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Protein

NADH-quinone oxidoreductase subunit M

Gene

nuoM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.

Catalytic activityi

NADH + a quinone = NAD+ + a quinol.

GO - Molecular functioni

  • NADH dehydrogenase (ubiquinone) activity Source: InterPro
  • ubiquinone binding Source: EcoCyc

GO - Biological processi

  • aerobic respiration Source: EcoCyc
  • ATP synthesis coupled electron transport Source: InterPro
  • electron transport coupled proton transport Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, Ubiquinone

Enzyme and pathway databases

BioCyciEcoCyc:NUOM-MONOMER.
ECOL316407:JW2272-MONOMER.
MetaCyc:NUOM-MONOMER.

Protein family/group databases

TCDBi3.D.1.1.1. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-quinone oxidoreductase subunit M (EC:1.6.5.11)
Alternative name(s):
NADH dehydrogenase I subunit M
NDH-1 subunit M
NUO13
Gene namesi
Name:nuoM
Ordered Locus Names:b2277, JW2272
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11773. nuoM.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1 – 2121HelicalSequence analysisAdd
BLAST
Topological domaini22 – 298CytoplasmicSequence analysis
Transmembranei30 – 5021HelicalSequence analysisAdd
BLAST
Topological domaini51 – 8232PeriplasmicSequence analysisAdd
BLAST
Transmembranei83 – 10321HelicalSequence analysisAdd
BLAST
Topological domaini104 – 12118CytoplasmicSequence analysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence analysisAdd
BLAST
Topological domaini143 – 17331PeriplasmicSequence analysisAdd
BLAST
Transmembranei174 – 19421HelicalSequence analysisAdd
BLAST
Topological domaini195 – 22127CytoplasmicSequence analysisAdd
BLAST
Transmembranei222 – 24221HelicalSequence analysisAdd
BLAST
Topological domaini243 – 25816PeriplasmicSequence analysisAdd
BLAST
Transmembranei259 – 27921HelicalSequence analysisAdd
BLAST
Topological domaini280 – 2856CytoplasmicSequence analysis
Transmembranei286 – 30621HelicalSequence analysisAdd
BLAST
Topological domaini307 – 3137PeriplasmicSequence analysis
Transmembranei314 – 33421HelicalSequence analysisAdd
BLAST
Topological domaini335 – 3395CytoplasmicSequence analysis
Transmembranei340 – 36021HelicalSequence analysisAdd
BLAST
Topological domaini361 – 38222PeriplasmicSequence analysisAdd
BLAST
Transmembranei383 – 40321HelicalSequence analysisAdd
BLAST
Transmembranei404 – 42421HelicalSequence analysisAdd
BLAST
Topological domaini425 – 4251PeriplasmicSequence analysis
Transmembranei426 – 44621HelicalSequence analysisAdd
BLAST
Topological domaini447 – 46418CytoplasmicSequence analysisAdd
BLAST
Transmembranei465 – 48521HelicalSequence analysisAdd
BLAST
Topological domaini486 – 50924PeriplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • NADH dehydrogenase complex Source: EcoliWiki
  • plasma membrane Source: EcoCyc
  • plasma membrane respiratory chain complex I Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 509509NADH-quinone oxidoreductase subunit MPRO_0000118039Add
BLAST

Keywords - PTMi

Quinone

Proteomic databases

PaxDbiP0AFE8.

Interactioni

Subunit structurei

Composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.

Protein-protein interaction databases

BioGridi4260887. 40 interactions.
DIPiDIP-59255N.
STRINGi511145.b2277.

Structurei

3D structure databases

ProteinModelPortaliP0AFE8.
SMRiP0AFE8. Positions 1-504.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I subunit 4 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C8S. Bacteria.
COG1008. LUCA.
HOGENOMiHOG000100682.
InParanoidiP0AFE8.
KOiK00342.
OMAiTWPILSV.
OrthoDBiEOG647TZ6.
PhylomeDBiP0AFE8.

Family and domain databases

InterProiIPR010227. NADH_Q_OxRdtase_chainM/4.
IPR003918. NADH_UbQ_OxRdtase.
IPR001750. ND/Mrp_mem.
[Graphical view]
PfamiPF00361. Proton_antipo_M. 1 hit.
[Graphical view]
PRINTSiPR01437. NUOXDRDTASE4.
TIGRFAMsiTIGR01972. NDH_I_M. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AFE8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLPWLILIP FIGGFLCWQT ERFGVKVPRW IALITMGLTL ALSLQLWLQG
60 70 80 90 100
GYSLTQSAGI PQWQSEFDMP WIPRFGISIH LAIDGLSLLM VVLTGLLGVL
110 120 130 140 150
AVLCSWKEIE KYQGFFHLNL MWILGGVIGV FLAIDMFLFF FFWEMMLVPM
160 170 180 190 200
YFLIALWGHK ASDGKTRITA ATKFFIYTQA SGLVMLIAIL ALVFVHYNAT
210 220 230 240 250
GVWTFNYEEL LNTPMSSGVE YLLMLGFFIA FAVKMPVVPL HGWLPDAHSQ
260 270 280 290 300
APTAGSVDLA GILLKTAAYG LLRFSLPLFP NASAEFAPIA MWLGVIGIFY
310 320 330 340 350
GAWMAFAQTD IKRLIAYTSV SHMGFVLIAI YTGSQLAYQG AVIQMIAHGL
360 370 380 390 400
SAAGLFILCG QLYERIHTRD MRMMGGLWSK MKWLPALSLF FAVATLGMPG
410 420 430 440 450
TGNFVGEFMI LFGSFQVVPV ITVISTFGLV FASVYSLAML HRAYFGKAKS
460 470 480 490 500
QIASQELPGM SLRELFMILL LVVLLVLLGF YPQPILDTSH SAIGNIQQWF

VNSVTTTRP
Length:509
Mass (Da):56,525
Last modified:December 20, 2005 - v1
Checksum:i3F8395683908EF97
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti464 – 4652EL → DV (PubMed:7690854).Curated
Sequence conflicti464 – 4652EL → DV (PubMed:8366049).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68301 Genomic DNA. Translation: CAA48372.1.
L19568 Genomic DNA. Translation: AAA53583.1.
U00096 Genomic DNA. Translation: AAC75337.1.
AP009048 Genomic DNA. Translation: BAA16105.1.
PIRiC64999.
RefSeqiNP_416780.1. NC_000913.3.
WP_000926441.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75337; AAC75337; b2277.
BAA16105; BAA16105; BAA16105.
GeneIDi947731.
KEGGiecj:JW2272.
eco:b2277.
PATRICi32119921. VBIEscCol129921_2370.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68301 Genomic DNA. Translation: CAA48372.1.
L19568 Genomic DNA. Translation: AAA53583.1.
U00096 Genomic DNA. Translation: AAC75337.1.
AP009048 Genomic DNA. Translation: BAA16105.1.
PIRiC64999.
RefSeqiNP_416780.1. NC_000913.3.
WP_000926441.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AFE8.
SMRiP0AFE8. Positions 1-504.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260887. 40 interactions.
DIPiDIP-59255N.
STRINGi511145.b2277.

Protein family/group databases

TCDBi3.D.1.1.1. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Proteomic databases

PaxDbiP0AFE8.

Protocols and materials databases

DNASUi947731.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75337; AAC75337; b2277.
BAA16105; BAA16105; BAA16105.
GeneIDi947731.
KEGGiecj:JW2272.
eco:b2277.
PATRICi32119921. VBIEscCol129921_2370.

Organism-specific databases

EchoBASEiEB1722.
EcoGeneiEG11773. nuoM.

Phylogenomic databases

eggNOGiENOG4105C8S. Bacteria.
COG1008. LUCA.
HOGENOMiHOG000100682.
InParanoidiP0AFE8.
KOiK00342.
OMAiTWPILSV.
OrthoDBiEOG647TZ6.
PhylomeDBiP0AFE8.

Enzyme and pathway databases

BioCyciEcoCyc:NUOM-MONOMER.
ECOL316407:JW2272-MONOMER.
MetaCyc:NUOM-MONOMER.

Miscellaneous databases

PROiP0AFE8.

Family and domain databases

InterProiIPR010227. NADH_Q_OxRdtase_chainM/4.
IPR003918. NADH_UbQ_OxRdtase.
IPR001750. ND/Mrp_mem.
[Graphical view]
PfamiPF00361. Proton_antipo_M. 1 hit.
[Graphical view]
PRINTSiPR01437. NUOXDRDTASE4.
TIGRFAMsiTIGR01972. NDH_I_M. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I."
    Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.
    J. Mol. Biol. 233:109-122(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / AN387.
  2. "Escherichia coli mutants lacking NADH dehydrogenase I have a competitive disadvantage in stationary phase."
    Zambrano M.M., Kolter R.G.
    J. Bacteriol. 175:5642-5647(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiNUOM_ECOLI
AccessioniPrimary (citable) accession number: P0AFE8
Secondary accession number(s): P31978, P78248
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 20, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.