQKYRTNLGRQGGLTVKLVGVRSTVVVLVPSTKDHRLRWKLIRLLTLAVYNDSLPDSISIGALLSLLAISFEQPAAVIRGLLSDPDLEVQMIEVSLDDQGEIRFAARGDILTRYKDAYFEKIRDFPNPDDDLAIFEDPELGDYSDITQDEYQAMITTITIQLWILLTKAVTAPDTAHDSEQRRFIKYLQQRKAYAAFKFTTIFTERVRRKIAQSLSIRKFMVSIMLEVRKSGSAKGRISECIADVSAYIEEAGLSGFILTLKYGIGTRFPVLALNAFQSDLSVIRNLIDLYKSMGTIAPFMVLIEDATQV... | Function: Encapsidates the genome, protecting it from nucleases. The nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by N is coupled to RNA synthesis and all replicative products are resi... |
Q5MBR6 | MEVPIAAMTFAHPANVMTLASRQPKSKRSHISPATTAHRNLQTRLAHHHHATPASLPMAICNTVDKVINRFIDLPEQRPTVDPRRVLSGNFAPVDELPPTSCHVIRGSIPSCLAGGVYIRNGPNPQHRLPQRTHHLFDGDGMLHSLLIPSASSTLLSEPVLCSRYVHTYKYLLERETGGPVLPNFFAGFHGVAGLARAVVMIARVLAGQINLNKGFGLANTSITLFADCLYALCESDLPYSMHINPANGEVTTLGRCDFGGDLSFRMTAHPKKDPVTMELFAFRYNVFQPFITYFWFDRAGSKVADVPILSLQKPSVMHD... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids.
Catalytic Activity: a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal
Sequence Mass (Da): 63868
Sequence L... |
Q69NX5 | MASSAPSAPGLAPVAKPPPPPSKVKVATATVPTNGKIKQGARPMRVSAPPVEPRRRMNPLQRLAAAAIDAVEEGLVAGLLERGHALPRTADPAVQIAGNYAPVGERPPVRGLPVSGRLPACLDGVYVRNGANPLHAPRAGHHLFDGDGMLHAVRLAGGRAESYACRFTETARLRQEREMGRPVFPKAIGELHGHSGVARLLLFGSRALCGVLDASRGIGVANAGLVYHDGRLLAMSEDDLPYHVRVTHDGDLETVGRYDFHGQLDADGTMIAHPKLDPVTGELFALSYNVVSKPYLKYFYFTADGRKSRDVDIPVGAPTM... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids.
Catalytic Activity: a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal
Sequence Mass (Da): 62948
Sequence L... |
Q9C6Z1 | MACSYILTPNPTKLNLSFAPSDLDAPSPSSSVSFTNTKPRRRKLSANSVSDTPNLLNFPNYPSPNPIIPEKDTSRWNPLQRAASAALDFAETALLRRERSKPLPKTVDPRHQISGNYAPVPEQSVKSSLSVDGKIPDCIDGVYLRNGANPLFEPVSGHHLFDGDGMVHAVKITNGDASYSCRFTETERLVQEKQLGSPIFPKAIGELHGHSGIARLMLFYARGLFGLLNHKNGTGVANAGLVYFHDRLLAMSEDDLPYQVRVTDNGDLETIGRFDFDGQLSSAMIAHPKIDPVTKELFALSYDVVKKPYLKYFKFSPEGE... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids (By similarity).
Catalytic Activity: a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal
Sequence Mass (Da): ... |
Q9LRM7 | MQHSLRSDLLPTKTSPRSHLLPQPKNANISRRILINPFKIPTLPDLTSPVPSPVKLKPTYPNLNLLQKLAATMLDKIESSIVIPMEQNRPLPKPTDPAVQLSGNFAPVNECPVQNGLEVVGQIPSCLKGVYIRNGANPMFPPLAGHHLFDGDGMIHAVSIGFDNQVSYSCRYTKTNRLVQETALGRSVFPKPIGELHGHSGLARLALFTARAGIGLVDGTRGMGVANAGVVFFNGRLLAMSEDDLPYQVKIDGQGDLETIGRFGFDDQIDSSVIAHPKVDATTGDLHTLSYNVLKKPHLRYLKFNTCGKKTRDVEITLPE... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids. Contributes probably to abscisic acid synthesis for the induction of seed dormancy.
Catalytic Activity: a 9-cis-epoxycarotenoid + O2 ... |
Q1JQE6 | MRSSCVLLTALLALAAYYIYIPLPSSVSDPWKLMLLDATFRSAQQVSNLIHFLGLSHHLLALNFIIVSFGKKSAWSSAQVKVTDTDFDGVEVRVFEGPPKPEEPLKRSIVYIHGGGWALASAKIRYYDELCTTMAEELNAVIVSIEYRLVPKVYFPEQIHDVVHATKYFLQPEVLHKYSVDPGRVGISGDSAGGNLAAALGQQFNQDTNLKNKLKVQALIYPVLQALDFNTPSYQQNMNTPILPRYVMVKYWVDYFNGNYDFVQAMIVNNHTSLDVDEASALRARLNWTSLLPTSITKNYKPVMQTTGNSRIVQEIPQLL... | Function: Hydrolyzes 2-acetyl monoalkylglycerol ether (1-O-alkyl-2-acetyl-sn-glycerol), the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor (By similarity). May be responsible for the hydrolysis of cholesterol esters (such as cholesteryl (9Z-octadecenoate)) in macrophages (By si... |
Q6PIU2 | MRSSCVLLTALVALAAYYVYIPLPGSVSDPWKLMLLDATFRGAQQVSNLIHYLGLSHHLLALNFIIVSFGKKSAWSSAQVKVTDTDFDGVEVRVFEGPPKPEEPLKRSVVYIHGGGWALASAKIRYYDELCTAMAEELNAVIVSIEYRLVPKVYFPEQIHDVVRATKYFLKPEVLQKYMVDPGRICISGDSAGGNLAAALGQQFTQDASLKNKLKLQALIYPVLQALDFNTPSYQQNVNTPILPRYVMVKYWVDYFKGNYDFVQAMIVNNHTSLDVEEAAAVRARLNWTSLLPASFTKNYKPVVQTTGNARIVQELPQLL... | Function: Hydrolyzes 2-acetyl monoalkylglycerol ether (1-O-alkyl-2-acetyl-sn-glycerol), the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor . May be responsible for the hydrolysis of cholesterol esters (such as cholesteryl (9Z-octadecenoate)) in macrophages (By similarity). Also... |
Q8BLF1 | MRSSCVLLAALLALAAYYVYIPLPSAVSDPWKLMLLDATFRGAQQVSNLIHSLGLNHHLIALNFIITSFGKQSARSSPKVKVTDTDFDGVEVRVFEGSPKPEEPLRRSVIYIHGGGWALASAKISYYDQLCTTMAEELNAVIVSIEYRLVPQVYFPEQIHDVIRATKYFLQPEVLDKYKVDPGRVGISGDSAGGNLAAALGQQFTYVASLKNKLKLQALVYPVLQALDFNTPSYQQSMNTPILPRHVMVRYWLDYFKGNYDFVEAMIVNNHTSLDVERAAALRARLDWTSLLPSSIKKNYKPIMQTTGNARIVQEIPQLL... | Function: Hydrolyzes 2-acetyl monoalkylglycerol ether (1-O-alkyl-2-acetyl-sn-glycerol), the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor . May be responsible for the hydrolysis of cholesterol esters (such as cholesteryl (9Z-octadecenoate)) in macrophages . Also involved in or... |
F4HQM3 | MELSLVRLWNTCFPSFFYISTVLFLLTGGGVYSHSEYLIGLGSYDITGPAADVNMMGYANMEQVASGIHFRLRARTFIVSEPQGKRVVFVNLDACMASQIVKLKVIERLKARYGDLYTEQNVGISGIHTHAGPGGYLQYVVYIVTSLGFVRQSFDALVDGIENSIIQAHENLRPGSIFLNNGELLDAGVNRSPSAYLNNPSKERSKHKYNVDKEMTLLKFVDDQWGPVGSFNWFATHGTSMSRTNSLISGDNKGAASRFMEDWYEQNTAERSYSEEFISDEIPRRVSSLIENHQDSHHELLELASYFESQPGKPVTRISS... | Function: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid. Regulates sphingolipid homeostasis. Promotes oxidative stress resistance.
Catalytic Activity: an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine
Sequence Mass (Da): 86771
Sequence Length: 779
Subcellular Location: Secreted
E... |
F4KHQ8 | MTRWSMSMHCTLFLLFLLRLTCIFSDSDYLMGLGSYDITGPAADVNMMGYANMEQVASGVHFRLRARAFIVAEPYKKRIAFVNLDAGMASQLVTIKVIERLKQRYGELYTEENVAISGTHTHAGPGGYLQYILYLVTSLGFVHQSFNALVDGIEQSIIQAHENLRPGSILINKGELLDAGVNRSPSAYLNNPAHERSKYEYDVDKEMTLVKFVDDQWGPVARIMEDWFERENGCRSVDVESPRRVSSIISDPYDQDLMEMASSLLSTGGKTVTRMSSVARRVRSRFRHADKPRFVSAFCQTNCGDVSPNVLGAFCIDTGL... | Function: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid (By similarity). Promotes oxidative stress resistance .
Catalytic Activity: an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine
Sequence Mass (Da): 81838
Sequence Length: 733
Subcellular Location: Secreted
EC: 3.5.1.23
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Q8EIC6 | MQQNIIKVIVGSKNPVKVNAAANAMTLLFPEYQIQTIGMDAPSGVPAQPMTDSDTRQGAINRVNYCQQHAEADYYFAMEGGVDHFEFGPATFAYIAIAHQQRLSIGRGALLPLPRQVYQALEAGEELGHVMDRLFNTVNIKQKGGAIGLLTHGHATRESNYTQALILAMAPFLNPEIYL | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorpo... |
Q96YP8 | MFVAIGSTNKAKVEAVKEALKIIGLNADVISVNVESGVSSQPFCHETFVGAKNRAYNALNATNADIGIGIEGGICYYENKYLAFAVVYAANKEGLENFSFSMAFSLPYSMVKHILEGRELGEATDLIFSTKDSKQHEGAIGYLTKVITRKELYIQPVIAALYPFYNKIE | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorpo... |
Q5JJ32 | MKVAVGSTNPAKVEAVREVFLGIYGDVEVVPIEVDSGVPDQPVGLEETVKGAINRAKQAIEKTDADFGVGIEAGLYRVPETITGYMDVQFCAVVDREGRITLGHGPGFEYPPGVIRRVFEEGVEVGIAMGELVNDPELKRKIGAIGVLTHGMLVRKELNKLAVLMALVPRLNPEWYGL | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorpo... |
Q9KU27 | MPPIIKRRVMRKIIIASQNPAKVNAVRSAFSTVFPDQEWEFIGVSVPSEVADQPMSDEETKQGALNRVRNAKQRHPGAEYYVGLEAGIEENKTFAWMIVESDQQRGESRSACLMLPPLVLERLRQAKELGDVMDEVFGTENIKQKGGAIGLLTRHHLTRSTVYHQALILALIPFINPEHYPSA | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorpo... |
Q06389 | MGAKTSKLSKDDLTCLKQSTYFDRREIQQWHKGFLRDCPSGQLAREDFVKIYKQFFPFGSPEDFANHLFTVFDKDNNGFIHFEEFITVLSTTSRGTLEEKLSWAFELYDLNHDGYITFDEMLTIVASVYKMMGSMVTLNEDEATPEMRVKKIFKLMDKNEDGYITLDEFREGSKVDPSIIGALNLYDGLI | Function: Regulator of phosphatidylinositol 4-kinase PIK1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22011
Sequence Length: 190
Subcellular Location: Bud membrane
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Q4QTJ1 | MSKLITTEPLKSMAEVISNYVIQRESFSARNILNKNSLVKKEIRYDLEVPTSADSIWSVYSCPDIPRLLRDVLLPGVFQKLDVIEGNGGVGTVLDIVFPPGAVPRSYKEKFVNINHEKRLKEVIMIEGGYLDMGCTFYMDRIHIFEKTPNSCVIESSIIYEVKEEYAGKMAKLITTEPLESMAEVISGYVLKKRLQVFGFEIKPKLRFNLLLCLIICLVIAGGMFVAGVPL | Function: Involved in the biosynthesis of (S)-coclaurine, the common precursor of all benzylisoquinoline alkaloids such as morphine, sanguinarine, codeine or papaverine. Condenses dopamine and 4-hydroxyphenylacetaldehyde.
Catalytic Activity: (4-hydroxyphenyl)acetaldehyde + dopamine = (S)-norcoclaurine + H2O
Location To... |
D4GSH6 | MECDKCGRDAVMHAAYSGAHLCDDHFCASVEKRVRRRIREDNMLPRDASPENPQTWVIGLSGGKDSVVLTHILDDTFGRDPRIELVALTIHEGIEGYRDKSVDACVELAEDLDIHHELVTYEDEFGVQMDDVVEKDPENMAACAYCGVFRRDLLERFADELGADKLLTGHNLDDEAQTALMNFFEGDLKQVAKHFDASIGDFEKRRDAGEFIPRAKPLRDVPEKEVALYAHLKDLPAHITECPHSSEAYRGEIQQLLLKLEENHPGTRHSIMAGYEELAELTAREYRGEGRVDLNDCERCGSKTAGDVCRKCRLIESIEA... | Function: Required for thiolation of mcm(5)S(2)U at the wobble uridine position of tRNA specific for lysine (tRNA(Lys)). Probably acts by catalyzing adenylation of tRNA, an intermediate required for 2-thiolation. May also act as a sulfurtransferase that transfers sulfur from thiocarboxylated SAMP2 onto the uridine of t... |
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