ID F9RYC3_9VIBR Unreviewed; 358 AA.
AC F9RYC3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=NADH oxidoreductase Hcr {ECO:0000313|EMBL:EGU46929.1};
GN ORFNames=VII00023_17709 {ECO:0000313|EMBL:EGU46929.1};
OS Vibrio ichthyoenteri ATCC 700023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=870968 {ECO:0000313|EMBL:EGU46929.1, ECO:0000313|Proteomes:UP000004605};
RN [1] {ECO:0000313|EMBL:EGU46929.1, ECO:0000313|Proteomes:UP000004605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700023 {ECO:0000313|EMBL:EGU46929.1,
RC ECO:0000313|Proteomes:UP000004605};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EGU46929.1}.
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DR EMBL; AFWF01000031; EGU46929.1; -; Genomic_DNA.
DR RefSeq; WP_006710830.1; NZ_AFWF01000031.1.
DR AlphaFoldDB; F9RYC3; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000004605; 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 Membrane {ECO:0000256|ARBA:ARBA00022692};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT DOMAIN 8..117
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 271..358
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 358 AA; 39049 MW; 6D4AA28ADA0C6258 CRC64;
MYFEWQGSQP VQLRCIDKYV ETPDTMSIKL APLESQLAAF DSIQFDFKPG QFITVGVEIE
QKMEYRAYSL SSIAGESHLQ LTIKRVEGGK VSNYLLDNLQ VGDLLFALPP SGEFNSVDHP
PKPINGNTKA LLISAGCGIT PVYAMAKQWL ANGANVDVQF LHVAKSAQQT IYFDALESMA
ATEEQFTLSL LLKDASGTMH PQGRLNKEWL LQLVPDLIQR TVYLCGPQQF MQDTHDNLQA
LGFDMSNFVQ ESFTPISSAN EFEPDDHAED KTVSVSVEAF DKEMTVQQGA VLADTLEAAG
LPLIVACRSG ICGSCKCKVI AGSVRSTSLE TLTAAEIEQG YVLACSSTVE SDLAVQIG
//
