ID A0A1E4NB28_9PROT Unreviewed; 486 AA.
AC A0A1E4NB28;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Flavodoxin oxidoreductase {ECO:0000313|EMBL:ODU88364.1};
GN ORFNames=ABT21_10585 {ECO:0000313|EMBL:ODU88364.1};
OS Thiobacillus sp. SCN 65-179.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660144 {ECO:0000313|EMBL:ODU88364.1, ECO:0000313|Proteomes:UP000094681};
RN [1] {ECO:0000313|EMBL:ODU88364.1, ECO:0000313|Proteomes:UP000094681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(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:ODU88364.1}.
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DR EMBL; MEGN01000006; ODU88364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4NB28; -.
DR STRING; 1660144.ABT21_10585; -.
DR Proteomes; UP000094681; 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; 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; 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}.
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 486 AA; 53302 MW; 860DE8170E18736A CRC64;
MSHLLPLSRV ARLVGQSRHA LQEMIRSGAL ATFDGMVEFD ELLRAFPDVK WDDDAELRRV
NEIKEKAFAK RVLERALPDK EVLAARLTEL GNDYAAAKAL LAHYASVMAW LDEKIDEIEE
EGSAETRHAL HTVRAFLLRN LAEAPADAAQ AQAAIAHERI LRIMSAHVTI QPSGHEFFVE
GNDTLLEAAL RNGVSLNYGC SNGNCGDCKA RLVSGEVKKV HAHDYVLKQA EKDRGVILLC
SYAPVNDVVV EANVAGARDI PVQEITAKVK SVEVFNPHMA ALHILAPRSQ RLRFLGGQGV
RLTVDGASGR YAIASCPCED RHIEVQIPRR EADVFAEALF TRLKANDSVA VEGPYGEFVL
DEDSPRPVIF LAFGAGFAPI KSLVQHAMSL DLAESMDLHW LADVAGHYQD NLCRAWADAL
DNFAYVPHPP VDDLDAALRA IVTDYPDLHR FDVYAAGTAA QLERAEAAFT GAGLHRPRWF
AGAIDA
//
