ID A0A106BNE6_THIDE Unreviewed; 487 AA.
AC A0A106BNE6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Flavodoxin oxidoreductase {ECO:0000313|EMBL:KVW95681.1};
GN ORFNames=ABW22_09630 {ECO:0000313|EMBL:KVW95681.1};
OS Thiobacillus denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW95681.1, ECO:0000313|Proteomes:UP000064243};
RN [1] {ECO:0000313|EMBL:KVW95681.1, ECO:0000313|Proteomes:UP000064243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG {ECO:0000313|EMBL:KVW95681.1,
RC ECO:0000313|Proteomes:UP000064243};
RX PubMed=26712544;
RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT Chemoautotroph.";
RL Appl. Environ. Microbiol. 82:1486-1495(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KVW95681.1}.
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DR EMBL; LDUG01000024; KVW95681.1; -; Genomic_DNA.
DR RefSeq; WP_059755521.1; NZ_LDUG01000024.1.
DR AlphaFoldDB; A0A106BNE6; -.
DR STRING; 1123392.GCA_000376425_02704; -.
DR PATRIC; fig|36861.3.peg.1587; -.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000064243; 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 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; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
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; 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:UP000064243}.
FT DOMAIN 166..256
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 262..361
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 487 AA; 53986 MW; BEEB09D2B038FA5B CRC64;
MSHLLPLSRV AKLVGQPRHT LQEMIRSGTL ATFDGMVELD ELLRAFPEVR WDDDAEFRRV
TEIKDKAFAK RVRERALPDK DVLVARLNEL GGDYAAAKAL LLHYGNVMIW LDEKIEELEE
NASAETHHAL HTVRAFLLRN LAETPPDAVL AQAVIAQERI LKLMSAHVTI QPSGHEFYVD
GNDTLLEAAL RNGVSLSYGC SNGNCGDCKA RVVSGEVKKV HAHDYVLKQA EKDAGVILLC
AYAPVNDVVI EANVAEARDI PVQQITAKVK SVEVFNPQMA ALHILAPRSQ RLRYLGGQSI
QVRVNGVSGR YAIASCPCDD RHIEVQIPHR PDDAFAEALF TTLKTNDTVE LEGPFGEFVL
DEDSPRPVIF LAFGAGFAPI KSLIQHAMSL ELAESMDLHW LADEAGHYQD NLCRAWADAL
DNFNYVPHAH RDDLDAVLAD IVLDYPDLHR FDVYAAGTAT QLDQARAHFV RHGLPGARWF
AGATDTY
//
