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VANB_PSES9
ID   VANB_PSES9              Reviewed;         314 AA.
AC   P12580;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Vanillate O-demethylase oxidoreductase;
DE            EC=1.14.13.-;
DE   AltName: Full=Vanillate degradation ferredoxin-like protein;
GN   Name=vanB;
OS   Pseudomonas sp. (strain ATCC 19151).
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3170489; DOI=10.1128/jb.170.10.4924-4930.1988;
RA   Brunel F., Davison J.;
RT   "Cloning and sequencing of Pseudomonas genes encoding vanillate
RT   demethylase.";
RL   J. Bacteriol. 170:4924-4930(1988).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- PATHWAY: Xenobiotic degradation; vanillyl-alcohol degradation.
CC   -!- SIMILARITY: Belongs to the PDR/VanB family. {ECO:0000305}.
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DR   EMBL; M22077; AAA26020.1; -; Genomic_DNA.
DR   AlphaFoldDB; P12580; -.
DR   SMR; P12580; -.
DR   PRIDE; P12580; -.
DR   KEGG; ag:AAA26020; -.
DR   UniPathway; UPA00217; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR000951; Ph_dOase_redase.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Flavoprotein;
KW   FMN; Iron; Iron-sulfur; Lignin degradation; Metal-binding; NAD;
KW   Oxidoreductase; Transport.
FT   CHAIN           1..314
FT                   /note="Vanillate O-demethylase oxidoreductase"
FT                   /id="PRO_0000189402"
FT   DOMAIN          1..101
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   DOMAIN          229..314
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         105..217
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   BINDING         263
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         268
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         271
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         302
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   314 AA;  33706 MW;  FC521516AA6CEB72 CRC64;
     MLDLMIRGLR LEAPGILGLE LVATDGSPLP TFEAGAHLDL HLPGGLVRPY SLCNAPGETH
     RYCLAVLLDP ASRGGSRAVH EQLRVGQHLT TSAPRNLFPL VAESSRSLLF AGGIGITPIL
     AMAQVLAARG DTFELHYCVR SRRLAAFIDW LEASTFAAHV HLHADDGPTP FDATALLRDA
     GDAHLYVCGP GGFMEHVLGC ARTAGWDETR LHREYFAAPV QPAGDARAFE GRLARSGLTL
     QVPAERSVAQ VLDDAGVCIP LACEQGICGT CLTRVLDGEP EHRDSFLTDA ERARNDQFTP
     CCSRARSACL VLDL
 
 
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