ID A0A0N1KIX1_9GAMM Unreviewed; 350 AA.
AC A0A0N1KIX1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=NADH oxidoreductase {ECO:0000313|EMBL:KPD03204.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:KPD03204.1};
GN ORFNames=M992_1336 {ECO:0000313|EMBL:KPD03204.1};
OS Moellerella wisconsensis ATCC 35017.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Moellerella.
OX NCBI_TaxID=1354267 {ECO:0000313|EMBL:KPD03204.1, ECO:0000313|Proteomes:UP000053226};
RN [1] {ECO:0000313|EMBL:KPD03204.1, ECO:0000313|Proteomes:UP000053226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35017 {ECO:0000313|EMBL:KPD03204.1,
RC ECO:0000313|Proteomes:UP000053226};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPD03204.1}.
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; LGAA01000014; KPD03204.1; -; Genomic_DNA.
DR RefSeq; WP_053907846.1; NZ_LGAA01000014.1.
DR AlphaFoldDB; A0A0N1KIX1; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000053226; Unassembled WGS sequence.
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; 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 Oxidoreductase {ECO:0000313|EMBL:KPD03204.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053226}.
FT DOMAIN 7..107
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 265..350
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 350 AA; 38765 MW; 2A2091CA269C93A5 CRC64;
MTMPTTLCPN RMQVHSVYQE TPDVWTINLI NHDFYTYDPG QFALVSIENS GDTLRAYTLS
SSPGLSPFIT ITVRRLDNGM GSNWLTQSVK PGDYLWLSDA QGEFSCANIA HDNYLMLAAG
CGVTPIMSMV RWLLANKPSA NIKVLFNVRD EQQVIFSREW QYLLGQYPQQ LQLCIMQESP
DQGEITQGRL TQQKLAALVP DIQSRVVMTC GPAAYMQNVQ NFATELGVDA ANFFMERFST
EPLLSETTLT EYKPSDAGKS AENTQTVMLK VRHQLTDYSV PVGMSLLAAM ELNKLPVVAA
CRAGVCGSCK TQVITGDYTQ SSQMTLTAEE IEQGYVLACS CQLRGNIEIA
//
