ID A0A171KQP9_9BURK Unreviewed; 317 AA.
AC A0A171KQP9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Vanillate O-demethylase ferredoxin subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=AAV32_11660 {ECO:0000313|EMBL:KKO71216.1};
OS Kerstersia gyiorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Kerstersia.
OX NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO71216.1, ECO:0000313|Proteomes:UP000078084};
RN [1] {ECO:0000313|EMBL:KKO71216.1, ECO:0000313|Proteomes:UP000078084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1 {ECO:0000313|EMBL:KKO71216.1,
RC ECO:0000313|Proteomes:UP000078084};
RA Greninger A.L., Kozyreva V., Chaturvedi V.;
RT "Genome sequence of Kerstersia gyiorum CG1.";
RL Submitted (APR-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:KKO71216.1}.
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DR EMBL; LBNE01000008; KKO71216.1; -; Genomic_DNA.
DR RefSeq; WP_068372136.1; NZ_LBNE01000008.1.
DR AlphaFoldDB; A0A171KQP9; -.
DR STRING; 206506.AAV32_11660; -.
DR PATRIC; fig|206506.3.peg.2483; -.
DR OrthoDB; 544091at2; -.
DR Proteomes; UP000078084; 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:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000078084}.
FT DOMAIN 1..103
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 232..317
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 317 AA; 34238 MW; 0E5DD444AC983DED CRC64;
MMTLTVTQKT READDVFSFQ LAASNGQPLP AYEAGAHIDL HLPQGQVRQY SLCMPSGAGQ
PGSYTVAVLR DPASRGGSIA LHDQIRVGMT LMASPPRNLF ALVPHAQKTL LFAGGIGITP
ILCMAQELAA RQQDFELHYC CRSRSKAAFA DFLESSAFAD RAHLHFDDVS PLDVQACLKP
PQAGQHLYVC GPNGFMQHVL TSASLCGWPE TQLHREHFAA VPANRPQADI AFEVEIASTG
AVHLIPPERS VFEVLDEAGI PLPVSCEQGV CGTCVTKLIA GTPDHRDQYL TAAEHARNDC
FTPCCSRALS PRLVLDI
//
