ID A0A0S9NV89_9BURK Unreviewed; 318 AA.
AC A0A0S9NV89;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Vanillate O-demethylase oxidoreductase {ECO:0000313|EMBL:KQP49156.1};
GN ORFNames=ASF44_00540 {ECO:0000313|EMBL:KQP49156.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP49156.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP49156.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP49156.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP49156.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP49156.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQP49156.1}.
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DR EMBL; LMNA01000001; KQP49156.1; -; Genomic_DNA.
DR RefSeq; WP_056897244.1; NZ_LMNA01000001.1.
DR AlphaFoldDB; A0A0S9NV89; -.
DR STRING; 1736318.ASF44_00540; -.
DR OrthoDB; 370747at2; -.
DR Proteomes; UP000051759; 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:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 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:KQP49156.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759};
KW Transferase {ECO:0000313|EMBL:KQP49156.1}.
FT DOMAIN 1..103
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 233..318
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 318 AA; 34001 MW; C41490C1817CE69E CRC64;
MVELDVRVRA RRNEADGICS FELEPVAEAP LPSFSAGAHI DVHVPSGPVR QYSLCSDPHD
RGIWRIGVLR EPASRGGSSG MHDAAPVGTV LKVSAPKNLF ALTEAPYSVL VAGGIGVTPI
LAMALQLQRD GQPFELHYCA RAPERMAFRD EIGASRFSDR ASMYFSDLAD GPKFDAVAAF
RTAPAGAHLY VCGPAGFMDH VLASARTAGW AEERLHREHF TGAVQETAGD QPFQLRLARS
GATLDVPVGM TALQVLLDSG IDVNYSCESG VCGTCITAVL EGLPDHRDAC LMDSEHADNK
LFTPCCSRAK TPALVLDL
//
