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Database: UniProt
Entry: Q57R64_SALCH
LinkDB: Q57R64_SALCH
Original site: Q57R64_SALCH 
ID   Q57R64_SALCH            Unreviewed;       323 AA.
AC   Q57R64;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 122.
DE   SubName: Full=NADH oxidoreductase for hcp gene product {ECO:0000313|EMBL:AAX64797.1};
GN   Name=hcr {ECO:0000313|EMBL:AAX64797.1};
GN   OrderedLocusNames=SCH_0891 {ECO:0000313|EMBL:AAX64797.1};
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314 {ECO:0000313|EMBL:AAX64797.1, ECO:0000313|Proteomes:UP000000538};
RN   [1] {ECO:0000313|EMBL:AAX64797.1, ECO:0000313|Proteomes:UP000000538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67 {ECO:0000313|EMBL:AAX64797.1,
RC   ECO:0000313|Proteomes:UP000000538};
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.Y., Wang H.S.,
RA   Lee Y.S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; AE017220; AAX64797.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q57R64; -.
DR   KEGG; sec:SCH_0891; -.
DR   HOGENOM; CLU_003827_14_3_6; -.
DR   OMA; MQVHHIH; -.
DR   Proteomes; UP000000538; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
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; 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; PR00409; PHDIOXRDTASE.
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:ARBA00022723}.
FT   DOMAIN          8..108
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          238..323
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   323 AA;  35806 MW;  D19B20E39C54A0A9 CRC64;
     MMTMPTSQCP WRMQVHHIRQ ETPDVWTIAL LCHDYYPYRA GQYALVSVRN SAETLRAYTL
     SSTPGVSEYI TLTVRRIEDG TGSQWLTHDI KRGDYIWLSD AMGDFTCDDK TEDKFLLLAA
     GCGVTPIMSM RRWLAKYRPQ ADVQVIFNVR SPDDVIFADE WRQYPVTLVA ENHATEGFVA
     GRLTTELLQS VPDLASRTIM TCGPAPYMDF VEQGVKALGV TRFFKEKFFT PVAETATSGL
     KFTKLQPAQE FYAPIGTTLL EALESNKVPV AAACRAGVCG CCKTKVVSGD YTVSSTMTLS
     EAEIAEGYVL ACSCHPQGDL VLA
//
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