ID   VANA_PSEUH              Reviewed;         354 AA.
AC   O05616;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Vanillate O-demethylase oxygenase subunit;
DE            EC=1.14.13.82;
DE   AltName: Full=4-hydroxy-3-methoxybenzoate demethylase;
GN   Name=vanA;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + vanillate = 3,4-dihydroxybenzoate +
CC         formaldehyde + H2O + NAD(+); Xref=Rhea:RHEA:13021, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16632,
CC         ChEBI:CHEBI:16842, ChEBI:CHEBI:36241, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.14.13.82;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
CC       Note=Binds 1 Fe cation. {ECO:0000305};
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 bacterial ring-hydroxylating dioxygenase
CC       alpha subunit family. {ECO:0000305}.
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DR   EMBL; Y11521; CAA72287.1; -; Genomic_DNA.
DR   AlphaFoldDB; O05616; -.
DR   SMR; O05616; -.
DR   PRIDE; O05616; -.
DR   KEGG; ag:CAA72287; -.
DR   BioCyc; MetaCyc:MON-14062; -.
DR   UniPathway; UPA00217; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0018489; F:vanillate monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR   InterPro; IPR044043; VanA_C_cat.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF19112; VanA_C; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Iron; Iron-sulfur;
KW   Lignin degradation; Metal-binding; Monooxygenase; NAD; Oxidoreductase.
FT   CHAIN           1..354
FT                   /note="Vanillate O-demethylase oxygenase subunit"
FT                   /id="PRO_0000085059"
FT   DOMAIN          7..107
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         47
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         49
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         66
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         69
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   354 AA;  39491 MW;  970AD00DD8A870C3 CRC64;
     MFPKNAWYVA CTPDEIADKP LGRQICNEKI VFYRGPEGRV AAVEDFCPHR GAPLSLGFVR
     DGKLICGYHG LEMGCEGKTL AMPGQRVQGF PCIKSYAVEE RYGFIWVWPG DRELADPALI
     HHLEWADNPE WAYGGGLYHI ACDYRLMIDN LMDLTHETYV HASSIGQKEI DEAPVSTRVE
     GDTVITSRYM DNVMAPPFWR AALRGNGLAD DVPVDRWQIC RFAPPSHVLI EVGVAHAGKG
     GYDAPAEYKA GSIVVDFITP ESDTSIWYFW GMARNFRPQG TELTETIRVG QGKIFAEDLD
     MLEQQQRNLL AYPERQLLKL NIDAGGVQSR RVIDRILAAE QEAADAALIA RSAS