ID C3TGT2_ECOLX Unreviewed; 322 AA.
AC C3TGT2;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=NADH oxidoreductase {ECO:0000313|EMBL:ACI85916.1, ECO:0000313|EMBL:QCL49388.1};
GN ORFNames=C9E67_20895 {ECO:0000313|EMBL:QCL49388.1}, ECs0958
GN {ECO:0000313|EMBL:ACI85916.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI85916.1};
RN [1] {ECO:0000313|EMBL:ACI85916.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=493/89 {ECO:0000313|EMBL:ACI85916.1}, 86-24
RC {ECO:0000313|EMBL:ACI85917.1}, 87-14 {ECO:0000313|EMBL:ACI85918.1},
RC and TW14359 {ECO:0000313|EMBL:ACI85920.1};
RX PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "A precise reconstruction of the emergence and constrained radiations of
RT Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
RN [2] {ECO:0000313|EMBL:QCL49388.1, ECO:0000313|Proteomes:UP000298553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=143 {ECO:0000313|EMBL:QCL49388.1,
RC ECO:0000313|Proteomes:UP000298553};
RA Bono J.L., Arthur T.M.;
RT "WGA of Escherichia coli O157:H7: comparison of multiple isolates.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; EU903370; ACI85916.1; -; Genomic_DNA.
DR EMBL; EU903371; ACI85917.1; -; Genomic_DNA.
DR EMBL; EU903372; ACI85918.1; -; Genomic_DNA.
DR EMBL; EU903374; ACI85920.1; -; Genomic_DNA.
DR EMBL; CP028607; QCL49388.1; -; Genomic_DNA.
DR RefSeq; WP_000178647.1; NZ_VODI01000074.1.
DR PATRIC; fig|562.7073.peg.3136; -.
DR OMA; MQVHHIH; -.
DR Proteomes; UP000298553; Chromosome.
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:UniProtKB-KW.
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:ARBA00022714}.
FT DOMAIN 7..107
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 237..322
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 322 AA; 35868 MW; B820FC024F37B680 CRC64;
MTMPTNQCPW RMQVHHIKQE TPDVWTISLI CHDYYPYRAG QYALVSVRNS AETLRAYTIS
STPGVSEYIT LTVRRIDDGV GSQWLTRDVK RGDYLWLSDA MGEFTCDDKA EDKFLLLAAG
CGVTPIMSMR RWLAKNRPQA DVRVIYNVRT PQDVIFADEW RNYPVTLVAE NNVTEGFIAG
RLTRELLTRV PDLASRTVMT CGPAPYMDWV EQEVKALGVT RFFKEKFFTP VAEAATSGLK
FTKLQPAQEF YAPVGTTLLE ALESNNVPVV AACRAGVCGC CKTKVVSGEY TVSSTMTLTD
AEIAEGYVLA CSCHPQGDLV LA
//
