ID   VANB_PSEUH              Reviewed;         317 AA.
AC   O05617;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 90.
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 HR199 / DSM 7063).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=86003;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9098058; DOI=10.1128/jb.179.8.2595-2607.1997;
RA   Priefert H., Rabenhorst J., Steinbuechel A.;
RT   "Molecular characterization of genes of Pseudomonas sp. strain HR199
RT   involved in bioconversion of vanillin to protocatechuate.";
RL   J. Bacteriol. 179:2595-2607(1997).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- PATHWAY: Xenobiotic degradation; vanillyl-alcohol degradation.
CC   -!- SUBUNIT: This demethylase system consists of two proteins: an oxygenase
CC       and an oxygenase reductase.
CC   -!- SIMILARITY: Belongs to the PDR/VanB family. {ECO:0000305}.
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DR   EMBL; Y11521; CAA72288.1; -; Genomic_DNA.
DR   AlphaFoldDB; O05617; -.
DR   SMR; O05617; -.
DR   PRIDE; O05617; -.
DR   KEGG; ag:CAA72288; -.
DR   BioCyc; MetaCyc:MON-14063; -.
DR   UniPathway; UPA00217; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
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; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR000951; Ph_dOase_redase.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 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..317
FT                   /note="Vanillate O-demethylase oxidoreductase"
FT                   /id="PRO_0000189403"
FT   DOMAIN          1..101
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   DOMAIN          232..317
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         105..220
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   BINDING         266
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         274
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         304
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   317 AA;  34461 MW;  42C8D6024FA41B64 CRC64;
     MIEVIISAMR LVAQDIISLE FVRADGGLLP PVEAGAHVDV HLPGGLIRQY SLWNQPGAQS
     HYCIGVLKDP ASRGGSKAVH ENLRVGMRVQ ISEPRNLFPL EEGVERSLLF AGGIGITPIL
     CMAQELAARE QDFELHYCAR STDRAAFVEW LKVCDFADHV RFHFDNGPDQ QKLNAAALLA
     AEAEGTHLYV CGPGGFMGHV LDTAKEQGWA DNRLHREYFA AAPNVSADDG SFEVRIHSTG
     QVLQVPADQT VSQVLDAAGI IVPVSCEQGI CGTCITRVVD GEPDHRDFFL TDAEKAKNDQ
     FTPCCSRAKS ACLVLDL