ID   NUOM_RHOCA              Reviewed;         512 AA.
AC   P50974;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
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;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=8566820; DOI=10.1016/0378-1119(95)00693-1;
RA   Dupuis A., Peinnequin A., Chevallet M., Lunardi J., Darrouzet E.,
RA   Pierrard B., Procaccio V., Issartel J.P.;
RT   "Identification of five Rhodobacter capsulatus genes encoding the
RT   equivalent of ND subunits of the mitochondrial NADH-ubiquinone
RT   oxidoreductase.";
RL   Gene 167:99-104(1995).
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       ubiquinone. 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.
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}.
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DR   EMBL; AF029365; AAC25004.1; -; Genomic_DNA.
DR   RefSeq; WP_013067260.1; NZ_VIBE01000008.1.
DR   AlphaFoldDB; P50974; -.
DR   SMR; P50974; -.
DR   GeneID; 31490416; -.
DR   OMA; ITRWGNQ; -.
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; IPR000260; NADH4_N.
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; PF01059; Oxidored_q5_N; 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; Ubiquinone.
FT   CHAIN           1..512
FT                   /note="NADH-quinone oxidoreductase subunit M"
FT                   /id="PRO_0000118045"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        464..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   512 AA;  55756 MW;  80101F033C529631 CRC64;
     MQNLLSIITF LPLAAAAVLA VVSRGSGPAA DRNAKWVALT ATVVTFLVSL LLLAGFDPAN
     PGMQFVEDRA WIMGLHYKLG VDGISILFVM LTTFLMPLTI ASAWHVETRV KEYMIAFLVL
     EALMIGVFVA LDLVLFYLFF EAGLIPMFLI IGIWGGKERI YAAFKFFLYT FLGSVLMLVA
     MVAMYMMAGT TDIVTLMSFD FPHADLPFLG WWTLTGGVQT LLFLAFFASF AVKMPMWPVH
     TWLPDAHVQA PTAGSVVLAA VLLKMGGYGF LRFSLPMFPV GAETMTTFVF ILSAVAIVYT
     SLVALAQEDM KKLIAYSSVA HMGYVTMGIF AANQQGVDGA IFQMLSHGFI SGALFLCVGV
     IYDRMHTREI AAYGGLVNRM PAYALIFMFF TMANVGLPGT SGFVGEFLTL LGIFQVNTWV
     ALFATSGVIL SAAYALWLYR RVVFGELVKE SLKTISDMTT REKAIFAPLV AMTLLLGVYP
     SLVTDLIGPS VAHLVQNYHA DLGTLAQATA GN