NUOM_MYCTO
ID NUOM_MYCTO Reviewed; 553 AA.
AC P9WIW4; L0TC01; O53307;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=NADH-quinone oxidoreductase subunit M;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit M;
DE AltName: Full=NDH-1 subunit M;
GN Name=nuoM; OrderedLocusNames=MT3245;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC menaquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK47584.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK47584.1; ALT_INIT; Genomic_DNA.
DR PIR; C70946; C70946.
DR RefSeq; WP_003416460.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WIW4; -.
DR SMR; P9WIW4; -.
DR EnsemblBacteria; AAK47584; AAK47584; MT3245.
DR GeneID; 45427144; -.
DR KEGG; mtc:MT3245; -.
DR PATRIC; fig|83331.31.peg.3493; -.
DR HOGENOM; CLU_007100_4_4_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507; PTHR43507; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
DR TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; NAD; Quinone; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..553
FT /note="NADH-quinone oxidoreductase subunit M"
FT /id="PRO_0000427934"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 113..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 59207 MW; E50510EEECBCC0DB CRC64;
MNNVPWLSVL WLVPLAGAVL IILLPPGRRR LAKWAGMVVS VLTLAVSIVV AAEFKPSAEP
YQFVEKHSWI PAFGAGYTLG VDGIAVVLVL LTTVLIPLLL VAGWNDATDA DDLSPASGRY
PQRPAPPRLR SSGGERTRGV HAYVALTLAI ESMVLMSVIA LDVLLFYVFF EAMLIPMYFL
IGGFGQGAGR SRAAVKFLLY NLFGGLIMLA AVIGLYVVTA QYDSGTFDFR EIVAGVAAGR
YGADPAVFKA LFLGFMFAFA IKAPLWPFHR WLPDAAVEST PATAVLMMAV MDKVGTFGML
RYCLQLFPDP STYFRPLIVT LAIIGVIYGA IVAIGQTDMM RLIAYTSISH FGFIIAGIFV
MTTQGQSGST LYMLNHGLST AAVFLIAGFL IARRGSRSIA DYGGVQKVAP ILAGTFMVSA
MATVSLPGLA PFISEFLVLL GTFSRYWLAA AFGVTALVLS AVYMLWLYQR VMTGPVAEGN
ERIGDLVGRE MIVVAPLIAL LLVLGVYPKP VLDIINPAVE NTMTTIGQHD PAPSVAHPVP
AVGASRTAEG PHP
