ID B0TJ82_SHEHH Unreviewed; 363 AA.
AC B0TJ82;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Oxidoreductase FAD-binding domain protein {ECO:0000313|EMBL:ABZ75673.1};
GN OrderedLocusNames=Shal_1104 {ECO:0000313|EMBL:ABZ75673.1};
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817 {ECO:0000313|EMBL:ABZ75673.1, ECO:0000313|Proteomes:UP000001317};
RN [1] {ECO:0000313|EMBL:ABZ75673.1, ECO:0000313|Proteomes:UP000001317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4 {ECO:0000313|EMBL:ABZ75673.1,
RC ECO:0000313|Proteomes:UP000001317};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004533}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
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DR EMBL; CP000931; ABZ75673.1; -; Genomic_DNA.
DR RefSeq; WP_012276218.1; NC_010334.1.
DR AlphaFoldDB; B0TJ82; -.
DR STRING; 458817.Shal_1104; -.
DR KEGG; shl:Shal_1104; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_14_3_6; -.
DR OrthoDB; 581532at2; -.
DR Proteomes; UP000001317; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 PRINTS; PR00406; CYTB5RDTASE.
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 Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT DOMAIN 20..123
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 279..363
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 363 AA; 40039 MW; C81C743EBDCE19E4 CRC64;
MVINKQASTV ESFSAEQWQS GEHQLVCVEK WNETHDVISF RFRGTTPVKF HFKPGQFLTL
LLEIDGEKIA RSYTISSSPS RPYSIVLTIK RIEGGKVSNY LADNLAVGHM VRALGPEGVF
NLLDIQADKY LFLSAGCGIT PMYSMSRWLT DTEIGADISF LHSAKSSEDL IFKDSLAQMA
QRNAQFNLNY ILEQLTCEAD VHIDSRAGRL TAEKLERLVP DFRSRTVFVC GPEPYMQAVK
ALLESLEFDM TQFHQESFGS FKGDMGELAA AKDDSAKASG FMLNIGERRR ALSAEQTVLD
GIEAEGLPII AACRSGVCGA CKCKVIEGDI ESTSQMALTP DEVAQGYVLA CSTRLKSDVT
LEL
//
