ID B6B086_9RHOB Unreviewed; 313 AA.
AC B6B086;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Vanillate O-demethylase oxidoreductase {ECO:0000313|EMBL:EDZ42304.1};
GN ORFNames=RB2083_1819 {ECO:0000313|EMBL:EDZ42304.1};
OS Rhodobacteraceae bacterium HTCC2083.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ42304.1, ECO:0000313|Proteomes:UP000005746};
RN [1] {ECO:0000313|Proteomes:UP000005746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746};
RX PubMed=21036993; DOI=10.1128/JB.01268-10;
RA Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of strain HTCC2083, a novel member of the marine clade
RT Roseobacter.";
RL J. Bacteriol. 193:319-320(2011).
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DR EMBL; DS995276; EDZ42304.1; -; Genomic_DNA.
DR AlphaFoldDB; B6B086; -.
DR STRING; 314270.RB2083_1819; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_17_0_5; -.
DR OrthoDB; 9792185at2; -.
DR Proteomes; UP000005746; Unassembled WGS sequence.
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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF2; PHENOXYBENZOATE DIOXYGENASE BETA SUBUNIT; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Methyltransferase {ECO:0000313|EMBL:EDZ42304.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005746};
KW Transferase {ECO:0000313|EMBL:EDZ42304.1}.
FT DOMAIN 1..104
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 227..313
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 313 AA; 33597 MW; FC62A397D9382226 CRC64;
MAKIEGVVLD VVTLSDRISG LRVAATDCSA LPIWEAGAHV EFDVADGARA YSLIAFDPVT
VAPSFYQIAV QREDDGQGGS RAMHDLQIGD PITFSAPKNN FRVKTDAPAV LLAGGIGVTP
MISMAAALHA AGQQFAFHYA GRSASVMAYH AELAATWSDA FHLHCDDNDS TLDLDAVMVS
LNDAHLYVCG PRGLLNATRA KAEALGILQS RVHYELFEAA ATQSNDRAFE VQINDGTVYT
IPVGQSIIDV LEENDVDVMY DCQRGDCGIC QCDVLEGTPD HRDVVLSDAE REAGDVMQIC
VSRAKTPRLV LDI
//
