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Database: UniProt
Entry: Q8EH66_SHEON
LinkDB: Q8EH66_SHEON
Original site: Q8EH66_SHEON 
ID   Q8EH66_SHEON            Unreviewed;       370 AA.
AC   Q8EH66;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 144.
DE   SubName: Full=NADH oxidoreductase Hcr {ECO:0000313|EMBL:AAN54429.2};
GN   Name=hcr {ECO:0000313|EMBL:AAN54429.2};
GN   OrderedLocusNames=SO_1364 {ECO:0000313|EMBL:AAN54429.2};
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN54429.2, ECO:0000313|Proteomes:UP000008186};
RN   [1] {ECO:0000313|EMBL:AAN54429.2, ECO:0000313|Proteomes:UP000008186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1 {ECO:0000313|EMBL:AAN54429.2,
RC   ECO:0000313|Proteomes:UP000008186};
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA   Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA   Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN54429.2; -; Genomic_DNA.
DR   RefSeq; NP_716984.2; NC_004347.2.
DR   AlphaFoldDB; Q8EH66; -.
DR   SMR; Q8EH66; -.
DR   STRING; 211586.SO_1364; -.
DR   PaxDb; 211586-SO_1364; -.
DR   KEGG; son:SO_1364; -.
DR   PATRIC; fig|211586.12.peg.1313; -.
DR   eggNOG; COG1018; Bacteria.
DR   HOGENOM; CLU_003827_14_3_6; -.
DR   OrthoDB; 581532at2; -.
DR   PhylomeDB; Q8EH66; -.
DR   BioCyc; SONE211586:G1GMP-1262-MONOMER; -.
DR   Proteomes; UP000008186; 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; IBA:GO_Central.
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   Reference proteome {ECO:0000313|Proteomes:UP000008186};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT   DOMAIN          18..121
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          285..370
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   370 AA;  40819 MW;  25366770842F549E CRC64;
     MQNIMPNTAL SSTPANPVGF NQLVCVERWH ETADVVSFRF QAGEPMKFDY KPGQFITFVL
     EINGEQACRS YTLSSTPSRP YSLMVTIKRV DGGLVSNYLI DHLQPGQTVR VLPPTGQFNL
     FDIPANKYLF LSAGCGITPM YSMSRYLTDT QINADIAVVH SARTQADIIF KNTLETMAAR
     HASFKLCYLV EGVTTDTVWH TEEAFHYVGR LSAQNLLSLV PDFAERIVFL CGPELYMQAV
     KTILTELNFD MNKLYHESFA TAVKEAQSHV KQAEIQSETP TTSSTGFMLS IGDKKHLLTA
     EQTLLDGIEA EGLPIIAACR SGVCGACKCK VLQGETESTS YMTLTPTDIE AGYVLACSTR
     LKSDVTLSLI
//
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