ID A5KWW5_VIBBS Unreviewed; 351 AA.
AC A5KWW5;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Flavohemoprotein {ECO:0000313|EMBL:EDK30055.1};
GN ORFNames=VSWAT3_26481 {ECO:0000313|EMBL:EDK30055.1};
OS Vibrionales bacterium (strain SWAT-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales.
OX NCBI_TaxID=391574 {ECO:0000313|EMBL:EDK30055.1, ECO:0000313|Proteomes:UP000004912};
RN [1] {ECO:0000313|EMBL:EDK30055.1, ECO:0000313|Proteomes:UP000004912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWAT-3 {ECO:0000313|EMBL:EDK30055.1,
RC ECO:0000313|Proteomes:UP000004912};
RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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:EDK30055.1}.
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DR EMBL; AAZW01000005; EDK30055.1; -; Genomic_DNA.
DR AlphaFoldDB; A5KWW5; -.
DR Proteomes; UP000004912; 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; cd06215; FNR_iron_sulfur_binding_1; 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; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF6; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
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}.
FT DOMAIN 7..110
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 265..351
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 351 AA; 38805 MW; E13B523684BBA614 CRC64;
MYAWSDSDSI NLVCLKKWHE TPDTVSFELG SIPQDLHFNF KPGQFITLGL DMPTKTDYRA
YSVASCPEDN RLKLTVKRVE GGLVSNFIVD ELDEGDEVAV LKPAGGFNCI DCMPTESKKV
TLVSAGCGIT PVMAMVKYWL SQDSGVEIDF IHMARNKRET IYFEELHQLD ETHSNFNLKL
LLKDNQGTTT PQGRLDKNWL VSLSPDILAR TVYLCGPVGF MQDIESYLKE LEFNMDNFYQ
ESFTPATQNG HSEEPETEVA DNENSAVKVF VPTFGKEVEA EVGTPLADSL EQAGVPIIIA
CRSGICGSCK CKVTKGSVES SSQETLTAEE VEQGYVLACS SSIQSDVEVE L
//
