VANB_PSEPU
ID VANB_PSEPU Reviewed; 315 AA.
AC O54037;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WCS358;
RX PubMed=9579070; DOI=10.1099/00221287-144-4-965;
RA Venturi V., Zennaro F., Degrassi G., Okeke B., Bruschi C.;
RT "Genetics of ferulic acid bioconversion to protocatechuic acid in plant-
RT growth-promoting Pseudomonas putida WCS358.";
RL Microbiology 144:965-973(1998).
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; Y14759; CAA75051.1; -; Genomic_DNA.
DR AlphaFoldDB; O54037; -.
DR SMR; O54037; -.
DR PRIDE; O54037; -.
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..315
FT /note="Vanillate O-demethylase oxidoreductase"
FT /id="PRO_0000189404"
FT DOMAIN 1..100
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 227..315
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 1..94
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT BINDING 104..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 303
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 315 AA; 34307 MW; 7A4679B15B499C7A CRC64;
MIDAVVVSRN DEAQDICSFE LAAVDGSLLR FSAGAHIDVH LPEGQVRQYS LCNHPEERHR
YLIGVLKDPA SRGGSRSLHE QIHNGARLRI SAPRNLFPLA QGARRSLLFA GGIGITPILC
MAEQLAASAD FELHYCARSS ERAAFIERMR GAAFADRLFV HFDEQPETAL DIAQVLANPQ
ADVHLYVCGP GGFMQHVLES AKAQGWQEAC LHREYFAAAP VDTQGDGSFS VQLNSTGQVF
EVPADQSVVH VLEQHGIAIA MSCEQGICGT CLTRVLSGTP EASRPVFLTE QEQALNDQFT
PCCSRSKTPL LVLDL