ID C6XD00_METGS Unreviewed; 516 AA.
AC C6XD00;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ACT50425.1};
DE EC=1.6.5.11 {ECO:0000313|EMBL:ACT50425.1};
GN OrderedLocusNames=Msip34_1178 {ECO:0000313|EMBL:ACT50425.1};
OS Methylovorus glucosotrophus (strain SIP3-4).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylovorus.
OX NCBI_TaxID=582744 {ECO:0000313|EMBL:ACT50425.1, ECO:0000313|Proteomes:UP000002743};
RN [1] {ECO:0000313|EMBL:ACT50425.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP3-4 {ECO:0000313|EMBL:ACT50425.1};
RX PubMed=21622745; DOI=10.1128/JB.00404-11;
RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT "Genomes of three methylotrophs from a single niche uncover genetic and
RT metabolic divergence of Methylophilaceae.";
RL J. Bacteriol. 193:3757-3764(2011).
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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DR EMBL; CP001674; ACT50425.1; -; Genomic_DNA.
DR RefSeq; WP_015829928.1; NC_012969.1.
DR AlphaFoldDB; C6XD00; -.
DR STRING; 582744.Msip34_1178; -.
DR KEGG; mei:Msip34_1178; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_3_0_4; -.
DR OrthoDB; 9805533at2; -.
DR Proteomes; UP000002743; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR CDD; cd03063; TRX_Fd_FDH_beta; 1.
DR Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 6.10.250.1450; -; 1.
DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:ACT50425.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002743}.
FT DOMAIN 425..470
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 516 AA; 55575 MW; DC1BAE08D56ADB97 CRC64;
MARIYVPRDS SALSLGAEKV AKAIAEHAAR QNLAVEIIRN GSRGMFWLEP LVEVETPAGR
IAYGPVDLAD VPSLFAADFI NGGAHALKLG VTDELPWLKQ QERLTFARVG ITDPVSLTDY
LAHDGYRGLQ NALALQPAEI VQQVTDSGLR GRGGAAFPTG IKWKTVHDCK ADQKYIVCNA
DEGDSGTYSD RMIMEGDPFV LIEGMTIAAL AVGATQGYIY LRSEYPHALA VLNEAIQHAR
EKHYLGPNIL GSGHAFELEV RRAAGAYVCG EETSLLESLE GKRGLVRFKP PLPAIEGLFG
KPTVVNNVIS FASVPIILDK GGAFYRDYGM GRSRGTLPIQ LAGNIKHGGL VEKAFGVTLR
QLLYDFGGGS ATGRPIRAVQ VGGPLGAYLP ESQFDTPLDY EEFSKLWAVL GHGGIVAFDD
TVDMAKMARY AFEFCAIESC GKCTPCRIGS TRGVEVMDKI MQGRDHAQNI ALVRDLSDTM
LNGSLCALGG MTPYPVLSAI NHFPEDFGLN KKAQAA
//
