NUOM_BUCAP
ID NUOM_BUCAP Reviewed; 501 AA.
AC Q8K9X6;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=BUsg_158;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient (By
CC 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 -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoA, H, J, K, L,
CC M, N constitute the membrane sector of the complex (By similarity).
CC {ECO:0000250}.
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; AE013218; AAM67726.1; -; Genomic_DNA.
DR RefSeq; WP_011053693.1; NC_004061.1.
DR AlphaFoldDB; Q8K9X6; -.
DR SMR; Q8K9X6; -.
DR STRING; 198804.BUsg_158; -.
DR EnsemblBacteria; AAM67726; AAM67726; BUsg_158.
DR KEGG; bas:BUsg_158; -.
DR eggNOG; COG1008; Bacteria.
DR HOGENOM; CLU_007100_4_4_6; -.
DR OMA; RIACSSV; -.
DR OrthoDB; 535707at2; -.
DR Proteomes; UP000000416; 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..501
FT /note="NADH-quinone oxidoreductase subunit M"
FT /id="PRO_0000118042"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 501 AA; 57884 MW; 2218E31ED3EFFDE2 CRC64;
MLLSLLVIIP FLSGIFSFFS FRFQKNIPRW IALTGMGLTL LTVIRIWFFE DYYTYQIQSY
THLSYQLILP WISSFGIQFH IAVDGFSIVM LFLTLFLGII AILCSWNEIK KNEGFFYLNI
MLVLMGTIGV FIAFDLFLFF FFWEIILIPM YFLISLWNQK KEDKKKCINI ANKFFIYTQI
SGLIMLASIL LLVLNYYINN KILTFNYDLL LIQPVDKSIE YIIMLGFFLA FIIKMPIVPF
HGWLADFHER SPYCGAVDII GALLKTAPYG LLRYNKMLFP NATEQFAPIA IFLGFLSMFY
GAWVAFSQVN IKRLIAYSSI SHMGLMLIAI YGGNEISFQG LIIQILSNSI STSALFILSG
QIYKYLKTQD ISEMGGLWTN IYWIPGFSLF FALSNLGIPG TGNFIGEFLI LFGIFKEHPL
VSIISTIGII FSSIYSLNMI QKIYYGLSKH DFPKFFLNIK EFWISIVLIF ALIFLGLIPQ
KILNISFESI HFIYNFSKRI Q