ID A0A0D5AGG4_9NOCA Unreviewed; 362 AA.
AC A0A0D5AGG4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Vanillate O-demethylase oxidoreductase {ECO:0000313|EMBL:AJW42010.1};
GN ORFNames=NY08_4005 {ECO:0000313|EMBL:AJW42010.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW42010.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW42010.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW42010.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP010797; AJW42010.1; -; Genomic_DNA.
DR RefSeq; WP_052683875.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5AGG4; -.
DR STRING; 1564114.NY08_4005; -.
DR KEGG; rhb:NY08_4005; -.
DR PATRIC; fig|1564114.4.peg.3952; -.
DR HOGENOM; CLU_003827_17_0_11; -.
DR Proteomes; UP000032410; Chromosome.
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; IPR008333; Cbr1-like_FAD-bd_dom.
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; PF00970; FAD_binding_6; 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:AJW42010.1};
KW Transferase {ECO:0000313|EMBL:AJW42010.1}.
FT DOMAIN 50..150
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 275..362
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 362 AA; 39012 MW; EF2790CBEF2BC060 CRC64;
MHSHLGEITV TAPGRGLRAI GAASRFYARL VTDSPIVTAL SPARPRRSVG YEFETVVDDT
IDEAEDVRSL LLSRRDGAPL PTWQPGAHID VTTPSGSVRQ YSLAGRPGSG DHYRISVRKI
PGGRASTEIH ALSRGAVLRV RGPRNAFPMA EAEHYLFVAA GIGITPIRAM IERAVRDGAR
WTLYYHGRSR ASLPFVALLQ QLALTSRGHV IVKTDDVDGF PVPEDIVDLG MGNSAMYVCG
PAALSGRLRD ESLASTAVRE FHTELFAPAA VVDGMPFVLK LDRSGDTIEV GAQETALDAL
RRSRPDQPFS CRQGFCGACV VGLVAGRVEH RDRVLSPSER ENSLTLCVSR AAVDGEALVL
DL
//
