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Database: UniProt
Entry: A0A160FVC9_9BURK
LinkDB: A0A160FVC9_9BURK
Original site: A0A160FVC9_9BURK 
ID   A0A160FVC9_9BURK        Unreviewed;       323 AA.
AC   A0A160FVC9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Vanillate O-demethylase oxidoreductase {ECO:0000313|EMBL:ANB76956.1};
GN   ORFNames=AYM40_32990 {ECO:0000313|EMBL:ANB76956.1};
OS   Paraburkholderia phytofirmans OLGA172.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB76956.1, ECO:0000313|Proteomes:UP000076852};
RN   [1] {ECO:0000313|EMBL:ANB76956.1, ECO:0000313|Proteomes:UP000076852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLGA172 {ECO:0000313|EMBL:ANB76956.1,
RC   ECO:0000313|Proteomes:UP000076852};
RX   PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA   Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT   "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT   chlorocatechol degradative operon in a region of genome plasticity.";
RL   Gene 586:239-247(2016).
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DR   EMBL; CP014579; ANB76956.1; -; Genomic_DNA.
DR   RefSeq; WP_063500164.1; NZ_CP014579.1.
DR   AlphaFoldDB; A0A160FVC9; -.
DR   STRING; 1804984.AYM40_32990; -.
DR   KEGG; buz:AYM40_32990; -.
DR   Proteomes; UP000076852; Chromosome 2.
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:ANB76956.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076852};
KW   Transferase {ECO:0000313|EMBL:ANB76956.1}.
FT   DOMAIN          2..104
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          236..323
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   323 AA;  35390 MW;  9D5D3B463B207069 CRC64;
     MNTLLQVKVA SKIWLADDIG GYELSPLSDG GLPAFEAGSH IDLHVPLGPM RQYSLYDLPG
     ENPCYRIGVL RDPQSRGGSV KLLDDVQVGD TLTISAPRNH FALHSGQEDR SILFAGGIGI
     TPILCMAQQL ARERRPFEMH YCGRTLSRMA FVDRLQQAQF GDESQVHVHV DDGTPGQQLD
     ASSSIGSPSP DKHLYVCGPT GFMDHILQTA RELGWDEGHL HREYFAASPI DSSDDERFEI
     EIGSSGRIIE VHADQSAAHA LLDAGFNLPL SCEQGVCGTC MTKVLDGVPD HRDLYLTDEE
     RASNDSFMPC CSRAKTSRLV LDL
//
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