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P0AFD4 (NUOH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH-quinone oxidoreductase subunit H

EC=1.6.99.5
Alternative name(s):
NADH dehydrogenase I subunit H
NDH-1 subunit H
NUO8
Gene names
Name:nuoH
Ordered Locus Names:b2282, JW2277
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. This subunit may bind ubiquinone. HAMAP MF_01350

Catalytic activity

NADH + quinone = NAD+ + quinol. HAMAP MF_01350

Subunit structure

NDH-1 is composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.

Subcellular location

Cell inner membrane; Multi-pass membrane protein HAMAP MF_01350.

Sequence similarities

Belongs to the complex I subunit 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 325325NADH-quinone oxidoreductase subunit H HAMAP MF_01350
PRO_0000117523

Regions

Transmembrane11 – 3121Helical; Potential
Transmembrane81 – 10121Helical; Potential
Transmembrane114 – 13421Helical; Potential
Transmembrane154 – 17421Helical; Potential
Transmembrane186 – 20621Helical; Potential
Transmembrane237 – 25721Helical; Potential
Transmembrane265 – 28521Helical; Potential
Transmembrane304 – 32421Helical; Potential

Experimental info

Sequence conflict35 – 362GE → AK in CAA48367. Ref.1
Sequence conflict531G → A in CAA48367. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0AFD4 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 0648FD831E1B8FB0

FASTA32536,219
        10         20         30         40         50         60 
MSWISPELIE ILLTILKAVV ILLVVVTCGA FMSFGERRLL GLFQNRYGPN RVGWGGSLQL 

        70         80         90        100        110        120 
VADMIKMFFK EDWIPKFSDR VIFTLAPMIA FTSLLLAFAI VPVSPGWVVA DLNIGILFFL 

       130        140        150        160        170        180 
MMAGLAVYAV LFAGWSSNNK YSLLGAMRAS AQTLSYEVFL GLSLMGVVAQ AGSFNMTDIV 

       190        200        210        220        230        240 
NSQAHVWNVI PQFFGFITFA IAGVAVCHRH PFDQPEAEQE LADGYHIEYS GMKFGLFFVG 

       250        260        270        280        290        300 
EYIGIVTISA LMVTLFFGGW QGPLLPPFIW FALKTAFFMM MFILIRASLP RPRYDQVMSF 

       310        320 
GWKICLPLTL INLLVTAAVI LWQAQ 

« Hide

References

« Hide 'large scale' references
[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: 7690854] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / AN387.
[2]"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. expand/collapse author list , 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: 9205837] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"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: 15919996] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68301 Genomic DNA. Translation: CAA48367.1.
U00096 Genomic DNA. Translation: AAC75342.1.
AP009048 Genomic DNA. Translation: BAA16110.1.
PIRH64999.
RefSeqNP_416785.1. NC_000913.2.

3D structure databases

ProteinModelPortalP0AFD4.
ModBaseSearch...

Protein-protein interaction databases

IntActP0AFD4. 1 interaction.

Protein family/group databases

TCDB3.D.1.1.1. H+ or Na+-translocating NADH dehydrogenase (NDH) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000002147; EBESCP00000002147; EBESCG00000001759.
EBESCT00000002148; EBESCP00000002148; EBESCG00000001759.
EBESCT00000017553; EBESCP00000016844; EBESCG00000016609.
GeneID946761.
GenomeReviewsGene locus JW2277 in contig AP009048_GR.
Gene locus b2282 in contig U00096_GR.
KEGGecj:JW2277.
eco:b2282.
PATRIC32119931. VBIEscCol129921_2375.

Organism-specific databases

EchoBASEEB2012.
EcoGeneEG12088. nuoH.

Phylogenomic databases

eggNOGCOG1005.
GeneTreeEBGT00050000009143.
HOGENOMHBG727670.
OMAMSWLTPE.
PhylomeDBP0AFD4.
ProtClustDBPRK06076.

Enzyme and pathway databases

BioCycEcoCyc:NUOH-MONOMER.
MetaCyc:NUOH-MONOMER.

Gene expression databases

GenevestigatorP0AFD4.

Family and domain databases

HAMAPMF_01350. NDH1_NuoH.
[Tree]
InterProIPR001694. NADH_UbQ_OxRdtase_su1/FPO.
IPR018086. NADH_UbQ_OxRdtase_su1_CS.
[Graphical view]
KOK00337.
PANTHERPTHR11432. Resp_NADH_DH_1. 1 hit.
PfamPF00146. NADHdh. 1 hit.
[Graphical view]
PROSITEPS00667. COMPLEX1_ND1_1. 1 hit.
PS00668. COMPLEX1_ND1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUOH_ECOLI
AccessionPrimary (citable) accession number: P0AFD4
Secondary accession number(s): P33603, P78307
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families