ID   VANB_ACIAD              Reviewed;         318 AA.
AC   O24840;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Vanillate O-demethylase oxidoreductase;
DE            EC=1.14.13.-;
DE   AltName: Full=Vanillate degradation ferredoxin-like protein;
GN   Name=vanB; OrderedLocusNames=ACIAD0979;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10348863; DOI=10.1128/jb.181.11.3494-3504.1999;
RA   Segura A., Bunz P.V., D'Argenio D.A., Ornston L.N.;
RT   "Genetic analysis of a chromosomal region containing vanA and vanB, genes
RT   required for conversion of either ferulate or vanillate to protocatechuate
RT   in Acinetobacter.";
RL   J. Bacteriol. 181:3494-3504(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; AF009672; AAC27106.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG67871.1; -; Genomic_DNA.
DR   AlphaFoldDB; O24840; -.
DR   SMR; O24840; -.
DR   STRING; 62977.ACIAD0979; -.
DR   EnsemblBacteria; CAG67871; CAG67871; ACIAD0979.
DR   KEGG; aci:ACIAD0979; -.
DR   eggNOG; COG1018; Bacteria.
DR   HOGENOM; CLU_003827_17_0_6; -.
DR   OMA; CGTCETD; -.
DR   UniPathway; UPA00217; -.
DR   Proteomes; UP000000430; Chromosome.
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; Reference proteome; Transport.
FT   CHAIN           1..318
FT                   /note="Vanillate O-demethylase oxidoreductase"
FT                   /id="PRO_0000189401"
FT   DOMAIN          1..103
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   DOMAIN          232..318
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         1..97
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   BINDING         107..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   318 AA;  35816 MW;  3D9A5BDF4C95B206 CRC64;
     MINMDVIIHK IHQLTPSIRA FELISANGSD LPAFDAGSHI DVHLKNGLTR QYSLSNCCSE
     QHRYVIGVLH DENSRGGSRC IHQDYREGDH LNIGTPRNLF EIHSKTQKAV LFAGGIGITP
     ILSMAYRLKH QQIPFELHYF VRSHEMIAFY GNLTEHFPEQ IHFHIQNQSE TQCEMSKVLE
     EVAPDRHLYV CGPAGFMQFV MDSAQQAGWS DEQLHQEHFV APQIDQSQNE AFTIEVLGSD
     RKIEVSAHQT ATQALLEHGF DVPVSCEQGI CGTCITRVVS GTPDHRDVFM TDEEHALNDQ
     FTPCCSRAKS KILVIDLA