ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q1WU20 | MINVLVAGFKGSMGNKTIHMVANNDKFKLAGVYNPVVTEKNVNEVAEFSDLDAPVYTDYEQIPVNDIDVWIDFTIPSAVYQNVKFALENKISVVVGTTGLKDEQIVELKEIAAKNGIGGLIAPNFGISAVLLMQFAKQAAKYMPDVEIIEMHHDNKLDAPSGTAINTAKLIAEVREEHQQGNPEETESLDGARGANYEGMHIHSVRLPGYVAHEQVLFGSKGEALTIRQDSFDRESFMTGVALAVEKIGDYNELMVGLENLL | 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): 28696
Sequence Length: 262
Pathway: Amino-acid biosynthesis;... |
B2GC12 | MTKVLIAGFAGAMGQQAVTLVKSLPGFELSAVVGHHLTDLDPTSYGLENSTTVYADREQVETGAADIWLDFTVPAAVFENVSYALRHGMAPVVGTTGLSDEQVEELQQLAKQNGLGGLIAPNFGMSAVLLMKFAKEAAAYFPEVEIIEMHHEDKKDAPSGTALATAKLISENRPAHETAPDSTESLPGARGGDYQGIKLHAVRLPGYVAHEQVLFGGSGEALTIRQDSFDRSSFMSGVKVGLEKVGTLTELVVGLENVL | 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): 27467
Sequence Length: 259
Pathway: Amino-acid biosynthesis;... |
Q8Y5Z6 | MRVAVSGFKGRMGHEVVKTVLREADLELVAVLDHEPKEKNINEMVEFSSLDVPVFGNLSEMLEEIKPDCVVDFTTPKVGYSNTKTILEHGVRAVVGTTGFTPEQISELRTIAESKKIGALIAPNFAVGAVLMMQFAQKAAKYFPNVEIIELHHDNKLDAPSGTGVKTAEMMAETREFVKQGAADEVELIEGARGAEYEGMRIHSVRLPGLVAHQEVIFGAEGQGLTIRHDSYDRISFMSGVALSVRKTKELETLIYGLENILD | 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): 28900
Sequence Length: 263
Pathway: Amino-acid biosynthesis;... |
A0L4Z4 | MTIKVGVTGVCGRMGRMLVEATHKAQGCMLGAASEYPGHTLIGADAGELAGVGKLGVLVGGDAETTFRDADVVIDFSVVEATLAHLRLALAQGTPIVIGTTGFSAAERQQIALAAERIPVVFAPNYAVGVNLLFKIAAEVAAVLGGEYDIEIVEAHHRHKVDAPSGTALGLGQAIAEAVERNLDEVAIYGRQGQTGARDPQTIGFSTIRGGDVVGDHTAMFMTDGERLELTHRASSRMTFAKGAVRAAKWVVEQKPGLYDMRDILGFK | 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): 28152
Sequence Length: 268
Pathway: Amino-acid biosynthesis;... |
Q67P64 | MQPIRVVLAGATGKVGQVLARALVQEPGFALTGAIARQGGGRNLAELVPLGGRPGPTVHGSLEEFLAAGGEADVLVDFSVAEAGRRTIPAAIEASIAPVVGTTGFQPGETETWAAMCRKRGLGGAFIANYAVGIMLLMRFAEEAHRFFPDVEIIEMHHKTKLDAPSGTALRTKARLERGRGDLAAAEVPVHSVRLPGLVAHQEVIFGGLGQTLTIRHDAPSREAYVPGVLMTCRWVLREKRVAFDLEEVAFPRT | 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): 27042
Sequence Length: 254
Pathway: Amino-acid biosynthesis;... |
Q2LTA0 | MLKAIVTGGGGKMGARIISLLEEEGGMQLTGVVEKKDHPAAGKDIGEFLGSGKRGIVIQSDLGFCIAGGDVIIDFTSHEASMRHMEMAAEHKRPIVIGSTGFSADEMDRIRKFAQNVPCVLAPNMSVGVNVMFKLLKIVAETLGDDYDVEILEVHHRLKKDAPSGTALKMAQVVAEALGRELDEVGIYERKGLIGERSKKEIGIQALRAGDIVGEHTVIFGAVGERLELIHRAHSRDNFARGAIRAAKWVVRQEPGLYDMQDVLGFRS | 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): 29069
Sequence Length: 268
Pathway: Amino-acid biosynthesis;... |
A0LEA6 | MVRAAVAGIAGRMGSRIAQLIRETDGIELAGGFEHSGHQAVNREISEIIGGSPTGLKVTSHIAQVLDTVDVVLDFTLAAASLEHLRQASARGKAMVIGSTGFAREQLEEAEKLAGRVPCVISPNMSMGVNVLFKVVGDVARLLGESFDVEIIEAHHRLKKDAPSGTALKLAQVAAGALGRNLEEVGVYARRGLIGERTGNEIGIQTIRGGDIVGEHTVMFAGSGERIEIVHRAQSRDNFARGAIRAALWVVRQPPGLYGMDHVLGMK | 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): 28338
Sequence Length: 267
Pathway: Amino-acid biosynthesis;... |
O25343 | MINKFKNFVSNYQQSNHYKEPLGFGIARVDIAPISKKILCATYPVLNWKDENLGSYAVFCNSLSKEKILKESASERVIEIDESFVLKALDFYTPFLNEAYSNKMAHKNIQVVLELLKALEENRLKNSDGESLYRLVILYEDKPCESVESAYMKLLALSLGKAPLRSLNLEGIFNQLSNAAWSGNKPYELEWLRMNEVALKMRDHFPSIDFIDKFPRYLMQLIPEFDNIRLLDSSKTRFGAYLGTGGYTQMPGASYVNFNAGAMGVCMNEGRISSSVVVGAGTDIGGGASVLGVLSGGNNNPISIGKNCLLGANSVTGISL... | 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): 44204
Sequence Length: 401... |
P41397 | MQQLQNVIESAFERRADITPANVDTVTREAVNQVISLLDSGALRVAKKIDG | Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA
Sequence Mass (Da): 5582
Sequence Length: 51
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): ste... |
O34916 | MKIEELIAIRRDLHRIPELGFQEFKTQQYLLNVLEQYPQDRIEIEKWRTGLFVKVNGTAPEKMLAYRADIDALSIEEQTGLPFASEHHGNMHACGHDLHMTIALGIIDHFVHHPVKHDLLFLFQPAEEGPGGAEPMLESDVLKKWQPDFITALHIAPELPVGTIATKSGLLFANTSELVIDLEGKGGHAAYPHLAEDMVVAASTLVTQLQTIISRNTDPLDSAVITVGTITGGSAQNIIAETAHLEGTIRTLSEESMKQVKERIEDVVKGIEIGFRCKGKVTYPSVYHQVYNTSGLTEEFMSFVAEHQLATVIEAKEAMT... | Function: Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
Catalytic Activity: H2O + N-acetyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + acetate
Sequence Mass (Da): 41557
Sequence Length: 374
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP p... |
B1YJ90 | MEYAIEMRRELHKIPEPGFKEFKTQAFILDQIRSYPEDRVSYDTFETGVFVRVKGLTGNRTIGYRADIDGLPIEEATGLPFCSEHPGFMHACGHDVHASIALGLLRRIVELPVMDDVVFLFQPAEEGPGGAEPMIKSPLFEKYRPSEMYGLHVAPEYPVGTIASRPGVLFASAREVHITIYGQSGHAAFPHLTIDTVVAQAALIMQLQTIVSRSINPMNCSVITIGKVDAGIRENVIAGRALLDGTMRALNGTDMEKLEQRVRDIIRGIEASFGVKIDLQFGNRYYEVVNDQRVVDKFSSFVKMNANYIECDAAMTGEDF... | Function: Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
Catalytic Activity: H2O + N-acetyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + acetate
Sequence Mass (Da): 41340
Sequence Length: 370
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP p... |
Q9K9H9 | MEPSLIDVRRALHRIPELGFEEYKTQTYLLDLIQSLPQDFLEVKTWKTGILVRVGGRKGEKTVAYRADMDGLPITEETGLPFVSQHEGRMHACGHDLHMTIAFGLLRHFAYHQPETHLLFIFQPAEEGPGGAKPMLDSEEFRMWWPDEIIALHIAPEYPVGTIATRKGLLFANTSELFIDLKGQGGHAAYPHLANDMVVAASHLVTQLQSVVSRNVDPLDSAVVTIGVIKGGTKQNIIAETARIEGTIRTLSIESMKKVKKRIEALVSGIEIGFSCQASIDYGSNYCQVWNDEERVARFIEYSQGREGVTFIECSEAMTG... | Function: Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
Catalytic Activity: H2O + N-acetyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + acetate
Sequence Mass (Da): 41544
Sequence Length: 371
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP p... |
Q5FKR0 | MTVLSEKELIQIRRHLHEIPELALQEKETHDYLLKVIKNLKQDHLTIVVPKTLPTAILGLVKGINPKKTIGYRTDIDALPVQEKTGLPFTSKHSGIMHACGHDIHMTVALGLLSYFSENQPKDNLLFFFQPAEESESGGKQAYEKGLFQGKFKPDEFYGLHDNPELPAGSIGCRMGTLFAGTTEINIDVIGKSGHAAFPQNANDTVVAAANLIMQIQTIISRSIDPIQSGVITLGKVNAGVIRNVIAGHTRIEGTIRGLTQKMILQIDRRLQDVCDGIAHSYNVEVNLELNQGGYWPVENDPKITKNFISYMKKNPKVNF... | Function: Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
Catalytic Activity: H2O + N-acetyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + acetate
Sequence Mass (Da): 42314
Sequence Length: 383
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP p... |
Q9CIS4 | MINLIEIRRQLHQIPEIGLEEYETQKYLLAIIQELTQNKPFIQVRTWQTGILVYLAGSQSQKTIGWRTDIDGLPIEELTDLPYASKNGRMHACGHDIHMTVALGLLEKMSESQPRDNLLFLFQPAEENEAGGKLMYDARAFENWLPDEFYGLHVRPDLKVGDIATNQHTLFAGTCEVELSFIGTGGHAAFPHTANDALVAAAYFITQVQTIVSRNVDPLASAVVTFGKMEAGTTNNIIAERAFLHGTIRSLTQEVNELTQKRLRELANGIAQSFNMEIELKLKQGGYLPVENHPKLAKELMEFFKKETKANLIDIAPAMT... | Function: Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
Catalytic Activity: H2O + N-acetyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + acetate
Sequence Mass (Da): 43100
Sequence Length: 384
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP p... |
O25002 | MDALEITQKLISYPTITPKECGIFEYIKSLFPHFKTLECGENGVKNLFLYRIFNPPKDHAEEKHAKENTKPLHFCFAGHIDVVPPGNHWQSDPFKPVIKEGFLYGRGAQDMKGGVGAFLSASLNFNPKTPFLLSILLTSDEEGPGIFGTRLMLEKLKEKDLLPHMAIVAEPTCEKVLGDSIKIGRRGSINGKLILKGVQGHVAYPQKCQNPIDTLASVLPLISGVNLDNGDEYFDPSKLVITNLHAGLGANNITPASVEIIFNARHSLKTTKESLKEYLEKVLKDLPYTLELESSSSPFITASHSKLTSVLKENILKTCH... | 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... |
Q5GS68 | MKIDPVELTKKLISFKSITPRDDGAIEHIAAILEKSGFDCEILEFGDNKTKVKNLYAKYINGVQNLCFAGHVDVVPPGQLKDWISDPFSPEVRDGLLYGRGATDMKSGIAAFITAMVDLVAEKFRFNGSISALITSAEESTEEYGTKAVLKWMESKHKKIDYCVVAEPTSSEKLGDTIKIGRRGSATFELICHGKQGHVAYPDLADNPIYKMISILNRIKDTTFDGGNKYFQPSNCEITTIDVGNSTDNVILDSITAGFNIRYNNMQTPDGLYKLIDEICFSVTNDYKLSMHSSRGAFLSTPDRNTDVMFDAINKVTNID... | 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... |
Q4USS4 | MTSDVLQLTCDLIARASVTPADAGCQALIADRLSAAGFACEHLRLGAVDNLWATHGSGAPVLVLLGHTDVVPPGPASDWASDPFAPQVRDGVLYGRGAADMKGSVAAFVVAAEQFVAAHPEHPGTLAVLLTSDEEGDAIDGVRHVARLFAERGQQIDWCITGEPSSTERLGDLLRVGRRGSLSGNLIVKGVQGHVAYPHKARNPIHLAAPALAELIARQWDDGFESFPPTSLQISNIHAGTGANNVIPGELQVAFNLRYTPHWNAETLEREIVALLERHALTYTLAWHRSGEPFYTPEGTLRRVAREVLGAFVGAPPEES... | 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... |
C1A8U3 | MSFVKMTGSGNDFVFFDGRTTPIDLVTQPEAIKAICNRYNGIGADGLVVLEPLQEEADVRVHYYNSDGTAADLCGNATLCSTAISAQWGITSASGMRLATGAGLINSRIDGLPAIALQPITDIRPDMPIAPATAQGRRVGFAVAGIPHLVILCEDADAVDVAGAGPALRRHEATGPAGANVNWVSPRPDGSWRYRTFERGVEGETLACGTGAVATAVLLRSWGLSDGATTTIRTSSGRDVEVDLEPLTAPDGRSLEGFRPTLRGEGRVVFRGEIAGL | 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): 28993
Sequ... |
B7KH06 | MGIEFTKYHGLGNDFILIDNRHGSEPMVSPEMAVEMCDRHFGIGADGVIFVLPGTSQTDYQMRIFNSDGSEPEMCGNGIRCLAQFIAELEKTTEVGKSYRIDTLGGLMTPRLEAQEQVTVDMGLPRLLGSEIPTTLVSRTEKVIDQPIEVAGQSWLVTCVSMGNPHCITFVEDVKSIALETIGPQFEHHVAFPQRTNTEFIEVLRPDYLKMRVWERGAGITLACGTGACASVVAGVLTGKSDRRCTVELPGGCLSIYWSETDGHVYMTGPAKRVFTGVYEM | 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): 30849
Sequ... |
Q5FQZ4 | MTLSFTKMHGLGNDFVVIDGRQNDPALETATIRHLCDRRFGIGCDQLVLLTPPTLAGADVHVRFFNPDGSEAGACGNASRCVAKFVGGAPTLQTAAGLLPTAQDGDLFTVDMGTPRLDWQDVPLSRACDTLHLPLHDAAACSMGNPHATLFGDAFRAEALGPGLERDPLFPERANIGFAQILSPIHMRLRVWERGAGLTLACGSGACAAVVNAVRRGLTERTCTVTMDGGDLRITWREDGHVFMTGPAVTVFHGTTA | 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): 27293
Sequ... |
Q0BS04 | MLIDFIKMHGLGNDFVVFDARKGPSLALSGSQAAAIADRRTGVGCDQLIVLEPSTVADAFMRIYNPDGSESGACGNATRCVADLLHRDGIAAPCMETVAGLLLAEINGNGICIDMGQPGLGWRDVPLAREMDTLFLPLEAPGLKMPAACSMGNPHATFFVADLAELDIPVTGPLLERHPLFPERANIGHAQMLSRSHIRLRVWERGAGLTLACGTGACATLVNAVRRGLAEREAVVELDGGQLLIHWREQDGHVLMTGPAATVFHGRIALESITG | 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): 29192
Sequ... |
A1WWB3 | MRFTKMEALGNDFVVLDGIRQRLHLTPETIRTLADRRRGVGCDQLLIAEPPAHIAADVRYRIFNADGTEVEHCGNGVRCLARFLVDEGLAAPGVLRIETDGRITEAEPRDDGQVSVDMGPPELEPARIPFQAPVRQEAYRLATSRGEQTIGAVSMGNPHAVLRVDDMTGAPVAELGPEIERHPRFPRRVNVGFMEVCTRDRIRLRVFERGVGETPACGTGACAAVVAGRLRDWLDAPVTVELTGGVLVIHWLGPGRSVWMTGPARTVFRGEIELPASAAATPRGPTR | 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): 31277
Sequ... |
B8CX90 | MELSFTKMHGTGNDFIMVNGSNYPDLDFSKLARQLCRRHFSIGADGLIIVLPPESVEHDFRMRIFNADGSEAEMCGNGIRCFAHYLRENNLTTRDVLKIETLAGIITPEIVSYNGDKSLIKVNMGRPHFKSEEIPVNIEDELDYVKNFPLKIGNKKLNINCVSMGNPHTIIFVEDVNQIPVSTWGQEIEHNPLFPQKTNVEFIQIQSEDEIIMRVWERGSGITLACGTGACASVVAGIKNGLLKNMVTVHLPGGDLNIEWQEQDVFMTGPAESVYTGKIVIQEG | 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): 31682
Sequ... |
B0TGR9 | MEFVKMHGLGNDFIVVNAMEPPLLDREDWEEIAVRICDRHYGIGGDGLILLFPSDKADIRWRILNSDGSEPEMCGNGIRCLARYVYERGIVAKRRIEVETLAGIIVPEIITDAAGAVTGVCVDMGEPRLQRHQIPMVGPEGPAVNQELVVGDAVVRVTALSMGNPHCLIYVNDIDEAPVTTLGPKVEVHPAFPAKTNVEFVQVVAPDEVQMRVWERGAGPTLACGTGACATVVGSVLNGYTDRKVTVHLAGGPLHIEWREENNRVYMTGPAVEVFRGELPL | 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): 30627
Sequ... |
A5F4I6 | MHFHFSKMHGLGNDFMVVDCITQNVFFSPELIRRLADRHTGVGFDQLLVVEAPYDPESDFHYRIFNADGSEVEQCGNGARCFARFVRMKGLTNKYTIHVSTKKGKMVLNVEEEDLITVNMGVPEFEPNKIPFRAKQSEKTYILRVGEHTLFCGAVSMGNPHVVTVVDDIRTAAVETLGPLLESHERFPERVNAGFMQVVSRDEINLRVYERGAGETQACGSGACAAVAVGILQGLLDEQVRVHLPGGELEIHWQGPGKPLYMTGPATHIYDGQISC | 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): 30651
Sequ... |
Q8D2T4 | MKFSKMHSLGNDFVIVNNIDKKNNISPIFIKKLSDRYTGIGFDQLILIEFFCKKYFYFKIKIFNSDSSESFQCINGIRCVFMFLKIKKLIKKNIAFIGNNLGLSKTLMTKNKLICVKIKPPRFYIEKDILVNPKYNNKEKIILRIFKKKITCYFVFVGNPHCIIISKNIEYNNFSLLSKYLLKNNIFPNKINISIMNILDFDLIKLKVYERGSGETQSCGSAAAAAAAVAIYYKKLNKKIKVNFSRGNLYVYWEKIGNFMSIIGPANHIYDGKINF | 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): 31989
Sequ... |
Q5GSB8 | MSSQSPKRMYGTGNNFVIIDSRSINNLNWNYREIANQNGCDQIIVITNSSAADCFMHIYNADGGEVEMCGNAARCVGYLIMSEKSTEYATIELVNKRILECFKVGGRSIKVNMGKPLFKWHEIPLSAKCDPLHLPIELEMLKDPVAVNIGNPHMVFFVDNISEIPLQSLGPKLEKHTLFPKKVNVNIAQVEKSGEISLRVWERGTGITASCGSAACAALIASVLRGYLITRQTSVNLPGGKLLIEWPDNIFMTGDIGFL | 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): 28565
Sequ... |
B7UP20 | MAYDYSASLNPQKALIWRIVHRDNIPWILDNGLHCGNSLVQAENWINIGNPELIGKRAGHPVPVGTGGTLHDYVPFYFTPFSPMLMNIHSGRGGIKRRPNEEIVILVSNLRNVAAHDVPFVFTDSHAYYNWTNYYTSLNSLDQIDWPILQARDFRRDPDDPAKFERYQAEALIWQHCPISLLDGIICYSEEVRLQLEQWLFQRNLTMSVHTRSGWYFS | Function: Toxic component of a hybrid type II/IV toxin-antitoxin (TA) system. ADP-ribosylates ssDNA in the sequence TTT/TCT. Its toxic effect is neutralized by cognate antitoxin DarG . May target ssDNA loops during DNA replication, probably modifies thymidine (Probable). Wild-type protein cannot be expressed at low lev... |
A0A0H3M0L1 | MITRYKPESGFVARSGGPDRKRPHDWIVWHFTHADNLPGIITAGRLLADSAVTPTTEVAYNPVKELRRHKVVAPDSRYPASMASDHVPFYIAARSPMLYVVCKGHSGYSGGAGPLVHLGVALGDIIDADLTWCASDGNAAASYTKFSRQVDTLGTFVDFDLLCQRQWHNTDDDPNRQSRRAAEILVYGHVPFELVSYVCCYNTETMTRVRTLLDPVGGVRKYVIKPGMYY | Function: Toxic component of a hybrid type II/IV toxin-antitoxin (TA) system. ADP-ribosylates ssDNA, preferentially in the motif TTTW. Its toxic effect is neutralized by cognate antitoxin DarG.
Catalytic Activity: a thymidine in DNA + NAD(+) = an N-(ADP-alpha-D-ribosyl)-thymidine in DNA + H(+) + nicotinamide
Sequence M... |
P0DV56 | MPQQGLAYPVPTLIYHITHLNNLQGILQRGGLLPYSQRPPTQQNVAYGHIQAHRAQVVVPVGPRGKLHDYVPFYFCPRSPMLYAIHTQQTDYQGDQRPILHLVSSAQKVAEARIPFVFTDRHAAVQYVCFFHKLEHLKALDWQAIQASYWANVREKKQAEFLVKDFFPWELVEEIGVIDKTIQAQVESILAQFPDLHHPPVRVRRSWYYKKRLCSASCEATF | Function: Toxic component of a hybrid type II/IV toxin-antitoxin (TA) system. Its toxic effect is neutralized by cognate antitoxin DarG. ADP-ribosylates ssDNA on the second thymidine of the consensus sequence 5'-TNTC-3'; the protein does not auto-modify. Has no activity on dsDNA in vitro. This leads to a decrease in DN... |
Q12084 | MDRKAVEEKRIVISIGGGHATGVGAIALDLQNTFKSLYNSINIRVINLDNMIEGNIKSYNNNDYDFDNILNLVYEKHAVTSQNDMIQHDYEDPIDLIIVCGCYALYDKRINEISQLKVFLDSDADKRLISLIKKKNVGSNEQLAQLITEYMDHLRPEMQQYIEPTRTFADLIIPSTNENLGRAVLVDGIVKAIEDTKSQIEGNNTNNKIRPRLWDFEAETMDLEKDRYYDLS | Function: Putative uridine kinase identified in a screen for mutants with increased levels of rDNA transcription.
Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 26595
Sequence Length: 232
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Subcell... |
Q9K491 | MKRKLIAAIGIAGMMVSIAACGGDSDDDGKKAGADGYAGETLTVWVMDGSSPDDWQADLAKDFEAKTKAKVKFEIQKWNGIQQKLTTALSEENPPDVFEIGNTQTPAYAKTGGLADLSDLKGEIGTDWSESLNKSAVFDGKQYAAPWFVVNRVVVYNKKIWADAGIKELPKTRDEFYNDLKTIGEKTDAEPIYLPGQNWYHFVGLVIGEGGELVKKDGDKYVSNLADPKVAAATETYKKFQALSKAPKDKDEATPQQGEIFAKGKTGSFIGMGWEGATAIATNPAIEKDLGYFTIPGPTADKPEGVFLGGSNLAVAAGSK... | Function: Part of the ABC transporter complex DasABC-MsiK involved in N,N'-diacetylchitobiose ((GlcNAc)2) uptake. Binds specifically to (GlcNAc)2. Can also bind to GlcNAc, (GlcNAc)3, (GlcNAc)4 and (GlcNAc)5, but it exhibits the highest affinity for (GlcNAc)2 . Involved in the control of morphological differentiation .
... |
Q9K490 | MTVQTERPPSGPSDVRKADGGGTGGTRARAASRAGALAPYLLLLPAAAATVLLLGWPLVKDGLLSFQNLNMAQLIQHVTEWTGFDNYKEVLTGEDFWRVTVRSIIFTAVNVVLTMVVGGLIGLLLARLGRVMRFVLMIGLVLAWAMPVVAATTVYQWLFAQRFGVVNWVLDKLGWHSMADFSWTGSQFSTFFVVTVLIVWMSVPFVAINLYAATTTIPDELYEAAALDGAGMWRSFTSVTLPFLRPFLYATTFLEVIWIFKAFVQVYTFNGGGPDRLTEILPVYAYIEGVGNQHYGMGAAIAVLTILILLGLTAYYLRIV... | Function: Part of the ABC transporter complex DasABC-MsiK involved in N,N'-diacetylchitobiose ((GlcNAc)2) uptake. Responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36132
Sequence Length: 328
Subcellular Location: Cell membrane
|
Q9K489 | MKRSLFGRVWPNVTAVVLFIGLVFPVYWMFATAFKPTGDIISENPVWFPTDITFEHFKTATEADHFWTYVSNSLIVTVCAVVFSLVIALAGSFALARMRFKGRRGFIVGFMLAQMAPWEVMVIAIYMIVRDASMLNSLVPLTLFYMMMILPFTILTLRGFVAAVPKELEESAMVDGCTRAQAFRRVILPLLAPGLMSTSMFGFITAWNELPLVLVVNKEAESQTLPLWLTSFQTVFGDNWGATMAASSLFAIPILILFVYLQRKAVSGLTAGAVKG | Function: Part of the ABC transporter complex DasABC-MsiK involved in N,N'-diacetylchitobiose ((GlcNAc)2) uptake. Responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30681
Sequence Length: 276
Subcellular Location: Cell membrane
|
O93884 | MALAKAASINDDIHDLTMRAFRCYVLDLVEQYEGGHPGSAMGMVAMGIALWKYTMKYSTNDPTWFNRDRFVLSNGHVCLFQYLFQHLSGLKSMTEKQLKSYHSSDYHSKCPGHPEIENEAVEVTTGPLGQGISNSVGLAIASKNLGALYNKPGYEVVNNTTYCIVGDACLQEGPALESISFAGHLGLDNLVVIYDNNQVCCDGSVDIANTEDISAKFRACNWNVIEVEDGARDVATIVKALELAGAEKNRPTLINVRTIIGTDSAFQNHCAAHGSALGEEGIRELKIKYGFNPSQKFHFPQEVYDFFSDIPAKGDEYVSN... | Cofactor: Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Function: Involved in assimilation of formaldehyde.
Catalytic Activity: D-xylulose 5-phosphate + formaldehyde = D-glyceraldehyde 3-phosphate + dihydroxyacetone
Sequence Mass (Da): 78137
Sequence L... |
Q5I396 | MVGSDGDGDGGGGEAHAPAAPAHHHRRPPRPRGGSGAIVEGFAAALRRRIRSGAAAAARASFGGDSGDEAASGEPSSSSSSSPSRRRGGDSNGAEASSAAGGGGGRGGGGDFSAFTFRAAAPVHRKAKESPLSSDAIFKQSHAGLFNLCIVVLVAVNSRLIIENLMKYGLLIRAGFWFNDKSLRDWPLLMCCLSLPAFPLGAFAVEKLAFNNVITDAVATCLHIFLSTTEIVYPVLVILKCDSAVLSGFLLIFIACIVWLKLVSFAHTNHDIRQLTMGGKKVDNELSTVDMDNLQPPTLGNLIYFMMAPTLCYQPSYPRT... | Function: Involved in triacylglycerol (TAG) synthesis. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59604
Sequence Len... |
A0A0P0WY03 | MAPPPSLAPDRGGGEPDDALRLRARAAAAAGDAPAPQQQQEQRHQEQQQQLLWYRASAPAHRRVRESPLSSDAIFRQSHAGLLNLCIVVLVAVNSRLIIENLMKYGLLIRAGFWFSGTSLADWPLLMCCLTLPTFPLAALMVEKLAQRKLISKHVVILLHIVITTSVLVYPVVVILKCDSAVLSGFVLMFLASIIWLKLVSFAHTNYDIRMLSKSIEKGVTHDISIDPENIKWPTFKRLSYFMLAPTLCYQPSYPRTTYIRKGWVVRQLIKCLVFTGLMGFIIEQYINPIVKNSKHPLKGNFLNAIERVLKLSVPTLYVW... | Function: Involved in triacylglycerol (TAG) synthesis. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55108
Sequence Len... |
Q5GKZ7 | MAISDEPETVATALNHSSLRRRPTAAGLFNSPETTTDSSGDDLAKDSGSDDSISSDAANSQPQQKQDTDFSVLKFAYRPSVPAHRKVKESPLSSDTIFRQSHAGLFNLCIVVLVAVNSRLIIENLMKYGWLIKSGFWFSSKSLRDWPLFMCCLSLVVFPFAAFIVEKLAQQKCIPEPVVVVLHIIITSASLFYPVLVILRCDSAFLSGVTLMLFACVVWLKLVSYAHTNYDMRALTKSVEKGEALPDTLNMDYPYNVSFKSLAYFLVAPTLCYQPSYPRTPYIRKGWLFRQLVKLIIFTGVMGFIIEQYINPIVQNSQHP... | Function: Major contributor to triacylglycerol (TAG) synthesis and oil accumulation in developing seeds. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA . Has a marked preference for oleoyl-CoA (18:1) and sn-1,2-dioleoylglycerol over vernoloyl-CoA and sn-1,2-divernoloylglycerol... |
Q5AUY3 | MTRTSPTLPVIILGAGMVGLTLAQALKKAGIPYEVYERDSAADTEKGRGWALTVHWALNALEECLPAELFNRLEEIQVDPTLDDSRRFCFLDLSTAIPKYVIPPSKRLRVNRRLLGNLLGEGLDINYNKTLSSFHVSPETPDSVTVTFTDGTSTTGCLLVGTDGRNSKTRRLLLGEEAGALNPLPVRSIGTTITMTPEQFAPIREIDPLLFQGSHPETGVYMWFSLVSSPTINGSKDTPNPFYEGQLIQSWLYKSEKDAVPETDADRLALFKNNAQHFQRRLREAIETLPEDSKVLHIKLVDWVPVDWDNRGGRVTLAGD... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives . The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produc... |
Q5AUY2 | MTEQPPQNHSVDLNQNEDNNENDYRSSSATDAERPCEPKIEESTAKPPTGPPAPPPPPNGGLVAWLHVIGGFMLFFNTWGIMNAFGVFQTYYESGALFERSSSDISWIGSIQATMLLLVGFFTGSIYDRGYLRALLVVGSFCIVFGHMMLSLCKTYGQVLLAQGFCVGIGAGCLFVPCVSVLPTYFSSRLGTALGLAVSGSSMGGVIYPIVLNELIGPLGFGWSVRVIGFIALGTLLVPIAVMKQRVKPPRARALIDWSAFSDIPYMAFTLASLLAFMGLFALLFYISYFGAAKPITDTRMAFYIVPILNAASCFGRTIP... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4- dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives . Is probably involved in the transport of the metabolites to the environment (Probable).
Location Topology: Multi-pass membrane prote... |
Q5AUY1 | MTIRIPSGEEADYTLHLPRILCLHGGGTNARIFRMQCRVLERFLRSTFRFVYAEAPFAAQPGSDVTSVYKDHGPFKAWLRCTAADPDRSAQEVVKKINLSIATAMYDDDMRGATGEWIALLGFSQGAKVAASILYAQQTIQQRLGERAATRPRFRFAVLMAGRGPLVWLLPETSSGPGSIPMGLVDAASPSMLDSEPELPTDSTEHMLRLPTLHVHGLRDPGLSLHRRLLRSYCQSDSVSLVEWEGEHRVPLKTKDVTAVVDQIYALARDTGVLDSWC | Function: Esterase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives . The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation ... |
Q5AUY0 | MKSVLASGALTLAFSLAALAADAFQASSWDSTHIIRRDVVIVGGGAAGTYAAIRLKDHGKSVVLVERRDRLGGHAVTYKDPNTGGSVDYGVQVYDNNTVVRDFFSRLNTPLADLSFASFGKPVYADFEEGMLLNLTAGTLGQDYINELNKYPYLDNGFELPDPVPEDLLLPWVEYIGKYNIDLSTAIATLARPAVTGNLLNILAIYVFNNLNHLLLHEMSGAVVVNANRDNSQLYRNAVSELQPDLLLRSRVVAGQRRTRKRDGVRLVVDTPTGRKLIIAKQLIVGMPPILDNMRTFGLDSHEHSVLSHIYGLPYYGGVV... | Function: FAD-dependent oxidoreductase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives . The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produ... |
P83376 | SHQDCYEALHKCMASHSKPFSCSMKFHMCLQQQ | Function: Has antibacterial activity against Gram-negative bacteria E.coli JM109 and DH5-alpha, H.influenza IID 983, and V.vulnificus RIMD 2219009. Has antibacterial activity against Gram-positive bacteria S.aureus IID 1677, B.subtilis RIMD 0225014 and L.monocytogenes VIU206. Possesses antifungal activity against S.cer... |
P80346 | MLGKIALEEAFALPRFEEKTRWWASLFSVDPEIEHADKYGVGYQILSYTAPGVQDIWDPVEAQAGEVGVDRILSIDYPFETFEDAAVVLRRDVQTYGFIGALVNDTQRTGPMGNNQEEAYNINDYIAEQIRDKPDRFGAFTLSMHNPQEAGRDNAARLFERNPTGTIYEKLGAFRDYDAKVKAEITDINKLRIENASWDIFWQTDTEAQALAVEDADVWFDGAEFYDNAAMQYVIAYGAKQADIYGPINHWFEDRLLGLAETCKWLVGPDLSFAHGVSLHVLGMTVNGVFDR | Catalytic Activity: 2,3-dihydroxybenzoate + H(+) = catechol + CO2
Sequence Mass (Da): 33001
Sequence Length: 292
Pathway: Aromatic compound metabolism; benzoate degradation via hydroxylation.
EC: 4.1.1.46
|
Q8SRB2 | MMHRGYGGDRRGFRPSFRSDRNSRYAPRTRREPQRYDPMPELAPVEFQKNFYQEAESISRMTPSEVSSFRKTNEMIVKGTNVPHPIQKFEEAGFSSEVVSSLVEKGFSEPTAIQGQGWPMALSGRDMVGIAQTGSGKTLSFILPALVHAKDQQPLRRGDGPIVLVLAPTRELVMQIKKVVDEFCGMFNLRSTAVYGGASSQPQIRALHEGAEVVIATPGRLIDLHDQGHAPLSRVTFLVLDEADRMLDMGFEPQLRKIIPKTNANRQTLMWSATWPREVRGLAESYMNEYIQVVVGNEELKTNSKIKQIVEVCSGREKED... | Function: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 55696
Sequence Length: 495
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases an... |
Q4IF76 | MSGYDGGYSGGGGRGGGGYGGGGYGRDRGGDRGGDRNGGGFGGRSNGNGYGGGGYGGGGGGYGGGGFGGGAGGDRMGALGSGLKNQEWDINSLPKFEKSFYKEHPDVETRSDADVEAFRRKHQMTIAGSNVPKPVETFDEAGFPRYVMDEVKAQGFPAPTAIQSQGWPMALSGRDVVGIAETGSGKTLTYCLPSIVHINAQPLLAPGDGPIVLVLAPTRELAVQIQEEMKKFGRSSRIRNTCVYGGVPKGPQIRDLSRGVEVCIATPGRLIDMLEAGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIIGQIRPDRQTLMW... | Function: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 60129
Sequence Length: 554
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases an... |
Q7SBC6 | MSGSYGGGGYGGRGGGGGGYSNGYDRNGGGYSNNYSSHGGSNGYGGGGGGYGGGGGGYGGGGYGGGGGGDRMSALGAGLQKQNWDMSALPKFEKSFYQEHPSVANRSPAEVDKFRADHSIAVFGNNVPKPVETFDEAGFPRYVMDEVKAQGFPAPTAIQSQGWPMALSGRDVVGIAETGSGKTLTYCLPAIVHINAQPLLAPGDGPIVLILAPTRELAVQIQQEISKFGKSSRIRNTCVYGGVPKGPQIRDLSRGVEVCIATPGRLIDMLESGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIIGQIRPDRQTLMWSATW... | Function: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 60200
Sequence Length: 562
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases an... |
A7E449 | MSYGGGYGGGRGGGNGYGNGDSSYGRGNSYSNGYSNGGSNGYSGGGGGGYGGGRGGSGGGNVNGYSGGGGGYGGGGGYGGGGGAGGDRMNNLGANLQKQNWDLNTLPKFEKSFYKEDPVVAARSEEDVAKFRAQHNIAVQGPNIPKPVETFDEAGFPAYVMTEVKAQGFPAPTPIQSQGWPMALSGRDVVGIAETGSGKTLTYCLPAIVHINAQPLLAPGDGPIVLVLAPTRELAVQIQQEITKFGKSSRIRNTCVYGGVPKGGQIRDLAKGVEVCIATPGRLIDMIESGKTNLRRVTYLVLDEADRMLDMGFEPQIRKI... | Function: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 60982
Sequence Length: 572
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases an... |
A7TTT5 | MGYGRDQQYNKSNFNSRGGDFRGDRSSDRNSYNRDRNDNFGQRGGNQGGRSFNQPQELIKPNWEEELPNLPVFEKNFYQEAESVKARSDQEINEFRREHEMTITGHDIPKPITSFDEAGFPDYVLEEVKAEGFEKPTGIQCQGWPMALSGRDMIGVAATGSGKTLSYCLPGIVHINAQPLLSPGDGPIVLVLAPTRELAVQIQKECSKFGSSSRIRNSCVYGGVPRGQQIRELSRGAEIVIATPGRLIDMLEIGKTNLKRVTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVKQLAHDYLNDPIQVQ... | Function: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 50024
Sequence Length: 441
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases an... |
P24783 | MTYGGRDQQYNKTNYKSRGGDFRGGRNSDRNSYNDRPQGGNYRGGFGGRSNYNQPQELIKPNWDEELPKLPTFEKNFYVEHESVRDRSDSEIAQFRKENEMTISGHDIPKPITTFDEAGFPDYVLNEVKAEGFDKPTGIQCQGWPMALSGRDMVGIAATGSGKTLSYCLPGIVHINAQPLLAPGDGPIVLVLAPTRELAVQIQTECSKFGHSSRIRNTCVYGGVPKSQQIRDLSRGSEIVIATPGRLIDMLEIGKTNLKRVTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVKQLAADYLNDPIQVQ... | Function: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing . Associates directly with chromatin, correlating with transcriptional activity . Required for assembly of mRNA-binding proteins YRA1, NAB2, and MEX67 onto poly(A)+ RNA .
Catalytic Activity: ATP + ... |
Q4PEX7 | MPQVAASSSNVGPSSAAASSASHVQEVAKSASDPPKHTSFSSIGISPMLIRSLASLQIKVPTPIQSLTIPSVLEGRDLVGGAQTGSGKTLCFALPILNKLIKDMVGGFAVVLTPTRELGVQLHEQFVAVGEGARMGLRCALVLGGMDMMKQASELANLRPHVIVATPGRLVDHLRSGGGEEWGLRRCKFLVLDEADRLLTDTFKPELEYLYSVLPSAKTLQTLLFTATLTEQVVEFANAKRPEGKPAPMVCKIEMDTKTPETLEQRYVFVPSHVREPYLYHILRHPPIKPSSERVRKLNAKHQADRERKEENQRKSGKRR... | Function: ATP-binding RNA helicase involved in 40S ribosomal subunit biogenesis and is required for the normal formation of 18S rRNAs through pre-rRNA processing at A0, A1 and A2 sites. Required for vegetative growth (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 58618
Seque... |
A2QCW6 | MKRKLDANDVPSPEVAETKETSDADEADFESLNLDPRLRQALIKEKFTKPTPVQAKAIPLALAGKDILARAKTGSGKTAAYVLPILQTILQKKAADPSLKATTGLILVPTRELAEQVQKVVTTFAAFCGKDVRSVNLTQKVSEAVQRTMLSDYPDIVISTPARVIANLGNSSLSLDNLTHLVIDEADLVLSYGYDEDINALSKAIPRGVQTFLMSATLTSEVDTLKGLFCRSPVVLKLEDKEEKGAGVSQFVVKCAEDEKFLLTYVIFKLQLIKGKVIIFVGDIDRCYRLKLFLEQFGVKSCVLNSELPVNSRIHVVQEF... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 68571
Sequence Length: 616
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
A6SNX1 | MKRKLDANDVPVPTEGSDAIKENVTFASLGLDARLLQGIAKQNFQSPTLVQSKAIPLTLEGRDILARAKTGSGKTAAYLLPILHSILKRKELSSTQCTTALILVPTRELADQVYKTVESFTAFCAKDVRAVNLTQRVSDAVQRSLLADSPDIVIATPARASLNANTSALSLANLTHMVIDEADLVLSYGYDEDLQNVAKIMPKGVQTVLMSATLTSEVETLKGLFCRNPEVLKLEEAEDEGEGVSQFVVKCAEDEKFLLTYVIFKLKLIKGKCIIFVGDIDRCYRLKLFLEQFGTRSCILNSQLPVNSRIHVVEEFNKNV... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 67559
Sequence Length: 607
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
Q5A4P9 | MSTSASSSYLDDETTWDSFNLDPRLLQAIDQLGFSNPTLIQSSAIPLALEEKRDIIAKASTGSGKTAAYCIPIVNNLLTDDSSQGIKSIILVPTRELSNQVFQFVEKLLTFSTNKINVLNLSSSYSDQVLNSLLVNKPEIIISTPAKLIQILEKNEKNIDLSTVKNLTIDEVDLVLSFGYLDDLKKLESYLPVKKNLQTFLMSATVNDDLDDLKQRYCTKPAILKLNEDSANQNNLVQYYAKTTEFDKFLLAYVIFKLNLIKGKTIAFVNNIDRGYRLKLFLEQFGIRCCILNSELPINSRLHIVEEFNKNVYHLLIATD... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 65186
Sequence Length: 574
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
P0CR11 | MLSKSNQPSDALLDADFSFSQPPFSTLIDSRVLVALADQKFAHPTLVQAKAIPLLLEGKDVLARARTGSGKTAAYIVPAVQKILEAKADLSPASAEYQATRAIILVPTKELALQVSSFTKNVTKYCDGLVQCVDVAAGGASIQRVLLNDKPDIVISTPTKLLSLLQSKSLSLSQLSFLAIDEADLLLSYGFKDDLTRIMDPTSGWIPKLGVQGCLMSATLSDDVEGIKGLVLRNPAILTLSEPASASSLLSQHYTHTSERDKFLLIYVLLKLKLIRGKSIIFVNDVERGYRVKLFLEQFGVKCCVVNSELPLASRYHVVE... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 68915
Sequence Length: 627
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
Q3E9D5 | MAVSGFEGFEKRLELRFFDDDKPITKNPMGLRLIDFESLDQVLNEVQCTVVSAVANRSFDAYVLSESSLFVYPTKIIIKTCGTTQLLKSIRPLIHLARNLGLTLRACRYSRGSFIFPKAQPFPYTSFKDEVIVVEESLPKSLCYRKASVMTPSNNPSRAWHVFTASADVESDEHVVVVEVCMTELDRVNARSFFKRKGDEKNNSDSAGKEMTRLSGIDNINANAYICDFAFDPCGYSMNGVDGDRYSTIHVTPEDGFSYASFECGLSLYDNGHEDISEVLSRAIDVFRPSDVSIATTYGGEDYNHEVTKRVERVLAKKLD... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Essential for biosynthesis of the polyamines spermidine and spermine. Essential for polyamine homeostasis, and normal plant embryogenesis, growth and development.
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme inv... |
P50244 | MSSCKDSLSLMAMWGSIARFDPKHERSFEGPEKRLEVIMRVVDGTHVSGLLAHDDDVWQKVIDAICAHIVSREFNEYIRSYVLSESSLFVMKDRVILITCGTITLLNCVPLICEAVSTVCGEVEWVSFMHKNYSFPWEQKGPHLSMAEEFKTLRSHFPSGQPFIFGPIDSDHYFLYFHSDVVQPSCSDDAQLSMTMYGLDRNQTKHWYSDKMLPTGPETAVIREATGLSEVVDDSWILHDLQYEPCGYSINAIRGSEYQTIHITPEEHCSFASYETNTCALNYSKCICGVLRVFDPERFSVIVFIDPDSAVGKSYHSGGT... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: In association with the catalytically inactive AdoMetDC prozyme, catalyzes the decarboxylation of S-adenosyl-L-methionine which is essential for the biosynthesis of the polyamine spermidine. Required for growth and survival during the bloodstream life c... |
P34039 | SSMFVWNTKLILKTCGTXL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: S-adenosylmethionine decarboxylase is essential for the biosynthesis of spermine and spermidine. The alpha subunit contains the active site.
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturatio... |
O02655 | MSATSATNFAVQTHPVKAPDEEYFFEGAEKLLELWFCSSTQNETRSLRIIPREEIDAMLDIARCKILHSKHNESIDSYVLSESSLFISDNRVILKTCGTTRLLAALPVIMQLAGAYAGLDQVQSVYYSRKNFLRPDLQPSLHKNFDAEVEYLDSFFVDGHAYCLGSLKQDRWYLYTFHREVEFPAHKQPDHTLEILMSDLDEEVLHKFTKDYAVDGNDCFMRAGIDKIIPAGADVHDELFDPCGYSMNAYMNDTDQYATIHVTPEKAFSFASFETNQDLVCLYSQTRKVLQCFRPNKILMTVFANDISEKGKDAQQQLWD... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Essential for biosynthesis of the polyamines spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
PTM: Is synthesized initially as an inactive proen... |
Q8T1E3 | MPILSTEIFNEADAGFVYQSNSNDYSDGFEGPEKKLDIRFGPISKGSVKSIAGSPSKVGLRTIDKEKWQTVLDSARCTIISQTSNDHMDSYVLSESSLFVYPRRAMIKTCGTTTLLHLIAKMVQVGKECGLEVEMVVFSRKNLNQPSKQVFPHCSFSDEVNFLNKIFDGQAYVMGDVNKDHWNLYIADFRKNPTLQRTEQTFEVMMHDLDETVMKQFFKREGVSAWDTTVNSGIADLLPGSMIDDFQFDPCGYSMNGLLNEFYWTIHITPESHCSYVSFDTNVALADYNQLLAKVLNVFKPGRFTAALYAEDGAPCGDPY... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: S-adenosylmethionine decarboxylase is essential for the biosynthesis of spermine and spermidine. The alpha subunit contains the active site (By similarity).
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves ... |
P91931 | MLENGSHFFEGVEKLLEIWFEESSNGDDDLRNISRSDWENVLSNVNCQIISTSKNDIIDAFVLSESSMFVSKRRWILKTCGTTTPLKCLGQLLKLAEANGYNVVADLFYSRKNFTRPEAQITPHQGFTEEVTYLDSIFPNGRSYCLGSMNLECWYLYTFSRSDIKITPQLISDEKNVDSDPDQTIEILMQDLDPETMSIFYKNKFNDANGATVKSGIDTILPTMHIDDFLFDPCGYSMNGINDKGEYMTIHITPENQFSYVSFETNVALSNYRKLINQVINTFKPGKFIVTIFANKCSLAYETMKELEVEYSQGSHWKRT... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Tw... |
P17707 | MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQKIEGFKRLDCQSAMFNDYNF... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels.
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme i... |
Q72W72 | MILTGKEIQKRIGNDIVITPYSEKQLNPNSYNLRLHEELLVYTELPLDMKKPNPAEKLVIPESGLLLKPGILYLGRTLESTETHNLVPMLEGRSSIGRLGMLVHVTAGFGDVGFKGFWTLEISVIQPLIVYPGVEVCQIFYHTLEGQITEYTSGKYQANRGIQTSMLYKDFEK | Function: Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
Catalytic Activity: dCTP + 2 H2O = diphosphate + dUMP + NH4(+)
Sequence Mass (Da): 19528
Sequence Length: 173
Pathway: Pyrimidine metabolism; dUMP biosynthe... |
Q2FQM7 | MILVDWQITDRIERGYIGIDPYNPELIQPNSIDIRLGNHFVWYTPGDEIIDPYIRDTVTGGTEEMTAESIVLHPGQFVLAETMEAIRLPDNIVASIEGKSSIARLGIELHQTGGWIDAGFAGSITLEMCNVNQRPVRMHAGMPIGQLVFYTTERALCPYNAKKDAKYLNQRQATLSRYYENKKRA | Function: Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
Catalytic Activity: dCTP + 2 H2O = diphosphate + dUMP + NH4(+)
Sequence Mass (Da): 20901
Sequence Length: 185
Pathway: Pyrimidine metabolism; dUMP biosynthe... |
Q57872 | MILSDKDIIDYVTSKRIIIKPFNKDFVGPCSYDVTLGDEFIIYDDEVYDLSKELNYKRIKIKNSILVCPLNYNLTEEKINYFKEKYNVDYVVEGGVLGTTNEYIELPNDISAQYQGRSSLGRVFLTSHQTAGWIDAGFKGKITLEIVAFDKPVILYKNQRIGQLIFSKLLSPADVGYSERKTSKYAYQKSVMPSLIHLDNHKKD | Function: Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate. It also acts as a dUTP diphosphatase with a lower affinity for dUTP than for dCTP.
Catalytic Activity: dCTP + 2 H2O = diphosphate + dUMP + NH4(+)
Sequence M... |
Q8TYK5 | MTVLSDRDIKRALEEGDIVVKPLEEEYLEEALGPASLDLRLGNEFVVFKTLHKPCIDPTVDAGENTERIVIDEDEEFVINPGELVLAVTHEWIEINAPDITGVLHGRSSLGRLGIQAHVEAGYVDPGWRGRLTLELVNFNPMPVKLRPGMRVVQIVFHRLSSPAERTYAESSGKYHGDERPSPSKMHLDFCRG | Function: Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
Catalytic Activity: dCTP + 2 H2O = diphosphate + dUMP + NH4(+)
Sequence Mass (Da): 21593
Sequence Length: 193
Pathway: Pyrimidine metabolism; dUMP biosynthe... |
O27875 | MAILSDRDIKRYIEEGLITIDPLDDPERQIQPSSVDLRIGNEFKGFRVIRKPCIDPKDPSDIESYMETFHVEDGPFIIHPGEFALATTHEYIALPEDLVARVEGRSSIGRLGITMHVTAGYIDPGFHGRITLEISNIGKMPVALYPRQRVCQIVFETMTSPAERPYGHPSRDSKYIGQTRPQTSRIKDDYEIRNSRL | Function: Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
Catalytic Activity: dCTP + 2 H2O = diphosphate + dUMP + NH4(+)
Sequence Mass (Da): 22427
Sequence Length: 197
Pathway: Pyrimidine metabolism; dUMP biosynthe... |
B3R622 | MSIKSDKWIRRMAEQHGMIEPFEPGQVREADGRKIVSYGTSSYGYDIRCADEFKIFTNINSTIVDPKNFDEKSFVDFKGDVCIIPPNSFALARTMEYFRIPRSVLTICLGKSTYARCGIIVNVTPFEPEWEGYVTLEFSNTTPLPAKIYAGEGCAQVLFFESDEICETSYADRGGKYQGQHGVTLPKT | Function: Catalyzes the deamination of dCTP to dUTP.
Catalytic Activity: dCTP + H(+) + H2O = dUTP + NH4(+)
Sequence Mass (Da): 21202
Sequence Length: 188
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.
EC: 3.5.4.13
|
B3Y522 | MLPYNQDFYNEDEALKDDHCEGAGNVSNPPTLDEAIKRSQDFLLSQQYPEGYWWAELEGNPTITSHTVILYKILGIEDEYPMDKMEKYLRRMQCIHGGWELFYGDGGQLSVTIESYVALRLLNVPPTDPALKKALKFIIDKGGVXKSRMFTKICLALLGCFDWRGIPSLPPWVMLLPGWFLSSIYETACWARGCVVPLIVVFDKKPVFKVSPEVSFDELYAEGREHACKTLPFCGDWTSHFFIAVDRVFKMMERLGVVPFQQWGIREAEKWLLERQEDTGDFLGVYPPMFYSVVCMKTLGYEVTDPVVRRALLSFKKFSI... | Function: Squalene cyclase producing the tetracyclic triterpene dammaradiene.
Catalytic Activity: squalene = dammara-20,24-diene
Sequence Mass (Da): 77463
Sequence Length: 685
EC: 5.4.99.37
|
Q7UU94 | MKETPIMILSGQDIQSRLGKDIVIDPFDPSRLSPNSYNLTLHDELLVYEEVVLDAASPNRYRRLPIPEEGLTLQPGTLYLGRTTEHTETHGLVPIIQGRSSLGRLGLFLNPGGSLGHAGYRGTWTLELHCVQPVRIYPHIQICQITYWEVSGDSPEEASEKYQNSNDIQPSLMHRELGYDDRDTQLELGFDEAIRSTP | Function: Catalyzes the deamination of dCTP to dUTP.
Catalytic Activity: dCTP + H(+) + H2O = dUTP + NH4(+)
Sequence Mass (Da): 22297
Sequence Length: 198
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.
EC: 3.5.4.13
|
Q2RQK4 | MKLSDTDIRRYMAEGRIAIDPVPGEDAIGAMSVDLQLGDSFRVFVPGKVSHVDLAPPGGIKGRDIEALMGHVEVGENEAFYLHPGEFALGITIQRVRLPADVAGRLDGRSSLARLGLMVHATAHTIDPGWDGRITLEFFNCGPLPLAMRPGMRICAISFEALMSPTSKPYAASPTAKYKDQLAPLPSRLASDQSA | Function: Catalyzes the deamination of dCTP to dUTP.
Catalytic Activity: dCTP + H(+) + H2O = dUTP + NH4(+)
Sequence Mass (Da): 20938
Sequence Length: 195
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.
EC: 3.5.4.13
|
Q9ZE77 | MAIMSDKWIKDAVMNQNMIRPFAAKQVRVHNKEKIISYGLSSYGYDARVSNEFKIFTNINSTTVDPKNFSEYNLVDREVDACIIPPNSFALGRTIEYFKIPRDVLVICVGKSTYARCGIIVNVTPLEPEWEGHVTLEFSNTTPLPAKIYANEGACQFLFLKSDQICDTSYAERQGKYMKQVGVTLPLT | Function: Catalyzes the deamination of dCTP to dUTP.
Catalytic Activity: dCTP + H(+) + H2O = dUTP + NH4(+)
Sequence Mass (Da): 21277
Sequence Length: 188
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.
EC: 3.5.4.13
|
Q980T7 | MILSDRDLKYYLEKSWIKIQPLREDTIRENGVDLRVGNEIARFKKTDKIFDPDNPDPSFFQTEKGEEFIIQPYEHVLLTTEEYIELNNDVMAFVNLRSTFARLGLFIPPTIVDAGFKGQVTIEVVGSSFPVKLKRSTRFIHLIFARTLTPVEYPYQGKYQGQKGVTLPKFNSQISSFYYQHQSI | Function: Catalyzes the deamination of dCTP to dUTP.
Catalytic Activity: dCTP + H(+) + H2O = dUTP + NH4(+)
Sequence Mass (Da): 21408
Sequence Length: 184
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.
EC: 3.5.4.13
|
D2Z025 | MIDLIVSQGRVADRAAWMIEGAARTARALEERYGLKGHYVGEPAPHADDDWSVALPQARETLVAVREAATESIKGDNLTVLVNNTCSVSLATLPVVAREHPDAVVLYIDGHGDFNTPETTDTGYLGGMVLSGACGLWDSGHGAGLRPEQAVLVGSRDIDEGERELIRKAGVRVIPPGEATAQAVLDAVKDAPVWIHIDWDVLEPGSIPADYTVPDGMLPAQIRAVFEAIPAERLIGVELAELNAPADSERAEQAVAVILDMVAPAFDAAAARP | Function: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the hydrolysis of N(omega)-hydroxy-L-arginine (NHA) to yield hydroxyurea (HU) and L-ornithine.
Catalytic Activity: H2O + N(omega)-hydroxy-L-arginine = hydroxy... |
D2Z026 | MIRMRTPSTLPFTKMHGAGNDFVVLDLRDGPDPSPELCRALADRHKGVGCDLVLGIREPRSARAVAAFDIWTADGSRSAQCGNGARCVAAWAVRAGLARGPRFALDSPSGTHEVDVLDADTFRVALAVPRFAPESIPLFGHDGEQDLYEADLGDGTRVRFAAVSMGNPHAVIEVDDTATAPVARVGRAVQASGLFLPTVNVGFARVESRDRVHLRVHEYGAGETLACGSGACAAAAVLMRRGRVDRNVSVVLPGGELRISWPDDAADVLMTGPAAFVYEGTFLHASV | Function: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the stereoinversion of O-ureido-L-serine to O-ureido-D-serine.
Catalytic Activity: O-ureido-L-serine = O-ureido-D-serine
Sequence Mass (Da): 30382
Sequence Le... |
D2Z027 | MPLFNSILDTIGRTPIVRLQRMAPEHTSVYVKVESFNPGGSVKDRLALSVVLDAEAKGLLKPGDTIVECTSGNVGIALAMVAAARGYRFVAVMGDTYSVERRKLIRAYGGKLVLFPGHLGSKGGNLIADELAEKYGWFRARQFDNPANPSYHRETTASEILADFAGKRLDHFVTGFGTTGTLTGVGQMLRVARPEVRVVALEPSNAAMLARGEWSPHQIQGLAPNFVPGVLDRSVIDDLVTMDEVTARDTSRRLAAEEGIFAGISAGATVATALSIAEHAPEGTVLLAMLPDTGERYLSTFLFDGVDEGSDDAWLASLDT... | Function: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent . Catalyzes the addition of hydroxyurea on O-acetyl-L-serine (OAS) to yield O-ureido-L-serine. It prefers sulfide as the second substrate, followed by hydroxyurea, L-hom... |
D2Z028 | MREFIPPASRFIELPDGFAMRRGGALYGARIAYETFGSLNAARDNAVLVLTGLSPDAHAASRPDDPTPGWWEAMVGPGKPVDTDLWHVICVNSLGSCKGSTGPASTDPRTGEPYRLSFPELSIEDIADAAAHTVRALGISRLACVVGASMGGMSALALLARHPELARTHISLSGAVHALPFSIAVRSLQREAIRSDPGWLQGHYDEGEGPRRGMLTARKLGMMTYRSAQEWDCRFGRTRIGERRRADQGRFGPEFEVESYLDFHAQRFADRFDPNSYLYLSHAMDQFDLGDGGGGGGGAPGALSRMRVERALVMGARTDI... | Function: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-serine to yield the activated serine, O-acetyl-L-serine. It prefers L-serine over ... |
D2Z030 | MGILALVTDAVSLPIDYDMPPLLEACRTVGITAEVCDWEDGTVDWSRFEAVVFRSPWTWAERQAEFLAFCERVSHVTRLITPMPLVRWALDKRYLADLAAHGVPVIPTTVVAPGSDALAAVRDFLAARPEAREFVVKPTDGCYSKDVQRYQRSLAEPASRHVARLLANGSHVILQPYVESVDRHGETDLTFFDGVYSHAIHKGAMLMPDGTVHVPTLDFRQARDADEDQRAVAAAALAASVAHLGLDLPLVCGRVDLVRGADGSPMVLEMELCEPSLNLTFSEDGALRFAQALAERLKP | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the synthesis of D-cycloserine from O-ureido-D-serine (D-OUS). It reacts with D-OUS, D-homocysteine and beta-aminoo... |
Q5T197 | MDIKHHQNGTRGQRRKQPHTTVQRLLTWGLPVSCSWFLWRQPGEFPVTALLLGAGAGGLLAIGLFQLLVNPMNIYEEQKIMFLYSLVGLGAMGWGTSPHIRCASLLLVPKMLGKEGRLFVLGYALAAIYVGPVANLRHNLNNVIASLGCTVELQINNTRAAWRISTAPLRAMFKDLLSSKELLRAETRNISATFEDLDAQVNSETGYTPEDTMDSGETAQGREARQAPASRLHLSTQKMYELKTKLRCSYVVNQAILSCRRWFDRKHEQCMKHIWVPLLTHLLCLPMKFKFFCGIAKVMEVWCRNRIPVEGNFGQTYDSL... | Function: E3 ubiquitin-protein ligase which mediates 'Lys-48'-linked ubiquitination of STAT2 and induces its proteasomal degradation thereby negatively regulating type-I-interferon signaling. Essential sperm cell-surface protein required for sperm-egg fusion and fertilization (By similarity).
Catalytic Activity: S-ubiq... |
A0A140LIJ0 | MEEGSSTARAVVRSTCGFTVGLSLATAFGLLELLGEGHSPFGCLVTTVTLAAFLSLGMGFSRQVRVSVLLLLPQAFSKQSRLLLLVASFGLVLQGPCANTLQNFTRASEAVACGAELALNQTAEMLERAKQPLISALSKIKAIAQKAKVVGDRIRKFFRSIIDAVKHIARCLQNVWYWLLHIGDMCNSELGNPYSKCTQVFDDAKIHCMKVVSGFPHLCYALLPYKLLVCGLASLVQKFCVLPSYLEFFLRTVIRTPVMKLLGKLRREFEFNMTATHYFSVDLNSSRSLSQVALDLQEAVSMKLYTAREALSLMGYTMPL... | Function: Essential sperm cell-surface protein required for sperm-egg fusion and fertilization.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78574
Sequence Length: 701
Subcellular Location: Cytoplasmic vesicle
|
Q9H295 | MGIWTSGTDIFLSLWEIYVSPRSPGWMDFIQHLGVCCLVALISVGLLSVAACWFLPSIIAAAASWIITCVLLCCSKHARCFILLVFLSCGLREGRNALIAAGTGIVILGHVENIFHNFKGLLDGMTCNLRAKSFSIHFPLLKKYIEAIQWIYGLATPLSVFDDLVSWNQTLAVSLFSPSHVLEAQLNDSKGEVLSVLYQMATTTEVLSSLGQKLLAFAGLSLVLLGTGLFMKRFLGPCGWKYENIYITRQFVQFDERERHQQRPCVLPLNKEERRKYVIIPTFWPTPKERKNLGLFFLPILIHLCIWVLFAAVDYLLYRL... | Function: Probable cell surface receptor that plays several roles in cellular fusion, cell differentiation, bone and immune homeostasis. Plays a role in TNFSF11-mediated osteoclastogenesis. Cooperates with OCSTAMP in modulating cell-cell fusion in both osteoclasts and foreign body giant cells (FBGCs). Participates in o... |
Q7TNJ0 | MRLWTLGTSIFLRLWGTYVFPRSPSWLDFIQHLGVCCFVAFLSVSLFSAAFYWILPPVALLSSVWMITCVFLCCSKRARCFILLAVLSCGLREGRNALIAAGTGVVIFGHVENIFYNFRGLLDSMTCNLRAKSFSVHFPLLKRYTEAIQWIYGLATPLNLFDDLVSWNQTLVVSLFSPSHALEAHMNDTRGEVLGVLHHMVVTTELLTSVGQKLLALAGLLLILVSTGLFLKRFLGPCGWKYENVYITKQFVRFDEKERHQQRPCVLPLNKKERKKYVIVPSLQLTPKEKKTLGLFFLPVLTYLYMWVLFAAVDYLLYRL... | Function: Probable cell surface receptor that plays several roles in cellular fusion, cell differentiation, bone and immune homeostasis. Plays a role in TNFSF11-mediated osteoclastogenesis. Cooperates with OCSTAMP in modulating cell-cell fusion in both osteoclasts and foreign body giant cells (FBGCs). Participates in o... |
Q8QG92 | MKPIPAAPEPLGQHQDSPRRKDKGEAESERQRTRERLEATLAGLAELGHLRHRQEVLIKSVLSPGTRTHGDAAARTGDNPRSLEEKFLEDNILLLKKQLNCLRKRDAGLLSQLHELDKQINDLRIDVEKTEEHLETDSRPSSGFYELSDGTSGSLSNSSNSVFSECLSSCHSSTCFCNPLETSLNLTDGQAKSADDFLEWLDYRESQHETGTVRRSFSAPHSNSVDIEADVHPKYQCDLVSKNGNDIYRYPSPLHAVAVQSPMFLLSVMGNIKAEEPEEGIDHNDNDDCIVPELDHLKDEDSFLHQSSLCSLPLSSAKKM... | Function: Involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. Binds to dvl2 to regulate the degradation of beta-catenin (ctnnb1-A and possib... |
Q09304 | MKSERVNYPVKLLNFILSIMNSYLFVLIVSIGFAESSSPKSSTSCSLMTSCAVEKCLDRGMVGRIITESSRDEVFGNLVEKFDMVCIAAKCGNECSQCKHCHYALEQMSALAQGEKTSGLCPKLETCVFNCLTEDVSKVLSCVATRCNVHCYDGDCPSCKMISRRIFSNICKQHSMTTQPQIKYEGTCPNLFMELADDYVAMKKKKL | Function: Acts downstream of daf-16/foxo to suppress tumors induced by disruption of gld-1. Potentially a direct target of daf-15/foxo.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23035
Sequence Length: 207
Subcellular Location: Membrane
|
Q9HU20 | MPRILAATAGSFVLKAYFHRWRSLVILALLLAPLLWPLQYFAERYYSEQLAEQNRQTLDLYVANLLGTLRRYEELPQILGGLPVLRQALQQPGDPLLQKIANEALADIRRRTGADVIYLLQPDGTTQVASNWAQADSFVHRNFAFRPYYREAMQGRLARFFGLGTTSIKRGYYFASAVKEGSRIIGVLVVKVDLEHIERLWGNSPEQLLVIDNYGVVILSSREDWRFHASRPLSAAERDEIHANIPYPVQDPKPLRLQQSAWLSQSRTLPETGWTVSIYAPRTLIERPVRSVLLIGGATLLALLLLLTLLTLSRRHYLDR... | Function: Member of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA . DctB functions as a membrane-associated protein kinase that phosphorylates DctD in response to environmental signals (By similarity).
PTM: Autophosph... |
P13633 | MHHVRMVKLPAEASDPHALRSRARRSWLVFAAVALVLLAAGLLLARDYGRSQALAGLAGQSRIDASLKASLLRAVVERQRALPLVLADDAAIRGALLSPDRPSLDRINRKLEALATSAEAAVIYLIDRSGVAVAASNWQEPTSFVGNDYAFRDYFRLAVRDGMAEHFAMGTVSNRPGLYISRRVDGPGGPLGVIVAKLEFDGVEADWQASGKPAYVTDRRGIVLITSLPSWRFMTTKPIAEDRLAPIRESLQFGDAPLLPLPFRKIEARPDGSSTLDALLPGDSTAAFLRVETMVPSTNWRLEQLSPLKAPLAAGAREAQ... | Function: Member of the two-component regulatory system DctB/DctD involved in the transport of C4-dicarboxylates. DctB functions as a membrane-associated protein kinase that phosphorylates DctD in response to environmental signals.
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activi... |
P16006 | MKASTVLQIAYLVSQESKCCSWKVGAVIEKNGRIISTGYNGSPAGGVNCCDYAAEQGWLLNKPKHAIIQGHKPECVSFGSTDRFVLAKEHRSAHSEWSSKNEIHAELNAILFAARNGSSIEGATMYVTLSPCPDCAKAIAQSGIKKLVYCETYDKNKPGWDDILRNAGIEVFNVPKKNLNKLNWENINEFCGE | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Supplies the nucleotide substrate for thymidylate synthetase.
Catalytic Activity: dCMP + H(+) + H2O = dUMP + NH4(+)
Sequence Mass (Da): 21198
Sequence Length: 193
EC: 3.5.4.12
|
P30648 | MVPPITSDEFCETSGCFGDSANLHTTLERLKININSDAKKLVDTNGDLKKHQRFLRIAKVTSLRSKDPNTQVGCVIVDKDNCIVSVGYNGFPIGVDDDVFRWDKEDPEDNKHLYVVHAEMNAIINKRCTTLHDCTVYVTLFPCNKCAQMLIQSRVKKVYFLENRDELAFRASKKMLDHARLPYEQIVMPQEAYVIEL | Function: Supplies the nucleotide substrate for thymidylate synthetase.
Catalytic Activity: dCMP + H(+) + H2O = dUMP + NH4(+)
Sequence Mass (Da): 22528
Sequence Length: 197
EC: 3.5.4.12
|
Q9VWA2 | MAEVSAQDLISQLSKSPESHKRKEYLHWDDYFMATSLLSAKRSKDPVTQVGACIVDSQNRIVAIGYNGFPRNCSDDVFPWSKAKKGSQEFDPLEDKKMYVVHAEANAILNSNGMSLSGTRLYTTLFPCNECAKLIIQVGISQVLYLSDKYADKPTYRASKRMLDAVGVEYKRHIPQKKTITIDFDTFPEEDPNASLGLNELHL | Function: Supplies the nucleotide substrate for thymidylate synthetase.
Catalytic Activity: dCMP + H(+) + H2O = dUMP + NH4(+)
Sequence Mass (Da): 22857
Sequence Length: 203
EC: 3.5.4.12
|
P32321 | MSEVSCKKRDDYLEWPEYFMAVAFLSAQRSKDPNSQVGACIVNSENKIVGIGYNGMPNGCSDDVLPWRRTAENKLDTKYPYVCHAELNAIMNKNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDSDEATAARLLFNMAGVTFRKFIPKCSKIVIDFDSINSRPSQKLQ | Function: Supplies the nucleotide substrate for thymidylate synthetase.
Catalytic Activity: dCMP + H(+) + H2O = dUMP + NH4(+)
Sequence Mass (Da): 20016
Sequence Length: 178
EC: 3.5.4.12
|
Q8K2D6 | MSDISCKKRDDYLEWPEYFMAVAFLSAQRSKDPSSQVGACIVNTENKIVGIGYNGMPNGCSDDLLPWRRTAENKLDTKYPYVCHAELNAIMNKNSADVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDSEETTAARLLFKLAGVTFRKFTPKYSKIVIDFDSINSRPSQKPQ | Function: Supplies the nucleotide substrate for thymidylate synthetase.
Catalytic Activity: dCMP + H(+) + H2O = dUMP + NH4(+)
Sequence Mass (Da): 20059
Sequence Length: 178
EC: 3.5.4.12
|
P10046 | MDTLMPVALIDDDKDLRRATAQTLELAGFSVSAYDGAKAALADLPADFAGPVVTDIRMPEIDGLQLFATLQGMDVDLPVILMTGHGDIPMAVQAIQDGAYDFIAKPFAADRLVQSVRRASEKRRLVLENRMLRKAAEDAQENLPLIGQTPVMENLRNILRHIADTDVDVLVAGETGSGKEVVAQILHQWSHRRKGNFVALNCGALPETVIESELFGHERGAFTGAQKRRTGRIEHASGGTLFLDEIESMPAATQVKMLRVLEMREITPLGTNEVRPVNLRVVAAAKIDLGDPAVRGDFREDLYYRLNVVTISIPPLRERR... | Function: Member of the two-component regulatory system DctB/DctD involved in the transport of C4-dicarboxylates. When activated by DctB acts in conjunction with sigma-54 to activate the transcription of dctA.
PTM: Phosphorylated by DctB.
Sequence Mass (Da): 49485
Sequence Length: 448
Subcellular Location: Cytoplasm
|
P13632 | MSAAPSVFLIDDDRDLRKAMQQTLELAGFTVSSFASATEALAGLSADFAGIVISDIRMPGMDGLALFRKILALDPDLPMILVTGHGDIPMAVQAIQDGAYDFIAKPFAADRLVQSARRAEEKRRLVMENRSLRRAAEAASEGLPLIGQTPVMERLRQTLKHIADTDVDVLVAGETGSGKEVVATLLHQWSRRRTGNFVALNCGALPETVIESELFGHEPGAFTGAVKKRIGRIEHASGGTLFLDEIEAMPPATQVKMLRVLEAREITPLGTNLTRPVDIRVVAAAKVDLGDPAARGDFREDLYYRLNVVTLSIPPLRERR... | Function: Member of the two-component regulatory system DctB/DctD involved in the transport of C4-dicarboxylates. When activated by DctB acts in conjunction with sigma-54 to activate the transcription of dctA.
PTM: Phosphorylated by DctB.
Sequence Mass (Da): 50061
Sequence Length: 460
Subcellular Location: Cytoplasm
|
O43012 | MPTVGLTGPLCSGKDAVVEYLETKHGFNAIFRLPQLNEDGEYIYRTGDLVLGSVDDLISYLTPRWRERFVINGIHSPRLLSALLKRPFFLLVYIDAPIMLRFNRYKTYSSLANTTLEEFCSIQDAAAFQSDNAGTRHRALANLLINNDSNIKLHLWEKLQKADLLNPNRFRPSWDSYFMEMASLAAKRSNCMKRRVGCVLVRGNRVIATGYNGTPRGATNCNEGGCPRCNSASSCGKELDTCLCLHAEENALLEAGRERVGNNAILYCDTCPCLTCSVKITQLGIKEVVYHTSYNMDSHTASLLQAAGVQLRQYIPPENS... | Function: Supplies the nucleotide substrate for thymidylate synthetase.
Catalytic Activity: dCMP + H(+) + H2O = dUMP + NH4(+)
Sequence Mass (Da): 35974
Sequence Length: 322
Subcellular Location: Cytoplasm
EC: 3.5.4.12
|
P06773 | MLIGVSGTKFCGCEDVINMLVDHFHFELLNHLDNPEEILDYATKNYTKNSVIFLEKLSLLEKLEKRPFFVHLSIDAPVTTRVALYRKTTQAESLSLEQIIQAIDQHDFQPEGIKLREKSHLRFKIVNEDRRGRRQSLINNITTQLKILDDKEKQMAPLMRPSWDSYFMKLATLAASRSNCMKRRVGCVIVRECRVIATGYNGTPRHLTNCFNGGCPRCNDGDSRNLHTCLCLHAEENALLEAGRDRVGQNATLYCDTCPCLTCSVKIVQTGISEVVYSQSYRMDEESFKVLKNAGITVRQFSFTEEPRIVMI | Function: Catalyzes the hydrolytic deamination of dCMP to yield dUMP, the nucleotide substrate for thymidylate synthetase.
Catalytic Activity: dCMP + H(+) + H2O = dUMP + NH4(+)
Sequence Mass (Da): 35646
Sequence Length: 312
EC: 3.5.4.12
|
Q312S1 | MSDPNVTATIMNAQGECSSGSLESRPGILGWLDANFEKPFLVAGMLAIIFIITFQTLYRYIGVYLHEGAAAAVWTEEMARFIFIWISYLAVPVAIKNRSSIRVDIIFDRLPVRFQNISWIIVDVCFLTLAATVLWQSLDLIKMQLTYPQTSPALQLPYYIPYLVLPVSFGLMAVRLLQDLAGQVRICGAADTVIGLILCAVLAAPLFIADYIDPLPVLFGYFALFLVVGVPIAIGLGLAALATIVAAGSLPIDYVAQIAFTSIDSFPIMAIPFFIAAGVFMGAGGLSRRLLNLADEMLGALPGGMALATIGTCMFFAAIS... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system DctPQM involved in the uptake of isethionate (2-hydroxyethanesulfonate), which is then catabolized by enzymes encoded by adjacent genes in the locus. Thereby is involved in an anaerobic respiration pathway that converts the sulfonate i... |
Q3AEU3 | MNDTFLKACRRENTPYTPVWLMRQAGRYMAEYMEIRNKYSFLEMCKTPELAVEVTLQPVRKLGVDAAILFADILLPLEGMGIGFRFARDEGPVIENPVRTIVDVKKVRVITPEEDVPYVLEAIKILRRELAGKVPLIGFSGAPFTLASYIIEGGGSKNYIQCKRLMWEAPEAWHELLGKIAESTVRYLKAQIAAGAQAVQVFDSWVGTLSPEDYEKYVLPHSKYVFDNLKETGVPVIHFANNAGSMLELVAAAGGDVIGLDWRVSLDRAWQTVGFDRGVQGNLDPVALFAPKEVIRQKVKEILIKAGKRPGHIFNLGHGI... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 39153
Sequence Length: 350
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
P0CAX3 | MTSSSPILKQTPKFLSALEGQSHANPPVWFMRQAGRYLPEYRAVRATAPDFISFCFDPEKAAEVTLQPMRRFPFDASIVFADILLIPGALGQKVWFEAGEGPKLGDMPSVESMAEKAGEAGKALSLVGETLTRVRSALDPDKALIGFAGAPWTVATYMIEKGSSDRSGARTFAYQNPETLDALIQVLVDATIDYLAMQVDAGAQALKLFESWAEGLSEPLFDRLVTQPHIRIIEGLRARGVTVPIIGFPRGAGTLVEDYAARTPVQGVALDTSASAKLGQTIQKTKTIQGALDPLLLRAGGDALLKRVDEMLEQWNQGPY... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen III to yield coproporphyrinogen III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 37944
Sequence Length: 351
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
P32920 | MTKTMLRALKGETLPTPPIWLMRQAGRYLPEYRATRAQAGDFLSLCYTPDLAAEVTLQPIRRYGFDAAILFADILLLPQALGADLWFETGEGPRMSTITDMAGVTALKGRDDIHETLAPVYETCRILARELPKETTFIGFAGMPWTVATYMIAGRGSKDQAAAHKLKDTDRPAFEALMDRVTEATIEYLAKQVEAGCEVVKLFDSWAGSLKGQDFEDFAVAPAKRIVSELKARFQGLPVIAFPREAGEGYIGFAEKTGADCVAIDNSVSPEWAAEKVQAGRTCVQGNLDPKYMVTGGEELVQATKRVVEAFRNGPHIFNL... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 37575
Sequence Length: 343
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
Q1D1F0 | MNDRLLRAARRQPTDTTPVWLMRQAGRYLPEYRAIRGNIAFLDLCKHPDLAAEVTVQPVTRLGVDAAIIFSDILIPVEAMGITLELGDKGPHFPDPVRSAADIDKLGVPDPVEGTGFVAEAIRRTRKALNDSVPVIGFAGAPFTLAAYMVEGGGSKSYILIKRLMFEQPELAHRLFGKLTDTLIPYLKMQVEAGASIVQIFDSWGGALSPWDYERFCIPYLKRMVSELKATGVPVIVFGVGMSSHLSLLKSTGADVVGLDWTLPMDEGRKVLGPDVAVQGNLDPLHLFLPREELDGRVKDILRRAGPEGHIFNLGHGILP... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 37949
Sequence Length: 348
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.