HCR_ECOLI
ID HCR_ECOLI Reviewed; 322 AA.
AC P75824;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=NADH oxidoreductase HCR;
DE EC=1.-.-.-;
GN Name=hcr; Synonyms=ybjV; OrderedLocusNames=b0872, JW5117;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10651802; DOI=10.1046/j.1432-1327.2000.01032.x;
RA van den Berg W.A.M., Hagen W.R., van Dongen W.M.A.M.;
RT "The hybrid-cluster protein ('prismane protein') from Escherichia coli.
RT Characterization of the hybrid-cluster protein, redox properties of the
RT [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH
RT oxidoreductase containing FAD and 2Fe-2S.";
RL Eur. J. Biochem. 267:666-676(2000).
CC -!- FUNCTION: NADH oxidoreductase acting in concert with HCP.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SIMILARITY: In the N-terminal section; belongs to the FAD-binding
CC oxidoreductase type 6 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC73959.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35586.2; -; Genomic_DNA.
DR PIR; H64825; H64825.
DR RefSeq; NP_415393.1; NC_000913.3.
DR RefSeq; WP_000178677.1; NZ_LN832404.1.
DR AlphaFoldDB; P75824; -.
DR SMR; P75824; -.
DR BioGRID; 4262097; 14.
DR BioGRID; 851973; 13.
DR IntAct; P75824; 16.
DR STRING; 511145.b0872; -.
DR jPOST; P75824; -.
DR PaxDb; P75824; -.
DR PRIDE; P75824; -.
DR EnsemblBacteria; AAC73959; AAC73959; b0872.
DR EnsemblBacteria; BAA35586; BAA35586; BAA35586.
DR GeneID; 66670854; -.
DR GeneID; 947660; -.
DR KEGG; ecj:JW5117; -.
DR KEGG; eco:b0872; -.
DR PATRIC; fig|1411691.4.peg.1405; -.
DR EchoBASE; EB3455; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_14_3_6; -.
DR InParanoid; P75824; -.
DR OMA; MQVHHIH; -.
DR PhylomeDB; P75824; -.
DR BioCyc; EcoCyc:G6456-MON; -.
DR BioCyc; MetaCyc:G6456-MON; -.
DR PRO; PR:P75824; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:EcoCyc.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 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; IPR000951; Ph_dOase_redase.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
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; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Transport.
FT CHAIN 1..322
FT /note="NADH oxidoreductase HCR"
FT /id="PRO_0000083928"
FT DOMAIN 7..107
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 237..322
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT REGION 111..213
FT /note="Oxidoreductase"
FT BINDING 273
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 278
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 281
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 311
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 322 AA; 35740 MW; 5138026DCBBD6A9C CRC64;
MTMPTNQCPW RMQVHHITQE TPDVWTISLI CHDYYPYRAG QYALVSVRNS AETLRAYTIS
STPGVSEYIT LTVRRIDDGV GSQWLTRDVK RGDYLWLSDA MGEFTCDDKA EDKFLLLAAG
CGVTPIMSMR RWLAKNRPQA DVRVIYNVRT PQDVIFADEW RNYPVTLVAE NNVTEGFIAG
RLTRELLAGV PDLASRTVMT CGPAPYMDWV EQEVKALGVT RFFKEKFFTP VAEAATSGLK
FTKLQPAREF YAPVGTTLLE ALESNNVPVV AACRAGVCGC CKTKVVSGEY TVSSTMTLTD
AEIAEGYVLA CSCHPQGDLV LA
