accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
A4SUS3
|
MNMG_POLAQ
|
Glucose-inhibited division protein A
|
Polynucleobacter
|
MRYSKNFDVIVVGGGHAGTEAALASARMGCDTLLITHSIENLGAMSCNPSIGGIGKGHLVKEIDAMGGAMAAATDEAGIQFRILNSSKGPAVRATRAQGDRVLYKAAIRRRLENQPNLSLFQAAVDDLLVKGDEVQGVVTQMGLEFMAKKVVLTAGTFLDGKIHVGLNNYAGGRAGDPAAVSLSARLKELKLPQGRLKTGTPPRIDGRTIDFSVMLEQPGDLDPVPVFSYLGRPEQHPKQVPCWISHTNEQTHDIIRGGLDRSPMYTGVIEGVGPRYCPSIEDKIHRFASRNSHQIFLEPEGLTTNEFYPNGISTSLPFDVQWELVRSIRGLESAVIVRPGYAIEYDFFDPRHLRHSLETKAIGGLYFAGQINGTTGYEEAAAQGMLAGINAGLAAQGKEAWLPKRSESYIGVLVDDLITRGVQEPYRMFTSRAEYRLSLREDNADMRLTAIGRDLGLVDDYRWEVFCRKQEAVSRETSRLKDIWVGPKHEIAPLVTQLLGQELSHECNLTELLRRPGITYEAITALGNRIWAPESLDDDLGLAAQISDQVEISVKYQGYIERQAVEIARQEHNETFPLPEGLDYSQVLGLSKEVQQKLNLHKPETLGQAGRISGVTPAALSLLLVHLKKGLGRTQETI
|
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
A4SUS3
|
Q9HJW8
|
P845_THEAC
|
Phosphatase Ta0845
|
Thermoplasma
|
MAMQIKGVIFDFDGTLLDSVELRITAWKKAFQNFGVNVPEDLIRPMIGYPGIDLAKKFVKNPLDVEMLQEDYFLKNIESAKFFQDVIPTLAELRKRGIKTAVVTSTRRIVMQKFSLQVDHVVTIDDVSKGKPDPEPYLKALKMMGIPAEECIVVGDIENDLIPAKKLRCISVLVKHGRDISSNYADYEIENIADILNVIDHLAEKNNR
|
Catalyzes the dephosphorylation of the artificial chromogenic substrate p-nitrophenyl phosphate (pNPP).
|
Q9HJW8
|
P0A3Y1
|
PETM_NOSS1
|
Cytochrome b6-f complex subunit VII
|
Nostoc
|
MSGELLNAALLSFGLIFVGWALGALLLKIQGAEE
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
P0A3Y1
|
Q91775
|
FABPI_XENLA
|
Intestinal-type fatty acid-binding protein
|
Xenopus
|
MAFDGTWKVDRSENYEKFMEVMGVNIVKRKLGAHDNLKVIIQQDGNNFTVKESSTFRNIEIKFTLAQPFEYSLADGTELNGAWFLQDNQLLGTFTRKDNGKVLQTTRQIIGDELVQTYEYEGTESKRIFKRG
|
FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
|
Q91775
|
Q89A34
|
ORN_BUCBP
|
Oligoribonuclease
|
Buchnera
|
MNTDIKNLIWIDLEMTGLNPNIHKIIEIATLITDKNLKILSYGPVIAIYQNNHQLSFMDPWNNKMHTKNGLITRIKNSLYTEHLAEIKTITFLKKWVPKNTSPMCGNSISTDRQFLFKYMPTLEKYFHYRQIDVSTIKELALRWKPKIYNKLKKKTLIKH
|
3'-to-5' exoribonuclease specific for small oligoribonucleotides.
|
Q89A34
|
Q4L5D0
|
COXX_STAHJ
|
Heme O synthase
|
Staphylococcus
|
MSKEQTLSQPSSRVSFKELQQIIKMGLVQGNLIPAFAGAWLAVVMSNHSFLSSIPQILLMLIGSTLIMGGACALNNYYDQDIDRIMPSKQNRPTVNDRISDKNLLILSFGMMLLGEACLFLLNVPSGVLGLIGIVGYVSYYSIWSKRHTTWNTVVGSFPGAVPPLIGWVAIDGNISLIAIALFLVVFCWQPIHFYALAIKRSDEYSLANIPMLPSVKGFKRTRISMFIWLVFLLPLPFLLSSLGTTFVVLATLLNLGWLYVGLTSFKKATDQTKWATKMFIYSLNYLVVFFVLVVVISLIKMI
|
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
|
Q4L5D0
|
A9IWF5
|
UBIC_BART1
|
Probable chorismate pyruvate-lyase
|
Bartonella
|
MSDLEDSILPPLKWLFDQNPPIPENIRDWLMESGSMTLRLKKYCTCFQVQRQRECFIMRDKLKEEAEHLPKSARYWLREVILMGDNKPWLLGRTVIPQETLLHNQSLMHLGTTPLGHYLFNNDKLTRDYIHIGQQGVLWARRSRLRLRDKPLLLTELFLPDSPLYLHHK
|
Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
|
A9IWF5
|
Q38WR3
|
RS20_LATSS
|
30S ribosomal protein S20
|
Latilactobacillus
|
MPQIKSAMKRVKTIEKANNRNASQLSTMRSAIKKFKAAQAAGNEEAADLLKAATRAIDMASTKGLIHANKAGRDKSRLNKMMAK
|
Binds directly to 16S ribosomal RNA.
|
Q38WR3
|
Q32RN4
|
RK14_ZYGCR
|
50S ribosomal protein L14, chloroplastic
|
Zygnema
|
MIQPQSYLNVADNSGARKLMCIRVLGSSNRKYAHIGDMVIAVVKETVPNMPLKKSEIVRAVIVRTRKGLKRDNGMVLRFDDNAAVVINQEGNPRGTRVFGPVARELRDLNFTKIVSLAPEVL
|
Binds to 23S rRNA.
|
Q32RN4
|
A1TJT0
|
RS14_ACIAC
|
30S ribosomal protein S14
|
Acidovorax
|
MAKVALIQRELKREKLAAKYAAKYAELKAIASDAKRSDEEREAARLGLQKLPRNANPTRQRNRCEITGRPRGTFRQFGLARAKIRELAFAGDIPGVTKASW
|
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
|
A1TJT0
|
B8CVV1
|
ATP6_SHEPW
|
F-ATPase subunit 6
|
Shewanella
|
MAATGEALTPQGYIQHHLTNLSVGEGFWTWHIDSLFFSVGLGVLFLWLFHSVGKKATTGVPGKLQCFVEMIVEFVDNSVKETFHGRNPVIAPLALTIFVWVFMMNFMDMVPVDWIPELAMAAGIPYMKVVPTTDLNITFSMAIGVFLLIIYYSIKVKGVSGFVKELTMQPFNHWAMIPVNFLLETVTLIAKPISLALRLFGNLYAGELIFILIALMYGANWALSTLGVTLQLGWLIFHILVITLQAFIFMMLTIVYLSMAHEDH
|
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
|
B8CVV1
|
Q39ZT7
|
ATPF1_SYNC1
|
F-type ATPase subunit b 1
|
Syntrophotalea
|
MSRHSRRMRILCLCATTLLMAGSALASEAGGHADGQLKDFLYRLLDFGITFGALYFLLRGPLKRALSARRQRVAEALEQARQMQASAERRFAACRQQLADADAQIAQLTADLKAESALQCQRIEEQARKMADDIRSEATRSAAREIEAARKQLHQEAVRLAMELAEQRLKQQIAPQDQARLVDEYLRKTGE
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
Q39ZT7
|
Q5RDG3
|
PREP_PONAB
|
Pitrilysin metalloproteinase 1
|
Pongo
|
MWRCGGRQGLGVLRRLSGGHAHHRAWRWNSNRACERALQYKLGDKIHGFTVNQVTSVPELFLTAVKLIHDDTGARYLHLAREDTNNLFSVQFRTTPMDSTGVPHILEHTVLCGSQKYPCRDPFFRMLNRSLSTFMNAFTASDYTLYPFSTQNPKDFQNLLSVYLDATFFPCLRELDFWQEGWRLEHENPRDPQTALVFKGVVFNEMKGAFTDNERIFSQHLQNRLLPDHTYSVVSGGDPLCILELTWEQLKQFHATHYHPSNARFFTYGNFPLEQHLKQIHEEALSKFQKIEPSTAVPAQTPWDKPREFQITCGPDSFATDPSKQTTVSVSFLLPDITDTFEAFTLSLLSSLLTSGPNSPFYKALIESGLGTDFSPDVGYNGYTREAYFSVGLQGIAEKDIETVRSLVDRTIDEVVEKGFEDDRIEALLHKIEIQMKHQSTSFGLMLTSYIASCWNHDGDPVELLKLGNQLAKFRQCLQENPKFLQEKVKQYFKNNQHKLTLSMRPDDKYHEKQAQVEATKLKQKVEALSPGDRQQIYEKGLELRTQQSKPQDASCLPALKVSDIEPTIPVTELDVVLTAGDIPVQYCAQPTNGMVYFRAFSSLNTLPEELRPYVPLFCSVLTKLGCGLLDYREQAQQIELKTGGMSASPHVLPDDSHMDTYEQGVLFSSLCLDRNLPDMMHLWSEIFNNPCFEEEEHFKVLVKMTAQELTNAIPDSGHLYASIRAGRTLTPAGDLQETFSGMDRVRLMKRIAEMTDIKPILRKLPRIKKHLLNGDNMRCSVNATPQQMSQTEKAVEDFLRSIGRSKKERRPVRPHTVEKPVPSSSGGDAHVPHGSQIIRKLVTEPTFKPWQMKTHFLMPFPVNYVGECIRTVPYMDPDHASLKILARLMTAKFLHTEIREKGGAYGGGAKLSHNGIFSLYSYRDPNTIETLQSFGKAVDWAKSGKFTQQDIDEAKLSVFSTVDAPIAPSNKGMDYFLYGLSDGMKQAHREQLFAVSHDKLLAVSNRYLGTGKSTHSLAILGPENPKIAKDPSWTIR
|
Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides. It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion. It is a highly efficient protease, at least toward amyloid-beta protein 40. Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently. It is also able to degrade amyloid-beta protein 42.
|
Q5RDG3
|
Q5R5S6
|
ZN540_PONAB
|
Zinc finger protein 540
|
Pongo
|
MAHALVTFRDVTIDFSQKEWECLDTTQRKLYRDVMLENYNNLVSLGYSGSKPDVITLLEQGKEPCVAARDVTGRQYPGLLSRHKTKKLSSEKDIHDISLSKGSKIEKSKTLHLKGSIFRNEWQSKSEFEGQQGLKERSISQKKIIFKKMSTDRKHPSFTLNQRIHNSEKSCDSNLVQHGKIDSDVKHDCKECGSTFNNVYQLTLHQKIHTGEKSCKCEKCGKVFSHSYQLTLHQRFHTGEKPYECQECGKTFILYPQLNRHQKIHTGKKPYMCKKCDKSFFSRLELTQHKRIHTGKKSYECKECGKVFQLVFYFKEHERIHTGKKPYECKECGKAFSVCGQLTRHQKIHTGVKPYECKECGKTFRLSFYLTEHRRTHAGKKPYECKECGKSFNVRGQLNRHKAIHTGIKPFACKVCEKAFSYSGDLRVHSRIHTGEKPYECKECGKAFMLRSVLTEHQRLHTGVKPYECKECGKTFRVRSQISLHKKIHTDVKPYKCVRCGKTFRFGFYLTEHQRIHTGEKPYKCKECGKAFIRRGNLKEHLKIHSGLKPYDCKECGKSFSRRGQFTEHQKIHTGVKPYKCKECGKAFSRSVDLRIHQRIHTGEKPYECKQCGKAFRLNSHLTEHQRIHTGEKPYECKVCRKAFRQYSHLYQHQKTHNVI
|
May act as a transcriptional repressor.
|
Q5R5S6
|
B8ELG8
|
RS12_METSB
|
30S ribosomal protein S12
|
Methylocella
|
MPTISQLIRKPRQEKTYREKARHLGASPQKRGVCTRVYTTTPKKPNSALRKVAKVRLTNGFEVIGYIPGEGHNLQEHSVVMIRGGRVKDLPGVRYHILRGVLDTQGVKNRKQRRSKYGAKRPK
|
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
|
B8ELG8
|
Q8R9K8
|
SEPF_CALS4
|
Cell division protein SepF
|
Caldanaerobacter
|
MSSKVIDKIMSFLGIEEEEEEIQTPQPVVSYDRRPKVVNIHTNPQIKVLISKPEKFEQVLSICNELKSKKPVIVDLQKMDKSEAQRVVDFLSGAVYALNGEITKISGYIFLVAPENFDVTGDIKEEVNALYNLN
|
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
|
Q8R9K8
|
P59763
|
PSBI_CHLRE
|
PSII 4.8 kDa protein
|
Chlamydomonas
|
MLTLKIFVYTVVTFFVCLFIFGFLSNDPARNPGKNLD
|
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly . PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
P59763
|
Q92CN9
|
ACKA2_LISIN
|
Acetokinase 2
|
Listeria
|
MHKIMAINAGSSSLKFQIFTMPGEEVLVKGLIERIGLPDAIFNMSFQNEKIKETRAINNHGEAVEILLEQLKTHQVINDLNEITGVGHRVAHGGEAFVSSCIVTDDVVKGIEDVTSLAPLHNPANIIGIKTFRELLPNAVSVAVFDTAFHQTIPEENFLYALPYELYEKHHIRKYGFHGTSHKYVAGKAAEVLKKPLEKLKIISCHLGNGASVCAIEAGKSVNTSMGFTPNAGLMMGTRSGTIDATIIPYLVDELGYSLDEVTHMMSSESGVLGVSGISSDFRDIEIAANEGNSRALLTLRMFTGQICNYIGAYASAMNGCDALLFTAGVGENSPLIRKMVTEQLSYLGVTCNVTKNNAGDMIISNDDEAVKVCIIPTNEELMIARDVEKYTKQTIS
|
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
|
Q92CN9
|
O31664
|
MTNU_BACSU
|
2-oxoglutaramate amidase
|
Bacillus
|
MKWTISCLQFDISYGKPSENIKKAEFFIEKESKHADVLVLPELWTTGYDLANLDELADEDGRSAQSWLKKTAKKHGVHIVAGSVAVRKNSDVYNTMYIADKEGQIIKEYRKAHLFQLMDEHLYLSAGSEDGYFELDGVKSSGLICYDIRFPEWIRKHTTKGANVLFISAEWPLPRLDHWKSLLIARAIENQCFVAACNCTGSNPDNEFAGHSLIIDPWGRVLAEGGREEGIVRAEIDLQESAEVRESIPVFDDIRKDLY
|
Involved in the methylthioribose (MTR) recycling pathway . Probably catalyzes the conversion of 2-oxoglutaramate to 2-oxoglutarate .
|
O31664
|
Q9DG02
|
KCC2D_XENLA
|
Calcium/calmodulin-dependent protein kinase type II delta chain
|
Xenopus
|
MASTTCTRFTDEYQLFEELGKGAFSVVRRCIKINIGQEYAAKIINTKKLSARDHQKLEREAKICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILESVNHCHLNGIVHRDLKPENLLLASKLKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDMWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPAKRINATEALRHPWICQRSTVASMMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSAKSLLKKPDGVKESTESSNTTIEDEDVKARKQEIIKVTEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHRFYFENALSKSNKPVHTIILNPHVHLIGEDAACIAYIRLTQYLDSAGMPKTMQSEETRVWHRRDGKWQNVHFHRSGSPTIPN
|
CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system.
|
Q9DG02
|
P86518
|
DEF1_ECHCG
|
Defensin Ec-AMP-D1
|
Echinochloa
|
RECQSQSHRYKGACVHDTNCASVCQTEGFSGGKCVGFRGRCFCTKAC
|
Has antifungal activity. Inhibits spore germination in F.graminearum (IC(50)=15 ug/ml), F.oxysporum (IC(50)=102 ug/ml), F.verticillioides (IC(50)=8.5 ug/ml) and D.maydis (IC(50)=12.5 ug/ml), but not in C.graminicola, B.cinerea and H.sativum at concentrations below 30 ug/ml. Inhibits hyphal development in P.infestans (IC(50)=25.5 ug/ml), but not release of zoospores. At concentrations above 100 ug/ml, induces morphological changes such as lysis of hyphae and sporangia in P.infestans.
|
P86518
|
Q1M3H2
|
CH603_RHIL3
|
Chaperonin-60 3
|
Rhizobium
|
MAAKEIKFSTEAREKMLRGVDILANAVKATLGPKGRNVVIERSFGAPRITKDGVSVAKEIELEDKFENMGAQMVREVASKTSDVAGDGTTTATVLAQAIVKEGAKAVTSGMNPMDLKRGIDLAVGAIVAELKANARKISNNSEIAQVGTISANGDAEIGRFLAEAMERVGNDGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNADKMRVEFEDPYILIHEKKLSNLQSMLPVLEAVVQSSKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTAGTVISEDLGIKLESVTLDMLGRAKKVSIEKENTTIVDGSGAKSDIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRVDDALHATRAAVEEGILPGGGVALLRAVKALDNVETANGDQRVGVDIVRRAVEAPARQIAENAGAEGSVIVGKLREKSEFSYGWNAQTGEYGDLYAQGVIDPAKVVRTALQDAASIAGLLVTTEAMIAEKPRKDAPPPMPAGHGMDF
|
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
|
Q1M3H2
|
P30335
|
PTSN_BRADU
|
Nitrogen-metabolic PTS system EIIA component
|
Bradyrhizobium
|
MPITDLVAPEAILPALKVNSKKQALQELAAKAAELTGQNERAVFEVLLQREKLGTTAVGYGVAIPHGKLPKLEKIFGLFARLDRPIDFESMDGQPVDLVFLLLAPEGAGADHLKALARIARLLRDQDIAKKLRASRDAQAIYSVLALPPATAA
|
Seems to have a role in regulating nitrogen assimilation.
|
P30335
|
Q06GS5
|
ATPA_PIPCE
|
F-ATPase subunit alpha
|
Piper
|
METLRADEISNIIRERIEQYNREVNIVNTGTVLQVGDGIARIHGLDEVMAGELVEFDEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTFQEQGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYREQHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNSSLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSSDLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSAPLAVEEQIVTIYTGANGYLDPLETGQVKKFLVQLRTYLKTNKPQFQEIISSTKIFTKDAEAILKEVIPEQIELFLLQEQT
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
Q06GS5
|
Q6D2F1
|
ARNA_PECAS
|
UDP-glucuronic acid dehydrogenase
|
Pectobacterium
|
MKAIVFAYHDIGCVGLEALALAGYEIQAVFTHSDAPGENHFYASVAKTAAGMDVPVFAPEDINHPLWVNRIRELAPDVIFSFYYRTILSDDILQLPSFGAFNLHGSLLPRYRGRAPVNWVLVNGETQTGVTLHKMVSRADAGDIVAQSVVAIDDEDTALTLHGKCRTAAATLLAQQLPLIRSREIALTPQDDSQASYFGRRTAADGLIDWQKSAHEINNLIRAVTEPYPGAFTFLGERKVIIWRARVVKNNRVNVNHPHGGDAGSIISTSPLVVSCGEDALEIVSGQSEAGLYMSGSRLAAEMGMVPQARLGNLASRVQRRRTRVLILGVNGFIGNHLTERLLRDDRYEIYGLDISSDAIARFLGDPRFHFVEGDISIHNEWIEYHIKKCDVILPLVAIATPIEYTRNPLRVFELDFEENLKIVRDCVRYNKRIVFPSTSEVYGMCDDKEFDEDTSRLIVGPINKQRWIYSVSKQLLDRVIWAYGAKNGLRFTLFRPFNWMGPRLDTLDAARIGSSRAITQLILNLVEGSPIKLVDGGAQKRCFTDIHDGIEALFRVIENRNGQCDGQIINIGNPHNEASIRELGEMLLTSFNAHPLRDRFPPFAGFIDVESSSYYGKGYQDVAHRTPSIRNAKRLLEWEPTVKMEQTVAETLDYFLRTVDVPHTADATDTQG
|
Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
|
Q6D2F1
|
Q9ZCX2
|
GYRB_RICPR
|
DNA gyrase subunit B
|
typhus group
|
MSVIEEKCNESSYSADSIKVLKGLEAVRKRPGMYIGDVGDGSGLHHMIYEVVDNSIDEALAGYCDLVQVTLNKNGSVTVSDNGRGIPVEIHEEEGISAAEVIMTQLHAGGKFDQQSYKISGGLHGVGVSVVNALSEWLELRIWRNNKEYFIRFNNGITEAPLSIVKENIDKKGTEVTFFPSVGTFTNIEFDFVTIEHRLRELAFLNSGVKILLVDNRFEEVKKVEFYYTGGIEAYVQYIDRAKHAIHPCIVVNTVHVESGISLELALHWNDSYHENILCFTNNIRQRDGGTHLSAFKSAITRVITSYLDTTGLNKKTKHDFSGEDTREGICCVLSVKVPDPKFSSQTKDKLVSSEVRPVVENAVYTKVLEWFEEHPTEAKAIIAKIMEAANAREAARKARELTRRKSALEVSNLPGKLADCHAKDPAISELFIVEGDSAGGTAKQGRDSKIQAILPLRGKILNVERARFDKMLGSDQIGTLITALGISVEREFSLEKLRYHKVIIMTDADVDGSHIRALLLTFFYRHMPELINKGYLYIAQPPLYKVKSGASELYLKNEKALQNYLIKSTINDTYLILDGQEQLVGENLEDLINKVVKFNNLLDHVSKKFNRSITEILAINDLFNKKIFEPESSARLQKALDILNNLEESPDKTNLQVLKHENKIEFFHFSRGLKETKILLKEQLELFEFVEISQFALSIFDIFSKRLKLIVKSKAFDILTPSQLLNTIIECGKKGITIQRFKGLGEMNSDQLWETTLDPTKRTLLQVRVAEVDEAEGIFSTLMGDVVEPRRLFIQANALNVMNLDV
|
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
|
Q9ZCX2
|
O22881
|
POT2_ARATH
|
Potassium transporter 2
|
Arabidopsis
|
MDLNLGKCCGSRSSKKESWRSVLLLAYQSLGVVYGDLSISPLYVFKSTFAEDIQHSETNEEIYGVMSFVFWTLTLVPLLKYVFIVLRADDNGEGGTFALYSLICRHVKVSLLPNRQVSDEALSTYKLEHPPEKNHDSCVKRYLEKHKWLHTALLLLVLLGTCMVIGDGLLTPAISVFSAVSGLELNMSKEHHQYAVIPITCFILVCLFSLQHFGTHRVGFVFAPIVLTWLLCISGIGLYNIIQWNPHIYKALSPTYMFMFLRKTRVSGWMSLGGILLCITGAEAMFADLGHFNYAAIQIAFTFLVYPALILAYMGQAAYLSRHHHSAHAIGFYVSVPKCLHWPVLAVAILASVVGSQAIISGTFSIINQSQSLGCFPRVKVIHTSDKMHGQIYIPEINWMLMILCIAVTIGFRDVKHLGNASGLAVMAVMLVTTCLTSLVIVLCWHKPPILALAFLLFFGSIELLYFSASLTKFREGAWLPILLSLIFMIIMFVWHYTTIKKYEFDLQNKVSLEWLLALGPSLGISRVPGIGLVFTDLTSGIPANFSRFVTNLPAFHRVLVFVCVKSVPVPFVPPAERYLVGRVGPVDHRSYRCIVRYGYRDVHQDVDSFETELVSKLADFIRYDWHKRTQQEDDNARSVQSNESSSESRLAVIGTVAYEIEDNLQPESVSIGFSTVESMEDVIQMAEPAPTATIRRVRFAVEENSYEDEGSTSSAEADAELRSELRDLLAAQEAGTAFILGHSHVKAKQGSSVMKRLAVNFGYNFLRRNCRGPDVALKVPPVSLLEVGMVYVV
|
Low-affinity potassium transporter. Could mediate the potassium-dependent cell expansion in growing tissues.
|
O22881
|
B8DVE0
|
ILVC_BIFA0
|
Ketol-acid reductoisomerase type I
|
Bifidobacterium
|
MAAQIWYEDDGDLSVLDGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLRPNSKSVEFAKEQGLEVKSVPEAAAEADVIMILAPDQYQKGIWENDIEPNIKPGAALAFAHGFNIHYGYIKPSEDHPVFMVAPKGPGHIVRREYVAGRGVPVVTAVEQDPRGDGWDLALAYAKALGALRAGAIKTTFKEETETDLFGEQNVLLGGVNKLVEMGFEVLTDAGYQPEIAYFEVCHELKMIVDLMNEGGLNKDRWSCSDTAQYGDYVSTVIDEHTRERMQYHLQRIQDGSFAKEFMDDQAAGAPKFKQLQEEYSNVRIEEVGPKLRAMFSWNNDAAKDADEANSFTGKIARAQVQ
|
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
|
B8DVE0
|
Q92P97
|
COBS_RHIME
|
Cobalamin-5'-phosphate synthase
|
Sinorhizobium
|
MADIRELWDDVARSVAFLSRIPVPDRYFHGYDGGLGRAVRAFPLAAILITLPAAAIAFILGALHASSLFSAFLVVAVQAMVTGALHEDGLGDTADGFGGGRDRESALEIMKDSRIGTYGAVALILSFGLRVSALAAFLPLLTPTGGGIALLATAALSRAAMVWHWSRLPPARRGGVAASAGIPEPGATSVALGSGVLLALVLFFLAGIPTVAVWLSFAAFGLAVPGFTRIASRKLGGHTGDTIGATQQLTEVAVLGALALAI
|
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
|
Q92P97
|
F1QCV2
|
HDA10_DANRE
|
Histone deacetylase 10
|
Danio
|
MASGSALIFDEEMSRYKLLWTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYNDVYFHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAKKNYNLNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDYSSVGKGKGSGFNINLPWNKVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVLEGGYNLTSLGQSVCQTVHSLLGDPTPRISGLGTACDSALESIQNVRNVQSSYWSSFKHLAQSETNPKRPRLDATNGGPKESSEPASESNPKKTAQDIVWPEPLKRMPASVRTVVVPPPGVELTLPKNCQHSGDISESTAKEVQRIRDKHFHDLTDQNILRSLGNIISVLDRMMRSDEVCNGCVVVSDLSVSVQCALQHALTEPAERVLVVYVGDGELPVKTNDGKVFLVQICTKETEDKCVNRLSLCLREGESLTAGFMQALLGLILPVAYEFNPALVLGIVGETAAKTGLMTVWGHMTCLIQGLARGRTLTLLQGYDKDLLELTVSALSGASISPLGPLRALKPEDVEMMEKQRQRLQERWGLLRCTVSES
|
Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine . Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine . Has a very weak lysine deacetylase, if any .
|
F1QCV2
|
P48392
|
CHS3_GERHY
|
Naringenin-chalcone synthase 3
|
Gerbera
|
MATSPAVIDVETIRKAQRAEGPATILAIGTATPANCVYQADYPDYYFRVTESEHMVDLKEKFQRMCDKSMIRKRYMHITEEFLKENPSMCKFMAPSLDARQDLVVVEVPKLGKEAATKAIKEWGFPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPNEGHLDSLVGQALFGDGAAAVIIGSDPDLSVERPLFEMVSAAQTILPDSEGAIDGHLKEVGLTFHLLKDVPALIAKNIEKALIQAFSPLNINDWNSIFWIAHPGGPAILDQVEFKLGLREEKLRASRHVLSEYGNMSSACVLFILDEMRKKSIKDGKTTTGEGLEWGVLFGFGPGLTVETVVLHSLPATISVATQN
|
The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
|
P48392
|
O67556
|
KPRS_AQUAE
|
Phosphoribosyl pyrophosphate synthase
|
Aquifex
|
MNGVKIIAGTSNKTLSEEIAGYLGLRLTDALITTFSDGEIRVQINESIRGYHVYVITSLSNPVNHNLMELLLTLDAVKRSSPKEITAVVPYYAYGRQDRQDKPRTPISAKLVADLIQKAGANRVIVVDLHSPQIQGFFDIPVEHLTAIPVLYDYIRKNVVLENPIVVSPDAGGVKRARDLANKLGCGIGVILKRRPEPNKAEVMDVVGDIEGKEAIIVDDIIDTAGTLVAAANLLVNKGVKRVIACATHGIFSGPAVERLTNSPIEKVIVTNTLPVYEKKFGKLEVVSIAPLIGEAIRRIQEGTSVSSLFT
|
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
|
O67556
|
Q17058
|
MAL1_APIME
|
Maltase
|
Apis
|
MKAVIVFCLMALSIVDAAWKPLPENLKEDLIVYQVYPRSFKDSNGDGIGDIEGIKEKLDHFLEMGVDMFWLSPIYPSPMVDFGYDISNYTDVHPIFGTISDLDNLVSAAHEKGLKIILDFVPNHTSDQHEWFQLSLKNIEPYNNYYIWHPGKIVNGKRVPPTNWVGVFGGSAWSWREERQAYYLHQFAPEQPDLNYYNPVVLDDMQNVLRFWLRRGFDGFRVDALPYICEDMRFLDEPLSGETNDPNKTEYTLKIYTHDIPETYNVVRKFRDVLDEFPQPKHMLIEAYTNLSMTMKYYDYGADFPFNFAFIKNVSRDSNSSDFKKLVDNWMTYMPPSGIPNWVPGNHDQLRLVSRFGEEKARMITTMSLLLPGVAVNYYGDEIGMSDTYISWEDTQDPQGCGAGKENYQTMSRDPARTPFQWDDSVSAGFSSSSNTWLRVNENYKTVNLAAEKKDKNSFFNMFKKFASLKKSPYFKEANLNTRMLNDNVFAFSRETEDNGSLYAILNFSNEEQIVDLKAFNNVPKKLNMFYNNFNSDIKSISNNEQVKVSALGFFILISQDAKFGNF
|
Converts sucrose in nectar to glucose and fructose.
|
Q17058
|
Q9JMC2
|
INSM2_MOUSE
|
Methylated in liver tumor 1
|
Mus
|
MPRGFLVKRTKRSGSSYRARPVEPLFPPPGPLAAQSSPEEPGRGLLGSPCLAPPQDDAEWGAGGGDGPGPSPARPAGPELRRAFLERCLRSPVSAESFPSATAFCSAAPAAVTSGEELVPPQVPVSVPIPVPGPAPHGLQRRGKGAPVCASAPAAVRKPKAVRRLSFADEVTTSPVLGLKIKEEEPGAPARALGGVRTPLGEFICQLCKHQYADPFALAQHRCSRIVRVEYRCPECDKVFSCPANLASHRRWHKPRPTPACAASKPPHAPLTPPDPSLATGKENGRVPRTDDQHPQAPDSSGDGQHRDSAARPGLQALVYPEAARPQAPYPEVILGRHGPGSSGASAGATSEVFVCPYCHKKFRRQAYLRKHLGTHETGSARAPTPGFGSERTAPLTFACPLCGAHFPSADIREKHRLWHAVREELLLPALVGAPSEAGPGGASDGSAQQIFSCKYCPSTFFSSPGLTRHINKCHPSESRQVLLLQMPLRPGC
|
May function as a growth suppressor or tumor suppressor in liver cells and in certain neurons.
|
Q9JMC2
|
B2S648
|
RECA_BRUA1
|
Recombinase A
|
Brucella
|
MSQNSLRLVEDNSVDKTKALDAALSQIERAFGKGSIMRLGQNDQVVEIETVSTGSLSLDIALGVGGLPKGRIVEIYGPESSGKTTLALHTIAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEITDTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDSLPGLQARLMSQALRKLTGSISRSNCMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGSIKERDEVVGNQTRVKVVKNKLAPPFKQVEFDIMYGAGVSKVGELVDLGVKAGVVEKSGAWFSYNSQRLGQGRENAKQYLKDNPEVAREIETTLRQNAGLIAEQFLDDGGPEEDAAGAAEM
|
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
|
B2S648
|
C7CM35
|
RUTB_METED
|
Ureidoacrylate amidohydrolase RutB
|
Methylorubrum
|
MEADAPAGYRDPSGRHGAVTLPARPEPIAFDADATVLIVVDMQNAYATKGGYLDLAGFDVSATGPVIERIARAVAAARAAGIRVVWFQNGWDPDYVEAGGPGSPNWHKSNALKTMRRRPEMNQRLLAKGTWDYALVDALTPEPGDIVLPKPRYSGFYNTPLDSMLRARGIRTLVFTGIATNVCVESTLRDGYHREYFGIVLADATHQAGPPALQEGALRNIETFFGWVSDVAAFEAALSSDEARRIPA
|
Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2.
|
C7CM35
|
Q92XJ1
|
KDPC_RHIME
|
Potassium-translocating ATPase C chain
|
Sinorhizobium
|
MLNQLRPALVLTFALTLITGLGYPLLITGVAQALMPAEANGSLVRKGSVLIGSQLIGQNFASEKYFWPRPSATGPEPYNAVASSGSNLGTTSDKLKERVAADIERLRAAGIGGEIPADAGMASGSGLDPHISPEFARVQIARVAKARGLPEAGVDALVDRATQGRLFGLIGEPRVNVLELNLALDAPRT
|
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
|
Q92XJ1
|
B0Z4W1
|
RPOC2_OENBI
|
Plastid-encoded RNA polymerase subunit beta''
|
Oenothera
|
MDEGVNLVFHKKVIDGTAIKRLISRLIDHFGMAHTSHILDQVKTLGFQQATATSISLGIDDLLTIPSKGWLVQDAEQQSLSLEKHHHYGNVHAVEKLRQSIEVWYATSEYLRQEMNPNFRMTDPFNPVHIMSFSGARGNASQVHQLVGMRGLMSDPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVRTSDAGYLTRRLVEVVQHIVVRRTDCGTLRGISVSPRRMPERIFIQTLIGRVLADDIYIGSRCIAIRNQDIGIGLVNRFITFRIQPISIRTPFTCRSTSWICRLCYGRSPTHGDLVELGEAVGIIAGQSIGEPGTQLTLRTFHTGGVFTGGTAEHVRAPSNGKIKFNFNEALVHPARTRHGHPALLCSMDLDVTIESEDILHNLTIPPKSFLLVQNNQYVESEQVIAEICAGTSTFHFKERVRKHIYSDSEGEMHWSTDVYHAPEFTYSNVHLLPKTSHLWILSGGSCRSRGAPFSLHKDQDQMNPRSTERERRYLSSLSANNDQIRYKFFSSSFSGKKKDDRSPGYSEMNRIICTLHCNLIYPSILRENSDLLAKRRRNRLVIPVQSSQEREKELIPHSGISIELPINGIFRKKSILAFFDDPRYRTKSSGITQYETMGMHSIVKKEGLVDYRGINEFKPKYQMTIDRFFFIPEEVHILPESSSIMVRNNSLIGVDTRIALNTRSRAGGLVRVERKKRGIALQIFSGTIHFPGETDKISWDSGILIPPGTGKINSKESKKWKNGIYVQRITPTKKKHFVLFRPVVTYEIADGLNLARLFPPDLCQEKDNMQLQIVNYIVYGNGKPIREISDTSIQLVRTWFILNWDQDKKSASAEAAHASFVEVRAKGLIRDFLRIDLVKSPILDPRKRNDPSGSGLISDNVSDHTNINPFYSKPKMKQSPRQNHGTIRTLLNQNKECPSLMILSASNCFRMGPFNDVKSQNVIKESIKKDAIIQIRNSIGPLGTALQVVNFDSFYYFITHNQVLLTKYLQVENLKQTFQVLQYYLMDESGRIYNPDPRSNIVLNSFNLSWYFLPHNNYENSCEEISTIVSLGQFICENGCIAKNGPYLRSGQVLIVQLDSVVIRSAKPYLATPGATVHGHYGEILYDGDTVVTFLYEKSRSGDITQGLPKVEQVLEVRSVDSISVNLEKRVENWNEHITRILGFPWGFLIGAELTIVQSRISLVNKIQKVYRSQGVQIHNRHIEIIVRQITSKVLVSEDGMSNVFLPRELIGLLRAERTGRALEESICYKAFLLGITRTSLNTQSFISEASFQETARVLAKAALRGRIDWLKGLKENVVIGGMIPVGTGFKGLVHCSKQHKSIPKNKHFFEGEIRDILFHHRELFDSCISKNFHDTPEQSFRVFNDS
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
B0Z4W1
|
Q07116
|
SUOX_RAT
|
Sulfite oxidase, mitochondrial
|
Rattus
|
MLPRLYRSVAVGLPRAIRAKSTPLRLCIQACSSSDSLKPQHPSLTFSDDNSRTRGWKVMGTLIGLGAVLAYHDHRCRASQESPRIYSKEDVRSHNNLKTGVWVTLGSEVFDVTKFVDLHPGGQSKLMLAAGGPLEPFWALYAVHNQPHVRELLAEYKIGELNPEDRMSPPLEASDPYSNDPMRHPALRINSQRPFNAEPPPELLTESYITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGGQSLSLSLDDLHKFPKHEVTVTLQCAGNRRSEMNKVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHRLRETEAHVCFEGLDSDPTGTAYGASIPLARAMDPQAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHWQRRDYKGFSPSVDWDTVDFDLAPSIQELPIQSAITQPQDGTTVESGEVIIKGYAWSGGGRAVIRVDVSMDGGLTWQEAELEGEEQHPRKAWAWRIWQLKAHVPAEQKELNIICKAVDDSYNVQPDTVAPIWNLRGVLSNAWHRVHVQVVP
|
Catalyzes the oxidation of sulfite to sulfate, the terminal reaction in the oxidative degradation of sulfur-containing amino acids.
|
Q07116
|
Q6KYV2
|
PFDA_PICTO
|
GimC subunit alpha
|
Picrophilus
|
MAGNNISGEELIEQANYMKSLIDSLNSRIASLSATLSEANQTLSFLKDNESDNSKQLRIMIGSGIYADATIKKDKFIVPVGSGVFIEEERERTIKRLSENLKDLNDSINRLNQQKKELENNYNMLLMQIQELDNNVRQS
|
Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding.
|
Q6KYV2
|
P65971
|
RBFA_STRP1
|
Ribosome-binding factor A
|
Streptococcus
|
MAMANHRIDRVGMEIKREVNDILQKKVRDPRVQGVTITEVQMQGDLSLAKVYYTIMSDLASDNQKAQTGLEKATGTIKRELGKQLTMYKIPDLVFEKDNSIAYGNKIDQLLRDLDNKS
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
|
P65971
|
D7U6G6
|
ANRPN_VITVI
|
Anthocyanidin reductase ((2S)-flavan-3-ol-forming)
|
Vitis
|
MATQHPIGKKTACVVGGTGFVASLLVKLLLQKGYAVNTTVRDPDNQKKVSHLLELQELGDLKIFRADLTDELSFEAPIAGCDFVFHVATPVHFASEDPENDMIKPAVQGVVNVMKACTRAKSVKRVILTSSAAAVTINQLDGTGLVVDEKNWTDIEFLTSAKPPTWGYPASKTLAEKAAWKFAEENNIDLITVIPTLMAGSSLTSDVPSSIGLAMSLITGNEFLINGMKGMQMLSGSVSIAHVEDVCRAHIFVAEKESASGRYICCAANTSVPELAKFLSKRYPQYKVPTDFGDFPSKSKLIISSDKLVKEGFSFKYGIEEIYDESVEYFKAKGLLQN
|
Produces the terminal flavan-3-ol monomers required for the formation of proanthocyanidins or condensed tannins in leaves and flowers, as well as in the skin and seeds of developing berries. Behaves as a reductase and as a C-3 epimerase. Catalyzes the double reduction of anthocyanidins, producing a mixture of (2S,3S)- and (2S,3R)-flavan-3-ols. The enzyme catalyzes sequential hydride transfers to C-2 and C-4, respectively and epimerization at C-3 is achieved by tautomerization that occurs between the two hydride transfers. Converts cyanidin, pelargonidin and delphinidin into catechin and epicatechin, afzelechin and epiafzelechin, and gallocatechin and epigallocatechin respectively.
|
D7U6G6
|
Q90YU3
|
RL24_ICTPU
|
60S ribosomal protein L24
|
Ictalurus
|
MKVELCSFSGYKIYPGHGPVYARIDGKVFQFLNAKCESAFLTKRNPRQINWTVLYRRKHKKGQSEEVTKKRTRRAVKFQRAITGASLAEILAKRNQKPEVRKAQREQAIRAAKEAKKAKQATKKVSTQSTKAPAKAAPKQKIAKPMKVSAPRVGGKR
|
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
|
Q90YU3
|
B7GUD5
|
COAX_BIFLS
|
Pantothenic acid kinase
|
Bifidobacterium
|
MLMAVDIGNTNIVIGFLEGDRIVGSYRITTKATHTSDEYGLMITQFLALSDYTADDVDDVIVCSVVPKVMYSFRASLIKFLGLEPMVVGPGVKTGMNIRLDDPKTLGSDCIADCAGAYHTYGGPVLVADFGTATTFNYVDSSGTIRSGFITTGIRTGAEALWGQTAQLPEVEITQPQSILATNTRTAMQAGLYYTFLGGIERTIQQFRKEIDEPFQVVATGGLSRIFKNNTDMIDVYDSDLIFKGMAYIYSRNVK
|
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
|
B7GUD5
|
Q8JG69
|
AA2DB_DANRE
|
Alpha-2Db adrenoreceptor
|
Danio
|
MDLSTITFLLPNSSEDTNGTSAPRLPPHSQCASVLIVLVVTVIILVTIVGNVLVVVAVFTSRALRAPQNLFLVSLAAADILVATLVIPFSLANEVMGYWYLGSTWCAFYLALDVLFCTSSIVHLCAISLDRYWSVTKAVSYNLKRTPRRIKIMITVVWVISAVISFPPLLMTKHDELECLLNNETWYILSSCIVSFFAPGLIMILVYCRIYRVAKQRASTVFVAKNGMERQPSQSETCFVRKGKSEVESPSSHSSGSRERKGELDDIDLEESSVSNRHRNSRFAKSRKVEGAQSCPKPNGRLSWACSRASELEQEPRARQLSLSKSKLAQMREKRFTFVLAVVMGVFVLCWFPFFFTYSLHAICRKSCTIPDSLFNLFFWIGYCNSSVNPIIYTIFNRDFRKAFKKIMCRHSTRT
|
Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. The order of potency for this receptor is dexmedetomidine > norepinephrine = epinephrine > oxymetazoline.
|
Q8JG69
|
Q9P9U1
|
YIDC_XYLFA
|
Membrane protein YidC
|
Xylella
|
MNQTRVLLIFSWLTVATLLWMDWGKNKNETLEISASQNLGVDSNLELEHAVPQINAGAVPVQKDSQLIAVAPKVPVINVKTDVLQLKLDGFSVLAADLLRFPQSKDRGAKPIKLLTDDPNYPYSATTGWVSQSNSPVPNLSTFLPEQPGVSYKLANDQDRLVVPFVWTAANGVSIRRTFTFERGRYAILIRDEIRNGGETPWNAYVFRKLSRVPIPNILNRAMTNPDSFSFNGAVWYSEKGGYERRAFKDYMNDGGLNREIGGGWIALLQHHFFTAWIPQKDQASLYLLAQNGSRDIAELRGPAFTVAPGQSTTTEARLWVGPKLVEQITKEHVKGLDRVVDYSRFQLMALIGQGLFWILSHLNSLLHNWGWAIVGLVVLLRIAMYPLSAAQYKSAAKMRKFQPRLQQLKERYGEDRQKFQQAMMELYKKEKINPMGGCFPILIQMPIFFALYWVLVESVELRQAPWLGWIQDLTTRDPYFILPLLNIVIMWATQKLTPTPAGMDPIAGKMMQVMPLIFGVMMAFVPSGLALYWVINGGLNLLIQWWMIRQHADFSRKRSRGNIK
|
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
|
Q9P9U1
|
B5DFK3
|
HXD9_RAT
|
Homeobox protein Hox-D9
|
Rattus
|
MSSSGTLSNYYVDSLIGHEGDEVFAARFGPPGPGTQGRPAGVADGPAAAAEFASCSFAPKSSVFSASWSAVAAQPPAAATMSGLYHPYVSPPPLAAAEPGRYVRSWMEPLPGFPGGAGGGGGSGGGGGGGSGGPGPVPSPGGPANGRHYGIKPETGAAPAPSAASTSSSTSSSSSSKRTECSAARESQGSGGPEFPCNSFLRDKAAAAAAAAAGNGPGVGIGTGPGTGGSSEPSACSDHPSPGCPLKEEEKQPPQPPQQQLDPNNPAANWIHARSTRKKRCPYTKYQTLELEKEFLFNMYLTRDRRYEVARILNLTERQVKIWFQNRRMKMKKMSKEKCPKGD
|
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
|
B5DFK3
|
A2SR44
|
EF1B_METLZ
|
aEF-1beta
|
Methanocorpusculum
|
MGEVVVILKIMPESPDVDLEKLQADIRAKVSGIEDMKVEPIGFGLSAIKIAMITEDDEGAGDKIEGLFSQIPGIDRTEIESLNRLL
|
Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus allowing the regeneration of EF-1-alpha/GTP that could then be used to form the ternary complex EF-1-alpha/GTP/AAtRNA.
|
A2SR44
|
Q7ZVQ8
|
NS1BB_DANRE
|
Influenza virus NS1A-binding protein homolog B
|
Danio
|
MTPNGYLIFEDESFLDSTVAKMNALRKSGQFCDVRLLVCGHELMAHKAVLACCSPYLFEIFNADTEPQGGVSLVKFDDLNPDAMEVLLNYAYTAQLKADKSLVSDVYSAAKKLKLERVKQICGEYLLSKMDSQSAISYRNFASSMADGRLLGKIDGYIQDHLHEISEQDDFLKLPRLKLEVMLEDNLNLPGNGKLYSKVISWVQRSLWKNGDPLEKLMEEVQTLYYSADHKLHDGSLLEGQAEVCSTEDDHIQFVQKKPPRERDEMGSGASGSISPSNSQFNKHEWKYIASEKTTSNSYLCLAVLRGLLCVISLHGRTSPHNSPSATPCVLKSPNFEAQLEDLQEKLLKPMHYARSGLGTAELDCKLIAAGGYNREECLRTVECYDPKKDCWTFIAPMRTPRARFQMAVLMGEVYVMGGSNGHSDELSCGEMYNPRADEWIQVPELRTNRCNAGVCSLQNKLFVVGGSDPCGQKGLKNCDSFDPVTKMWTSCAPLNIKRHQAAVCELSGYMYVIGGAESWNCLNSVERYNPENNTWTLVASMNVARRGAGVAVYEGKLFVVGGFDGSHALRCVEVYDPATNEWRMLGSMTSARSNAGLAVLNNVLCAVGGFDGNEFLNSMEVYNLEKNEWSPFIEALGKN
|
Plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats.
|
Q7ZVQ8
|
P0DTB9
|
URUM_HYDBH
|
Host defense peptide
|
Hydrophylax
|
IPLRGAFINGRWDSQCHRFSNGAIACA
|
Amphibian peptide that shows viricidal activity against human H1N1 influenza A virus. It specifically targets the conserved stalk region of H1 hemagglutinin, and acts by actively destroying influenza virions. It shows a reduced activity on human H3N2 influenza A virus and no activity against other viruses (HIV, SIV, HSV-II, hepatitis C, Ebola, Zika, and Dengue viruses). In vivo, the peptide also protects mice infected with mouse-adapted influenza virus from lethal influenza infection. The peptide synthesized in D-amino acids is inactive.
|
P0DTB9
|
P50105
|
TAF4_YEAST
|
TBP-associated factor 48 kDa
|
Saccharomyces
|
MANSPKKPSDGTGVSASDTPKYQHTVPETKPAFNLSPGKASELSHSLPSPSQIKSTAHVSSTHNDAAGNTDDSVLPKNVSPTTNLRVESNGDTNNMFSSPAGLALPKKDDKKKNKGTSKADSKDGKASNSSGQNAQQQSDPNKMQDVLFSAGIDVREEEALLNSSINASKSQVQTNNVKIPNHLPFLHPEQVSNYMRKVGKEQNFNLTPTKNPEILDMMSSACENYMRDILTNAIVISRHRRKAVKINSGRRSEVSAALRAIALIQKKEEERRVKKRIALGLEKEDYENKIDSEETLHRASNVTAGLRAGSKKQYGWLTSSVNKPTSLGAKSSGKVASDITARGESGLKFREAREEPGIVMRDLLFALENRRNSVQTIISKGYAKIRD
|
Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.
|
P50105
|
Q3UZW7
|
EF2KT_MOUSE
|
eEF2-lysine methyltransferase
|
Mus
|
MAPEDHEGATSLLQSFERRFLAARALPSFPWQSLEEKLKDPSGSELLLAILQRTVKHPVCVQHGPSVKYARCFLSKLIKKHEAVPTEPLDALYEALAEVLMTQESTQCHRSYLLPSGNSVTLSESTAIVSHGTTGLVTWDAALYLAEWAIENPAAFTDRTILELGSGAGLTGLAICKACCPRAYIFSDCHAQVLEQLRGNVLLNGFSLEPHTPIDAGSSKVTVAQLDWDEVTASQLSAFQADVVIAADVLYCWEMTLSLVRVLKMLEDCQRKSAPDVYVAYTIRSQDTGKLFIEELDRAGIYWEEVPPHTGKLFPYEEHSAIVILKLVLTSRHGV
|
Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on 'Lys-525'.
|
Q3UZW7
|
A7N178
|
HTPG_VIBC1
|
High temperature protein G
|
Vibrio
|
MSETVSHNKETRGFQSEVKQLLHLMIHSLYSNKEIFLRELISNASDASDKLRFQALSNPDLYEGNADLGVKLAFDESANTLTISDNGIGMSRDDVIEHLGTIAKSGTAEFFSKLSDDQSKDSQLIGQFGVGFYSAFIVADAVTVCTRAAGLAADEAVQWQSAGEGDYTVETITKDSRGTDIVLHMREEGKEFLNEWRLRDVISKYSDHIGIPVSIQTSVRDDEGKETGEKKWEQINKAQALWTRNKSEISEEEYQEFYKHVSHDFADPLTWSHNRVEGKNDYTSLLYIPAKAPWDMMNRDHKSGLKLYVQRVFIMDDAEQFMPSYMRFVRGLIDSNDLPLNVSREILQDNKVTQSLRNACTKRVLTMLDRMAKNDTEKYQSFWKEFGLVMKEGVAEDMANKEKVAGLLRFASTEVDSAEQTVGLASYVERMKEGQDKIYFLTADSYAAAKNSPHLEQFRAKGIEVILMFDRIDEWLMNYLTEFDGKQFQSITKAGLDLSKFEDEAEKEKQKETEEEFKSVVERTQSYLGDRVKEVRTTFKLATTPAVVVTDDFEMGTQMAKLLEAAGQAVPEVKYIFEINPEHALVKRMADEADEEVFGRWVEVLLGQAMLAERGSMEDPSQFVGAINKLLTKV
|
Molecular chaperone. Has ATPase activity.
|
A7N178
|
P48885
|
CYB_ALECH
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Alectoris
|
MAPNIRKSHPLLKMVNNSLIDLPTPSNISAWWNFGSLLAVCLVTQILTGLLLAMHYTADTTLAFSSVAHTCRNVQYGWLIRNLHANGASFFFICIFLHIGRGLYYGSYLYKETWNTGVILLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGQTLVEWAWGGFSVDNPTLTRFFALHFLLPFVIAGITIIHLTFLHESGSNNPLGISSNSDKIPFHPYYSIKDILGLTLMFIPFLTLALFSPNFLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLILLLIPFLHKSKQRTMTFRPLSQTLFWLLVANLLILTWIGSQPVEHPFIIIGQMASLSYFSILLILFPMIGTLENKILNY
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
P48885
|
P59914
|
FIMA_PORGI
|
Major fimbrial subunit protein type-4
|
Porphyromonas
|
MKKTKFFLLGLAALAMTACNKDNEAEPVVETNATVSFIIKSGESRAVGDDLTDAKITKLTAMVYAGQVQEGIKTVEEDGGVLKVEGIPCKSGANRVLVVVANHNYELTGKSLNEVEALTTSLTAENQNAKNLIMTGKSAAFTIKPGSNHYGYPGGTASDNLVSAGTPLAVTRVHAGISFAGVEVNMATQYQNYYSFKPADAKIAALVAKKDSKIFGNSLVSNTNAYLYGVQTPAGLYTPDAAGETYELEASLNTNYAVGAGFYVLESKYDASNELRPTILCIYGKLLDKDGNPLTEPALTDAINAGFCDGDGTTYYPVLVNYDGNGYIYSGAITQGQNKIVRNNHYKISLNITGPGTNTPENPQPVQANLNVTCQVTPWVVVNQAATW
|
Structural subunit of the major fimbriae . These long, filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in the invasion of periodontal tissues. Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification. The sequence-based classification correlates with pathogenicity.
|
P59914
|
A6TF98
|
ARNA_KLEP7
|
UDP-glucuronic acid dehydrogenase
|
Klebsiella
|
MKAVVFAYHDMGCTGIQALLDAGYDIAAIFTHPDNPGENHFFGSVARLAAEQGIPVWAPEDVNHPLWIERIREMKPDVLFSFYYRNLLGDEILNLAPKGAFNLHGSLLPKYRGRAPLNWVLVNGESETGVTLHRMVNRADAGDIVAQQAVAIGADDAALTLHRKLCAAATELLSRALPAILAGTTDERPQDHSQATYVGRRTPEDGRLDWELPAQTLHNLVRAVSDPWPGAFGYAGANKFIVWKSRVRHDLPAAKPGTVLSIAPLIVACQDGALEIVTGQTERGVYMQGAQLAQALGLVSGAVISSKPVVAIKRRTRVLILGVNGFIGNHLTERLLQDDNYEIYGLDIGSDAISRFLDCPRFHFVEGDISIHSEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLKIIRDCVKYNKRIIFPSTSEVYGMCTDKNFDEDSSNLVVGPINKQRWIYSVSKQLLDRVIWAYGDKNGLKFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIEGGKQKRCFTDISDGIEALFRIIENKDGRCDGQIINIGNPDNEASIKELAEMLLACFERHPLRDRFPPFAGFREVESSDYYGKGYQDVEHRKPSIRNAKRCLNWEPKVEMEETVEHTLDFFLRTVELVDDKNP
|
Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
|
A6TF98
|
A5G8U0
|
RL31_GEOUR
|
50S ribosomal protein L31
|
Geotalea
|
MKEGIHPNYTEVTVKCLCGNTFQTRSTKPEISTEICSACHPFFTGKQKLIDTAGRVERFKRRYGM
|
Binds the 23S rRNA.
|
A5G8U0
|
Q8VYB1
|
MED31_ARATH
|
Mediator complex subunit SOH1
|
Arabidopsis
|
MASPEEMGDDASEIPSPPKNTYKDPDGGRQRFLLELEFIQCLANPTYIHYLAQNRYFEDEAFIGYLKYLQYWQRPEYIKFIMYPHCLYFLELLQNPNFRTAMAHPANKELAHRQQFYYWKNYRNNRLKHILPRPLPEPVPPQPPVAPSTSLPPAPSATAALSPALSPMQYNNMLSKNDTRNMGATGIDRRKRKKGI
|
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
|
Q8VYB1
|
Q9AQ99
|
ILVC_BUCUN
|
Ketol-acid reductoisomerase type II
|
Buchnera
|
KKNSIAKKNQSWINAIENNFKVDDYESLIPNADLVINLTPDKEHHHVVQVLQKLMKKNSCLGYSHGFNIVEFGEIIRKDITVIMVAPKCPGTEVREEYKRGFGVPTLIAVHNENDIRQIGLDIAKAWSFSIGSHRAGVLESSFIAEVKSDLMGEQTILCGMLQTASLLCYEKLIANKNDPAYASKLIQNGWETITESLKHGGITLMMDRLSNASKIRAYNISEKIKKILSSLFQKHMNDIISGEFSHKMMQDWQNNNKQLLDWRNKNKNTSFEKAPVYHNKIPEQEYYDHGILMIAILKAGIELSFETMLNSGIIAESAYYESLHELPLIANTIARKKLYEMNKV
|
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
|
Q9AQ99
|
A8B006
|
PTH_STRGC
|
Peptidyl-tRNA hydrolase
|
Streptococcus
|
MTKLIVGLGNPGDKYFETKHNVGFMLVDKLCKDLNLKFTVDKIFQSEIASTFLNGEKIYFIKPTTFMNESGKAVHALLTYYGLEVEDLLVIYDDLDMEVGKIRLRAKGSAGGHNGIKSIIKHIGTQDFKRVKIGIGRPKEGMTVVHHVLGKFDRDDYITILNTLDKVDNAVNYYLQSGNFEQAMQKYNG
|
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
|
A8B006
|
P47822
|
MED21_YEAST
|
Suppressor of RNA polymerase B 7
|
Saccharomyces
|
MTDRLTQLQICLDQMTEQFCATLNYIDKNHGFERLTVNEPQMSDKHATVVPPEEFSNTIDELSTDIILKTRQINKLIDSLPGVDVSAEEQLRKIDMLQKKLVEVEDEKIEAIKKKEKLLRHVDSLIEDFVDGIANSKKST
|
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
|
P47822
|
Q28NN1
|
MRAY_JANSC
|
UDP-MurNAc-pentapeptide phosphotransferase
|
unclassified Jannaschia
|
MLYWLNELSDGGDVFNLFRYITFRAGGAFFTALIFGFIFGQPLINALRRKYKDGQPIREVGPAHETKAGTPTMGGLLILAALSLATLLWARLDNPYVWLVLGVTWCFGLIGFADDWAKVSRNSSAGVSGKVRLAIGFVVAFGAALIAAWVHPEELSNQLAMPVFKDVLLNMGWMYVPFVMIVIVGSANAVNLTDGLDGLAIMPVMIAAGTLGVIAYAVGRVDFTDYLDVHYVPGTGELLIFTAGLIGGGLGFLWYNAPPAAVFMGDTGSLALGGALGAIAVCTKHEIVLAIVGGLFVAEAVSVIVQVLYFKATGKRVFLMAPIHHHFEKKGWAEPQVVIRFWIISLILALIGLATLKLR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
Q28NN1
|
E3Q717
|
LCPS_COLGM
|
Phytoene synthase
|
Colletotrichum graminicola species complex
|
MGYDYALVHVKYTIPLAALLTVFSYPVFTRLDVVRTLFIVTIAFVATIPWDSYLIRTNVWTYPPDAVLGPTLYDIPAEELFFFIIQTYITAQLYIILNKPVLHAQYLNSPATLPQWIKSGKLVGQLALSGSVLLGTWLIAKKGEGTYLGLILVWACTFALFTWTITAHFLLALPLACTALPILLPTVYLWIVDEMALGRGTWAIESGTKLELQLFGSLEIEEATFFLVTNMLIVFGIAAFDKAVAVCDAFPEKFDKPADALAMSLLRARVFPSSKYDMQRILGIRQAAARLAKKSRSFHLASSVFPGRLRIDLTLLYSYCRLADDLVDDAATPEEAAVWISKLDRHLSLLYKDPDATSTPLASKYAAENFPPSALSALDMLPTSLLPREPLAELLKGFEMDLSFSNSAFPIADPEDLELYAARVASTVGQACLELVFCHCQHGLPDYMKAYLRNTARQMGLALQFVNISRDIAVDAKIGRVYLPTTWLKEEGLTPEDVLKSPNSEGVGKVRRRILAKALDHYGEARDSMKWIPSEARGPMIVAVESYMEIGRVLMRNGGSAAADGSGRATVPKSRRIWVAWSTLMAA
|
Bifunctional enzyme that catalyzes the reactions from geranylgeranyl diphosphate to phytoene (phytoene synthase) and lycopene to beta-carotene via the intermediate gamma-carotene (lycopene cyclase).
|
E3Q717
|
A4RBZ3
|
COQ4_MAGO7
|
Coenzyme Q biosynthesis protein 4
|
Pyricularia
|
MNSSPARAVRALVQSQSRQRPTLERACLSCATVVHARRCFSVLDRPPPNYPGHVPLTRVERAGLAVGSGLWSLLDPRRGDLIAAFAEATATPYFVPRLRDAMLASPTGRRILRDRPRITSSSLDLPRLRSLPQGTVGATYVAWLDREGVTPDTRAHVRYVDDEECAYVLQRYRESHDFYHALTALPVVREGEVALKAFEFANTLLPMTGLATFAAFTLREGERRRFVDTYLPWAVKNGLRAKEIINVYWEEEMETDVVDLRKALGIEPPPDMRDARKRERDARRRRKQLETEAQQGLDAASL
|
Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
|
A4RBZ3
|
B1L8Y1
|
SYP_THESQ
|
Prolyl-tRNA synthetase
|
unclassified Thermotoga
|
MRMKDLYAPTLKETPSDVETVSHEYLLRGGFIRKTAAGIYTYLPLGRRVLLKIENIVREEMNRIGAQEILMPILQPAELWKQSGRWDDYGPEMMKLKDRHERDFTLGPTHEEIVTDLVKNELRSYRQLPLVVYQVANKYRDEIRPRFGLLRAREFIMKDAYSFHSSWESLDETYELFKEAYSRIMERLGVKYMVIEAETGAIGGNASHEFVVPAKIGETNVLFCEKCGYQASDEKAEYKGEYTQEQEEEKPFKKVPTPGVKTIEEVSEFLGVPPSKIVKSLLYKGREGYVMVLIRGDLELNEAKLKAHLKDQSLRMATPEEILKDFGVPVGFIGPIGVDVKKVADHSVRGLKNFVVGGMEEDTHYVNANHPRDFKVDEWYDLRTMVEGDPCPVCGEPLKATKGIELGHIFKLGTKYSEAMKAYFMDENGEMKPFIMGCYGWGVSRTMAAVVEHFHDENGMIWPLSIAPYTVVVDILNMNDAEQKQVGEKIYQVLSEKGEEVVLDDREVSPGFKFKDADLIGFPIRINVGRSLKEGVVELKKRYSKELVKVNIKNGFGTLLETLEKMKREYDPKEAAR
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
|
B1L8Y1
|
A5UNI4
|
ATGT_METS3
|
Archaeal tRNA-guanine transglycosylase
|
Methanobrevibacter
|
MFEIKAKDNRGRVGVLKTNSGDVKTPNLMPVIHPRKQTIDVKKYGADIVITNAYLIYKDEDLKKKAAEIGLHKLINFDGPIMTDSGSFQLSVYGDVDITNKEVIEFQELIKTDIGTSLDIPTAPFVTREKAEADLEVTLERAKEAVDYRNSQNMEMKLNSVVQGSTFPDLRRKCADELTKLDADLYPIGAVVPLMESYHYKELVDVVMNSVAHLPDSKPRHLMGAGHPMIFALAVAMGCDLFDSAAYILYAEDDRLLSVRGTYKLENLQEMPCSCEVCCNYTPDDLRAMPKEKRRDLIAQHNLNVSFAELRLIRQAIYEGSLMELVEERCRAHPNLLEALRQLGNYSKDLEKYDPRSKKSAFFYTGSESLYRSEVLRHIQKLRAMPRKRDLVILPPSRKPYSKYVSSKLGNFYVYGSEQELDLNNTDFMVLDIPFGLIPLEIDEIYPLSQNESPRTWDVSSLEFIEDFISEFVEYYDQVLIHSNVIKKLDIGLYNIHSQSDEIRYAKDDLKKVKAIADYQFGVGAGDALFAGNIKIEKSKKTGKIRHIYDGKTLIVNMRASDSFLILSKEGAKRLHAATQYPKNRVVVNKDSEPFSLEGKSVFAKFVVECDEDIRAKDEVLIVNEEDKLLAYGKALLGACEINDFQTGQAIKTRKGMKK
|
Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.
|
A5UNI4
|
A4T2X3
|
CH602_MYCGI
|
Chaperonin-60 2
|
Mycolicibacterium
|
MAKTIAYDEEARRGLERGLNSLADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEAVTQGLLKSAKEVETKEQIAATAAISAGDVQIGELIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDAERQEAVLEDPYILLVSSKVSTVKDLLPLLEKVIQAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVVSEEVGLSLETADVALLGTARKVVVTKDETTIVEGAGDSDAIAGRVAQIRAEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVALLQSAPVLEDLGLSGDEATGANIVRVALSAPLKQIAFNGGLEPGVVAEKVSNLPAGHGLNAATGEYEDLLKAGVADPVKVTRSALQNAASIAALFLTTEAVVADKPEKAAAPAGDPTGGMGGMDF
|
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
|
A4T2X3
|
Q9VAF5
|
CAD99_DROME
|
Cadherin-99C
|
Sophophora
|
MAARNSLTPQQGLGFFGLLILLCSAVLGKSQMCEVETGQTNIILDIEESRESFIGQPTTPPELPIFGDPDTEIALNLVFPKGQPIFQLNGKKLQLLQPLDRDEENLSHIVFQVSCTTRSTGKKRTIPIIVRVSDINDNAPRFMNTPYEVTVPESTPVGTTIFRNIQALDKDAGVNGLVEYFIAEGSPNSTNVEKYSADGYGTFAISFPHQGQVTVAKTLDFEKIQTYYLTIVASDRARNTADRLSSTTTLTVNIADSNDLDPSFIYSGCVSLDGACINPEYSASVPAGSLLGVLTVLPERIQAVDLDTINSPIRYSFASGMPGNYADYFQIDESTGVLKQTKAVDTSTAKKYDIIVKAEEVSPGPQRFTTAKLEIFVKPVDANPPVISSSQAEGYVDENSPIGTRVLDAHGNPISFMTTDADLSDSDPKPDYIYELTTPSFNVTGDGILVVNEENLDRDPPAPGRFKFQVVAREPRTNAASAPLSLTVHLRDVNDNAPKLAMVAPISITAGDQSESRLVTQVTATDNDEGPNAVVTYSIYHVSNNGIQKFTINATTGEIRTQGRLLAGEQYSITVQATDIGGLSSQAIVEVSVTPGPNTKPPRFQKPIYEVQVSEGAEINSTVTVVHAEDPENDAVVYSIISGNDLRQFAVGQESGVIIVIRKLDRESLTRYQLILKAEDTGGLSSSATVNIKVTDINDKNPEFEASTLPYVFQVEEGKAQASVGVVHATDADEGINAEITYSIPTDIPFTINATSGEILTAKELDYEQLNEYKFVVTAKDGAPDARLGTASVTVMVLDLPDEVPKFSDARIDVHIPENEENFLVATVQAFDPDSMPEITYVLRKGNAELFKVSEKSGEVRTIKGLDYESQKQHQLTIGTIENDGNGPGDTILLVVDVEDRNDLPPRFITVPDPVTVNDDQGIGTIIATLPAIDGDGTSPGNVVRYEIVGRGKAPKYFQVDPDTGAVRIRDELRKEEDTEYQVDIRAYDLGEPQLSSVAPLRVDVHHLLSSGNNEIKLDNKLESGTGMSSESIGLAFSDDSYTTSVPESMEANSTLKLIQIVNSKTSGDGPPAFRCEFVSGNGGGIFNLSSADHGCNLLLIQPLDFENKSSYSLQLRLTSHRYFVNPLKDTTSVEIIVQDENDNAPEFEFNRLRGQQDTFYTVVTEEMDVDTTILQVRATDRDSGKFGTVRYTLYDDDENRVNMPTSFFMMSEDTGVLRTAKHFKNENDFPLTFLVEARDSDGQEQGSHRTRARIVVNKLADINRMALSFPNAAPSDLRNYYTELEELLDKKTGLVSGIERMSSQKYLAKNGSVIENPAATDIWFYLIDPKTEQLVSRKDSIVETTLLEPAARSELNIALPRATAENISFPLERKEHVHKVKAAVAIDNEVFPFTLIAISLVILILGTIGIIYICISWSKYKNFKQRMRQYSSTNPPRYDPVIVNQQASSASETIANMKEYETQMLAMAVPPDVDDDLQLDFSAKNHAFSLDNVSYITHKENTNGGGQSSPSHSDATTATIATLRRHKNLNNASMNNNLAINNRQNTFNRTLEMNTRNNANPLASPPNGALSGTLTLGRIKHQNSNHYQNGAYNIDPTGPNNMAHAKNNAYSTMGRRGNTFGDVGLLNGNGELMNATLGRNGQLNNRLYGGEVPITNPLFQRSNSDHNHLSSTNENVSFGKRDYGQIGFSYLNDLDRSEVETTTEL
|
Cadherin that functions in epithelial morphogenesis and the intestine epithelial immune response . Essential for female fertility . Regulates the length and organization of apical microvilli in developing follicle cells and salivary glands . Function in the follicle cell is essential for egg development as the microvilli secrete eggshell material such as the vitelline membrane . Acts at least in part by regulating the recruitment of the myosin ck to the follicle cell microvilli . Also required to regulate cell rearrangements during salivary tube elongation, possibly by modulating cellular adhesion between the apical surface and apical extracellular matrix during epithelial tube elongation . May also function in cellular adhesion during the development of other tubular epithelia such as the trachea . Possibly functions as an apical membrane determinant which acts in apical membrane expansion during salivary and tracheal epithelial tube elongation . In salivary gland development, this function is independent of the other apical membrane determinants crb and sas . Essential downstream component of a hh-signaling pathway which regulates the Duox-dependent gut epithelial immune response to bacterial uracil; required for endosome formation in the enterocyte and activating norpA-dependent Ca2+ mobilization, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection .
|
Q9VAF5
|
P83251
|
TOP2D_OXYTA
|
Oxyopinin-2d
|
Oxyopes
|
GKFSVFSKILRSIAKVFKGVGKVRKQFKTASDLDKNQ
|
Disrupts biological membranes, particularly those rich in phosphocholine. Has antimicrobial activity against Gram-negative bacterium E.coli, Gram-positive bacteria B.subtilis and S.aureus, and hemolytic activity against sheep, pig and guinea pig red blood cells. Has insecticidal activity against S.frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides.
|
P83251
|
Q99489
|
OXDD_HUMAN
|
D-aspartate oxidase
|
Homo
|
MDTARIAVVGAGVVGLSTAVCISKLVPRCSVTIISDKFTPDTTSDVAAGMLIPHTYPDTPIHTQKQWFRETFNHLFAIANSAEAGDAGVHLVSGWQIFQSTPTEEVPFWADVVLGFRKMTEAELKKFPQYVFGQAFTTLKCECPAYLPWLEKRIKGSGGWTLTRRIEDLWELHPSFDIVVNCSGLGSRQLAGDSKIFPVRGQVLQVQAPWVEHFIRDGSGLTYIYPGTSHVTLGGTRQKGDWNLSPDAENSREILSRCCALEPSLHGACNIREKVGLRPYRPGVRLQTELLARDGQRLPVVHHYGHGSGGISVHWGTALEAARLVSECVHALRTPIPKSNL
|
Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate.
|
Q99489
|
O46642
|
GLHA_EQUQB
|
Thyrotropin alpha chain
|
Equus quagga
|
MDYYRKHAAVILATLSVFLHILHSFPDGEFTTQDCPECKLKVNKYFSKLGVPIYQCMGCCFSRAYPTPARSRKTMLVPKNITSEATCCVAKAFIRVTLMGNIRLENHTQCYCSTCYHHKI
|
Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways.
|
O46642
|
A7RX69
|
TIKI1_NEMVE
|
Metalloprotease TIKI homolog
|
Nematostella
|
MAAFTLWILVLNVFLLGFQARKLASNLKFPIQKCDDSTPQKNFNSFLWLVKRTPPAYFYGTIHVPYTRVWDFIPMNSKQAFTASQHVYFELDLTDEKTMRALMKCQMLPSGTMLRQTLPRKMFKRLKSHLRYIKRMIPKWIKHRDQETSSAGPYANKLYEMLTKDWDKKRPIWVMLMVNSLTESDIKTRGIPVLDQYLALEASRNHKLIGAVENVDEQCKPLNALNASQVVFALNQSLHFQERLRRGQVQVTYTTDDLIDHYNCGDLKSVLFSTQTSLPTLTVNSSLEQRERKRAQEIDQYFRNELIFQRNKRMAQRVITLLNNHPEKDFFFAFGAGHFLGNHSIIDIMKKHGYDVEYVKPEQELPSFKAKKSLNTRRERRKGCRGRRKKSKRCQKKKKRKRPDYSRVRLLQVATRRWNPTRKPYPTKLSEAPGARDISSRKAAASCTPIWTVSLALTCAVTCLLTYSGFR
|
Metalloprotease.
|
A7RX69
|
P48231
|
TCB2_YEAST
|
Tricalbin-2
|
Saccharomyces
|
MSPNSSKTRTDQISSMPGINEATKVESKNVVKDAVPIKSEVETNGTSIVREKQDPSYVGWKQVGGWEEKDELTSEDLLVDVNKDTFLGNLLPDKFYGDWYHEVAILIIAGLCSFVLGYFKFSLASVLIVMLTTGMLYRTSSKKYRESLRDLAQKEQTVEKITSDYESVEWLNTFLDKYWPIIEPSVSQQIVDGTNTALSENVAIPKFIKAIWLDQFTLGVKPPRIDAIKTFQNTKSDVVVMDVCLSFTPHDMSDLDAKQCRNYVNSNVVLKAKIFGMDIPVSVADIFFQVFVRFRFQLMTTLPLVETINIQLLEVPEVDFISRLLGNSVFNWEILAIPGLMRLIQKMAFKYLSPVLLPPFSLQLNIPQLLSKTGLPIGVLEIKVKNAHGLRKLVGMIKKTVDPYLTFELSGKIVGKTKVFKNSANPVWNESIYILLQSFTDPLTIAVYDKRETLSDKKMGTVIFNLNKLHANHYHKNEKVHFLRNSKPVGELTFDLRFFPTIEPKKLLNGDEEPLPDMNTGITKITIRELKGLDELSDKKFVFAELYVNAELVMTTKKEKRTAHLKWNSDYYSVVTDRRKTICRFVLKDQSGKVISSSVQPLNHLIDRTEVNKEWIPLRNGKGELKVTTYWRPVDIDLGLKSVGYTTPIGMLRVFINKAENLRNPDSLGKISPYAKVSVNGVARGRTNERIETLNPIWNQSIYVSVTSPLQKVSIDCFGIDTNGDDHNLGSLNIQTQNIYHKDNDDKYTIFIDNAPRTGNLIGKKGVKGTVTYYLSFYPVVPVLSLEEAKEVDEINEKKDKLEKQKSTLDDKNISKEEKERIKKEEFRLTEKYDMYSYKMKLDLDELLQYNAGVLGVTVLGGELPQPGLYVQTFFDSCGYAAITSAKNAIRTIKTGWSGDFMIKELEWSVTTFRVTKTKDANKAENFICEVNIPTIELVRNCYYKPSVLNLIGKKSAKLLVQVSWFPVTATELPQSDLITNSGDLKITAKSAENLIGVNKNGYSDPYVEFFLNEKSTSPFFKTAVQKKTLNPTWNESKTIEVSNRVNDYLTINVKDYESTNSNRSIGKAVVPLSTIDPESDTTFNIPLVGPKGEDGGVLHLEFEFEPRYTTNVVKREAGLGNFATKGLGTGIKAGSTVFALGTNVVSTGLGTIDKVKAGVFGGKKSTTTGDKKSEEKQ
|
May play a role in membrane trafficking.
|
P48231
|
B7UI83
|
CAIC_ECO27
|
Crotonobetaine/carnitine--CoA ligase
|
Escherichia
|
MDIIGGQHLRQMWDDLADVYGHKTALICESSSGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESTWILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLTDVSLPADDGVSSFTQLKNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSTGATFVLVEKYSARAFWGQVQKYRATITECIPMMIRTLMVQPLSANDQQHRLREVMFYLNLSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGQAGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTIFKEYFLNPKATAKVLEADGWLHTGDTGYRDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFCFCEQNMAKFKVLSYLEIRKDLPRNCSGKIIRKNLK
|
Catalyzes the transfer of CoA to carnitine, generating the initial carnitinyl-CoA needed for the CaiB reaction cycle. Also has activity toward crotonobetaine and gamma-butyrobetaine.
|
B7UI83
|
Q0BXU2
|
MURG_HYPNA
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Hyphomonas
|
MADTGTEKLVIIAAGGTGGHMFPARAFADEMRARGWNTALISDSRGLRYAADFPADWKEEIEAASPNFRKPWTVPGAALKINAGIARARRLMKQHRPALVAGFGGYPAFPALAAARRLGVPIIIHEQNAVLGRVNRQFAKHAQLVASGFERLDRLPRGSAHMVIGNPVRAPIIAAGQVPFPPTDGTLNIFITGGSQGSRIIGEIVPLAIANHVAPPLRVRLKVVQQVREEQFESVSNLYRSAGIECELAAFFGDMPERLAAAHLVIARSGAGTVSELATVGRPSILIPLAIAMDDHQAANAEALTAIGAADMILETNATPKLLGELISARLSDGADLTARAAAAKSAARPDAAQKLAEMAERIAEL
|
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
|
Q0BXU2
|
A1ACN7
|
HIS6_ECOK1
|
ImGP synthase subunit HisF
|
Escherichia
|
MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGGIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAETGKYHVNQYTGDESRTRVTQWETLDWVEEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQIINIGELKAYLATQGVEIRIC
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
|
A1ACN7
|
B3A0N3
|
PA2B3_BOTMA
|
Phosphatidylcholine 2-acylhydrolase
|
Bothrops
|
DLWQWGQMILKETGKLPFSYYTAYGCYCGWGGRGGKPKADTDRCCFVHDC
|
Snake venom phospholipase A2 (PLA2) that causes irreversible neuromuscular blockade in chick biventer cervicis muscle preparations. The neuromuscular blockade is mediated by inhibitory action at the presynaptic motor nerve endings. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
B3A0N3
|
Q8XV35
|
RS13_RALSO
|
30S ribosomal protein S13
|
Ralstonia
|
MARIAGVNIPNHKHTVIGLTAIYGIGRSRARKICEATGIPTDKKVKDLTDPDQDALRKEIEKFLVEGDLRRETTMNIKRLMDLGCYRGVRHRKGLPLRGQRTRTNARTRKGPRKAGVALKK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
Q8XV35
|
Q3B7M3
|
RIPR2_BOVIN
|
Rho family-interacting cell polarization regulator 2
|
Bos
|
MLVGSQSFSPGGPNGIIRSQSFAGFSGLQERRSRCNSFIENSSAVKKPQAKLKKMHNLGHKNSSPPKEPQPKRVEEVYRALKNGLDEYLEVHQTELDKLTTQLKDMRRNSRLGVLYDLDKQIKTIERYMRRLEFHISKVDELYEAYCIQRRLQDGASKMKQAFATSPASKAARESLAEINRSYKEYTENMCAIEAELEKQLGEFSIKMKGLAGFARLCPGDQYEIFMKYGRQRWKLKGRIEVNGKQSWDGEEMVFLPLIVGFISIKVTELKGLATHLLVGSVTCETKELFAARPQVVAVDINDLGTIKLNLEITWYPFDVEDMTPSSGAGNKVAALQRRMSMYSQGTPETPTFKDHSFFSNLPDDIFENGKAAEEKMPLSLSFSDLPNGDCTLAPGPADSLPGACAANPEITITSTELPPGSQSSQNEGLKDSSSASCSSSSREGSEPRPHPEGETQGLGKPEGCPVATGARPERLFLQKGVAEALLQEALLQEPSELKPVELDTFEGNITKQLVKRLTSAEVPAATERLLSEGSISAESEGCRSFLDGSLEDAFNGLFLALEPHKEQYKEFQDLNQEVMHLDDILKCKPAVSRSRSSSLSLTVESALESFDFLNTSDFDEEEDGDEVCNVGGGADSVFSDTETEKNSYRSVHPEARGHLSEALTEDTGVGTSVAGSPLPLTTGNESLDLTIIRHLQYCTQLVQQIVLSSKTPFVASNLLEKLSRQIQVMEKLSAVSDENIGNISSVIEAIPEFHKKLSLLSFWTKCCTPIGVYHSSADRVIKQLEASFARTVNRDYPGLADPVFHTLVSQILDRAEPLLPASLSSEVITVFQYYSYFTSHGVSDLESYLNQLAKQVSVVQTLQSLRDEKLLQAVSDLAPGSFPAPQEEVLRTLALLLTGEDSGASEAVTLYLTAASRSEHFREKALLYYCEALTKTDFRLQKAACLALKSLKATESIKMLVTLCQSDTEEIRNVASETLLSLGEDGRLAYEQLDKFPRDCVKVGGRLASEVATAF
|
Acts as an inhibitor of the small GTPase RHOA and plays several roles in the regulation of myoblast and hair cell differentiation, lymphocyte T proliferation and neutrophil polarization. Plays a role in fetal mononuclear myoblast differentiation by promoting filopodia and myotube formation. Maintains naive T lymphocytes in a quiescent state and prevents chemokine-induced T lymphocyte responses, such as cell adhesion, polarization and migration. Involved also in the regulation of neutrophil polarization, chemotaxis and adhesion. Required for normal development of inner and outer hair cell stereocilia within the cochlea of the inner ear. Plays a role for maintaining the structural organization of the basal domain of stereocilia. Involved in mechanosensory hair cell function. Required for normal hearing.
|
Q3B7M3
|
Q9JW59
|
MSBA_NEIMA
|
Lipid A export ATP-binding/permease protein MsbA
|
Neisseria
|
MIEKLTFGLFKKEDARSFMRLMAYVRPYKIRIVAALIAIFGVAATESYLAAFIAPLINHGFSAPAAPPELSAAAGILSTLQNWREQFTYMVWGTENKIWTVPLFLIILVVIRGICRFTSTYLMTWVSVMTISKIRKDMFAKMLTLSSRYHQETPSGTVLMNMLNLTEQSVSNASDIFTVLTRDTMIVTGLTIVLLYLNWQLSLIVVLMFPLLSLLSRYYRDRLKHVISDSQKSIGTMNNVIAETHQGHRVVKLFNGQAQAANRFDAINRTIVRLSKKITQATAAHSPFSELIASIALAVVIFIALWQSQNGYTTIGEFMAFIVAMLQMYAPIKSLANISIPMQTMFLAADGVCAFLDTPPEQDKGTLAPQRVEGRISFRNVDVEYRSDGIKALDGFNLDIRQGERVALVGRSGSGKSTVVNLLPRFVEPSAGNICIDGIDIADIKLDCLRAQFALVSQDVFLFDDTLFENVRYSRPDAGEAEVLSALQAANLQSLIDASPLGLHQPIGSNGSNLSGGQRQRVAIARAILKDAPILLLDEATSALDNESERLVQQALERLMENRTGIIVAHRLTTIEGADRIIVMDDGKIIEQGTHEQLMSQNGYYTMLRNISNKDAAVRTA
|
Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
|
Q9JW59
|
Q81MB2
|
BIOC_BACAN
|
Biotin synthesis protein BioC
|
Bacillus cereus group
|
MINKTLLQKRFNVAAVSYDQYANVQKKMAHSLLSTLDRRYSANSSIRILELGCGTGYVTEQLSNLFPKAHITAIDFAESMIAVAKTRQNVKNVMFYCEDIERLQLEETYDVIISNATFQWLNDLKQVIRNLFHHLSIDGILLFSTFGQETFQELHTSFQRAKEEKNIQNETSIGQRFYSKNQLRHICEVETGDVHVSETCYIERFTEVREFLHSIRKVGATNSNEESYCQSPSLFRAMLRIYERDFTGNEGIMATYHALFMHITKEGKR
|
Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
|
Q81MB2
|
Q9GE34
|
PSBT_AMBTC
|
Photosystem II reaction center protein T
|
Amborella
|
MEALVYTFLLVSTLGIIFFAIFFREPPKVPNKKIK
|
Seems to play a role in the dimerization of PSII.
|
Q9GE34
|
Q9SAF0
|
ORP1D_ARATH
|
OSBP-related protein 1D
|
Arabidopsis
|
MNPLCCIAPVSIDDRTNPVVAKSSNHHLGLEAIPVSKHASKPSFSTQASWISQDQLERLSSEVVDDVNLDGKDASSSSNKGCFFFGNCVGAGAGVAGIMYKWVNYGKGWRARWFELEDGVLSYYKIHGPDKIVMNPSREKGVRVIGEESVRYIRKASCGSSNRLGASAVAASRPCKPFGEIHLKVSSIRASKSDDKRLAIFTGTKTLHLRCVSKENRAAWVEAFQVAKDLFPRVASGDILPSEDAVVSTEKLREKLLQEGVGETVVKDCEAIMLSEVSVLQNRLKVLTHKHIILLDTLRQLETEKIELEATVVDETKEHDSCCGQGRRFSDFYSVMSEVSASDSEADNESQDGADVESDEDDVPYFDTNDILSAEAMRSASYRSREAEGNGSIYDKDPFFSDRLQIPARIPQYPYVRRRDNLPEPKEKEKPVGLWSIIKENIGKDLSGVCLPVYFNEPLSSLQKCFEDLEYSYLIDRALEWGKQGNELMRILNIAAFAVSGYASTEGRQCKPFNPLLGETYEADYPDKGLRFFSEKVSHHPMIVACHCEGQGWNFWGDSNIKGKFWGRSIQLDPVGVLTLKFDDGEIYQWSKVTTSIYNIILGKLYCDHYGTMRIKGGSNYSCRLKFKEQSVIDRNPRQVHGFVQDNRTGEKVAILIGKWDEAMYYVLGDPTTKPKGYDPMTEAVLLWERDKSPTKTRYNLSPFAISLNEITPGMIDKLPPTDSRLRPDQRHLENGEYESANAEKLRLEQLQRQARRLQEKGWKPRWFEKDEEGNYRYLGGYWEAREKKDWDRITDIFKKQQQRNSLSSSSSSTFL
|
May be involved in the transport of sterols.
|
Q9SAF0
|
A0A0J9X1W9
|
HD1A_CYRDO
|
Mu-theraphotoxin-Hd1a
|
Cyriopagopus
|
ACLGFGKSCNPSNDQCCKSSSLACSTKHKWCKYEL
|
Gating-modifier toxin that reversibly and voltage-independently inhibits human Nav1.1/SCN1A and Nav1.7/SCN9A (IC(50)=111 nM) . It also shows moderate inhibition on Nav1.2/SCN2A (1 uM inhibits current by 55%), Nav1.6/SCN8A (31%), Nav1.3/SCN5A (27%) and Nav1.4/SCN4A (23%) . This toxin inhibits Nav1.7/SCN9A by interacting with the S3b-S4 paddle motif in channel domain II .
|
A0A0J9X1W9
|
O05545
|
IPYR_GLUOX
|
Pyrophosphate phospho-hydrolase
|
Gluconobacter
|
MDVSKISPGKDLPNDINVVIEIPQGSQVKYEVDKDSGALVVDRFLFTPMAYPAAYGFIPGTLAADGDPADALVLTPAAVVPGSVIRARPIGMLKMEDESGQDEKIICVPHDKVHPQFSNVHSVDDLPEITKKAITHFFERYKDLEPNKWVKVTGWADKAEAGKVIMEALAAAK
|
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
|
O05545
|
Q17607
|
MCE1_CAEEL
|
GTP--RNA guanylyltransferase
|
Caenorhabditis
|
MATRGPTPDKARMGLPDRWLHCPKTGTLINNLFFPFKTPLCKMYDNQIAERRYQFHPAEVFSHPHLHGKKIGLWIDLTNTDRYYFREEVTEHECIYHKMKMAGRGVSPTQEDTDNFIKLVQEFHKKYPDRVVGVHCTHGFNRTGFLIAAYLFQVEEYGLDAAIGEFAENRQKGIYKQDYIDDLFARYDPTEDDKILAPEKPDWEREMSIGMSTQIDNGRPSTSQQIPATNGNNNQNGNQLSGGGDNSKLFMDGLIRGVKVCEDEGKKSMLQAKIKNLCKYNKQGFPGLQPVSLSRGNINLLEQESYMVSWKADGMRYIIYINDGDVYAFDRDNEVFEIENLDFVTKNGAPLMETLVDTEVIIDKVEINGAMCDQPRMLIYDIMRFNSVNVMKEPFYKRFEIIKTEIIDMRTAAFKTGRLKHENQIMSVRRKDFYDLEATAKLFGPKFVQHVGHEIDGLIFQPKKTKYETGRCDKVLKWKPPSHNSVDFLLKVEKKCKEGMLPEWIGYLFVQNLSDPFGTMKATATLKKYHNKIIECTLLVDNQGRPKEWKFMRERTDKSLPNGLRTAENVVETMVNPVTETYLIEYVNHALRVLKRAAAAHRHHQIHQQQLHEGEPEARRQKL
|
Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus via a covalent enzyme-GMP reaction intermediate.
|
Q17607
|
B2I6Q0
|
GCSH_XYLF2
|
Glycine cleavage system H protein
|
Xylella
|
MSDIPGDLKFLKSHEWVRIEDNNRAIVGVSDHAQNLLGDLVYVELPNIGDHLDAGATAAVIESVKAASDIYSPVTGKVIEVNTTLSDKPETINEDPYGEGWIMVIEMQAPEEISNLLSPDDYTEVLESDEH
|
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
|
B2I6Q0
|
Q14Q07
|
POTA_SPICI
|
Spermidine/putrescine import ATP-binding protein PotA
|
Spiroplasma
|
METNILELRNISKQYDGKVVLKGINLNIKEGEFVTLLGPSGCGKTTTLRIIAGFEQPNSGELLFLGKDYLKTPVHKREVNTVFQNYALFPHLTVFDNIAYGLKVKRNKYDVIETEVKKFLQLVGLEGFEDKSVEQLSGGQRQRVALARALINKPRVLLLDEPMAALDVKLRKKMQAELKALQGEIGITFILVTHDQEEALTLSDRIIVMNDGAIQQVGTPAEIYNEPENLWTAQFIGDSNIISNAIFIKDNLVTIDGKKIVCVDRGFGENENQIDIIIRPEDIDIVPVGKGFFTGTVKRVNFKGVHWEIIVKCKERKYLIHSTDRVEEGDQVDISWNVEDIHVMWKEIDD
|
Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
|
Q14Q07
|
P07602
|
SAP_HUMAN
|
Protein C
|
Homo
|
MYALFLLASLLGAALAGPVLGLKECTRGSAVWCQNVKTASDCGAVKHCLQTVWNKPTVKSLPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPNMSASCKEIVDSYLPVILDIIKGEMSRPGEVCSALNLCESLQKHLAELNHQKQLESNKIPELDMTEVVAPFMANIPLLLYPQDGPRSKPQPKDNGDVCQDCIQMVTDIQTAVRTNSTFVQALVEHVKEECDRLGPGMADICKNYISQYSEIAIQMMMHMQPKEICALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVEPIKKHEVPAKSDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDTYGSSILSILLEEVSPELVCSMLHLCSGTRLPALTVHVTQPKDGGFCEVCKKLVGYLDRNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIEILVEVMDPSFVCLKIGACPSAHKPLLGTEKCIWGPSYWCQNTETAAQCNAVEHCKRHVWN
|
Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.
|
P07602
|
A0RDW1
|
IOLA1_BACAH
|
Methylmalonate-semialdehyde dehydrogenase 1
|
Bacillus cereus group
|
MITTEIKRVKNHINGEWVESTGTEVEAVPNPATGKIIAYVPLSPKEDVEKAVEAAKAAYETWSKVPVPNRSRQLYKYLQLLQENKEELAKIITLENGKTLTDATGEVQRGIEAVELATSTPNLMMGQALPNIASGIDGSIWRYPIGVVAGITPFNFPMMIPLWMFPLAIACGNTFVLKTSERTPLLAERLVELFYEAGFPKGVLNLVQGGKDVVNSILENKDIQAVSFVGSEPVARYVYETGTKHGKRVQALAGAKNHAIVMPDCNLEKTVQGVIGSAFASSGERCMACSVVAVVDEIADEFIDVLVAETKKLKVGDGFHEDNYVGPLIRESHKERVLGYINSGVADGATLLVDGRKIKEEVGEGYFVGATIFDGVNQEMKIWQDEIFAPVLSIVRVKDLEEGIKLTNQSKFANGAVIYTSNGKHAQTFRDNIDAGMIGVNVNVPAPMAFFAFAGNKASFFGDLGTNGTDGVQFYTRKKVVTERWF
|
Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively.
|
A0RDW1
|
B4SAN6
|
ATPB_PELPB
|
F-ATPase subunit beta
|
Pelodictyon
|
MQEGKISQIIGPVVDVDFPEGRLPSILDALTVTRADGTKLVLETQQHLGEERVRTVAMESTDGLVRGMNVTHTGKPIQVPVGLEVLGRMLNVVGDPIDGRGPVNTKKSYSIHRLAPRFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVLIMELINNIAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDEEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQDRIVSTKKGSVTSVQAIYVPADDLTDPAPATAFAHLDATTVLSRSIAELGIYPAVDPLDSTSRILDPNIVGDDHYDTAQAVKQLLQRYKDLQDIIAILGMDELSDEDKLVVSRARKVQRFLSQPFFVAEAFTGLAGKYVKLEETIKGFKEIIAGRHDNLPESAFYLVGTIEEAVEKAKTL
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
B4SAN6
|
A0A0H3MFZ3
|
PIPS_MYCBP
|
CDP-diacylglycerol--D-myo-inositol-3-phosphate 3-phosphatidyltransferase
|
Mycobacterium tuberculosis complex
|
MSKLPFLSRAAFARITTPIARGLLRVGLTPDVVTILGTTASVAGALTLFPMGKLFAGACVVWFFVLFDMLDGAMARERGGGTRFGAVLDATCDRISDGAVFCGLLWWIAFHMRDRPLVIATLICLVTSQVISYIKARAEASGLRGDGGFIERPERLIIVLTGAGVSDFPFVPWPPALSVGMWLLAVASVITCVQRLHTVWTSPGAIDRMAIPGKGDR
|
Catalyzes the conjugation of the 1'-hydroxyl group of D-myo-inositol-3-phosphate (also named L-myo-inositol-1-phosphate) with a lipid tail of cytidine diphosphate diacylglycerol (CDP-DAG), forming phosphatidylinositol phosphate (PIP) and CMP. PIP is a precursor of phosphatidylinositol (PI) which is an essential lipid for mycobacteria required for formation of their cell wall.
|
A0A0H3MFZ3
|
Q62HQ3
|
IF11_BURMA
|
Translation initiation factor IF-1 1
|
pseudomallei group
|
MAKEELIELDGIVDEVLPDSRYRVTLDNGVVVGAYASGQMRRHRIRILAGDRVTLELSVYDLTKGRINFRHKDERRSDAAPRASARRR
|
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
|
Q62HQ3
|
Q5SD43
|
PSBE_HUPLU
|
PSII reaction center subunit V
|
Huperzia
|
MSGNTGERPFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESRQEIPLITGRFNSLEQVDEFTRSL
|
This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
Q5SD43
|
B5XQ60
|
NUDL_KLEP3
|
Uncharacterized Nudix hydrolase NudL
|
Klebsiella
|
MADHALNLDDFLSRFQLLRPQPSRHALNQRQAAVLVPIVRRPQPGLLLTQRSPLLRKHAGQVAFPGGAVDNTDATLIAAALREAQEEVAIPPEAVEVIGVLPPVDSVTGFQVTPVVGIIPPNLHYHASQDEVSAVFEMPLAEALRLGRYHPLDIHRRGNDHRVWLSWYQHYFVWGMTAGIIRELALQIGARP
|
Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.
|
B5XQ60
|
A9W565
|
LSPA_METEP
|
Signal peptidase II
|
Methylorubrum
|
MTAFRSGLIALLATLALDQASKLWLYFGTDLVMTQPWRLAPFADFVVVWNRGVSYGLFQQEGGLGRWLLVAVSLAAVIGLSVWMRRAGSRLLAVALGLIVGGALGNAIDRAAYGAVFDFVHLHAGPWSWYVFNVADAAIVAGVVGLILDSLRPAPRAPSTDVAGNGGHPQA
|
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
|
A9W565
|
Q9Z2D1
|
MTMR2_MOUSE
|
Phosphatidylinositol-3-phosphate phosphatase
|
Mus
|
MEKSSSCESLGAQLPAARLPSEDSLSSASTSHSENSVHTKSASAISSDSISTSADNFSPDLRVLREANKLAEMEEPALLPGENIKDMAKDVTYICPFTGAVRGTLTVTSYRLYFKSMERDPPFVLDASLGVISRVEKIGGASSRGENSYGLETVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVSNGLPLFAFEYKEVFPENGWKLYDPLLEYRRQGIPNESWRITKINERYELCDTYPALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATVTRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPTIEETHWLSNLESTHWLEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPKKTVSLWSYINSQLEDFTNPLYGSYSNHVLYPVASMRHLELWVGYYIRWNPRMKPQEPIHSRYKELLAKRAELQRKVEELQREISNRSTSSSERASSPAQCVTPVQTVV
|
Phosphatase that acts on lipids with a phosphoinositol headgroup . Has phosphatase activity towards pho sphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate . Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate . Stabilizes SBF2/MTMR13 at the membranes . Specifically in peripheral nerves, stabilizes SBF2/MTMR13 protein .
|
Q9Z2D1
|
Q04BH8
|
WHIA_LACDB
|
Probable cell division protein WhiA
|
Lactobacillus
|
MASYASEVKKELTSIEVHPEHAKAELAAFLRMNAVLSRHDGQMSLDIVTENPAIARRIFSLIKTAYGFEPQLIVTRKMKLKKNHQYLVRVAQMVSEIMADLEIYSPKKGFITGVPDKIKYSEQRSMSYLRGGFLASGSVNNPETSRYHLEIYCTYANHSQDLQEIMNKYFDLNAKVTARRSGSIVYLKEAEKIGDFLHVVGAVNAMLAFEDLRIMRDMRNSVNRLVNCDTANLRKTAGAAAKQVEDIELIDQKQGLESLPEKLASLARFRLQHPELSLKELAEQVPDGPISKSGVNHRLKKLHEIAENLR
|
Involved in cell division and chromosome segregation.
|
Q04BH8
|
A5VZH8
|
PYRC_PSEP1
|
Dihydroorotase
|
Pseudomonas
|
MSDRLTLLRPDDWHIHLRDGAVLPHTVGDVARTFARAIIMPNLVPPVRTANEAGAYRERILAARPAGSRFEPLMVLYLTDNISPEDIRAAKASGFVYAAKLYPAGATTNSDSGVTSIDNIFPAIEAMAEVGMPLLVHGEVTRSEIDVFDREKRFIDEHMRRVVERFPTLKVVFEHITTSDAAQFVTEAPANVGATITAQHLLYNRNHMLVGGIRPHFYCLPILKRNTHQVALLDAATSGNPKFFLGTDSAPHARHAKEAACGCAGCYTAYAAIEMYAEAFEQRNALDKLEGFASLHGPAFYGLPANTDTITLVREEWTAPESLPFGEQTVVPLRAGEKLRWRLLEKNA
|
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
|
A5VZH8
|
D4GYE8
|
LEU3_HALVD
|
3-isopropylmalate dehydrogenase
|
Haloferax
|
MTEEIVVIPGDGIGAEVIPAAVDVLKAVGDFEFVEADAGDHVKEETGEALPQETYDLAAEADATLFGAAGETAADVILPLRTAVDSFVNVRPAKAYPGVDALRPETDLVFLRENTEGVYSGHEDRLSEDLSTLTRVVTTSASERLAEYACDYVGGEGGSFQVAHKANVMRETDGRFRDAAVAVADERGVETEEVLMDAFATRVCLDPTQFDTIVCPNLAGDVLSDLAAGLVGGLGLLPSANIGPDAALFEPVHGSAPDIAGEGIANPAATILSAAMLLDYLDHEAEADRVRSAVEGVLADGPRTPDLGGDASTEDVTAAILDRL
|
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
|
D4GYE8
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.