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Q98KR3 (NUOH_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Gene names
Name:nuoH
Ordered Locus Names:mll1361
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP MF_01350

Catalytic activity

NADH + quinone = NAD+ + quinol. HAMAP MF_01350

Subunit structure

NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity.

Subcellular location

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

Sequence similarities

Belongs to the complex I subunit 1 family.

Ontologies

Keywords
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandNAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMQuinone
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADH dehydrogenase (quinone) activity

Inferred from electronic annotation. Source: EC

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347NADH-quinone oxidoreductase subunit H HAMAP MF_01350
PRO_0000244937

Regions

Transmembrane13 – 3321Helical; Potential
Transmembrane82 – 10221Helical; Potential
Transmembrane115 – 13521Helical; Potential
Transmembrane161 – 18121Helical; Potential
Transmembrane198 – 21821Helical; Potential
Transmembrane248 – 26821Helical; Potential
Transmembrane283 – 30321Helical; Potential
Transmembrane321 – 34121Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q98KR3 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 1092F351BD97EC57

FASTA34738,371
        10         20         30         40         50         60 
MDTFFSFYVL PALLILLKSV VLIVVLLIFV AYILYADRKI WAAVQLRRGP NVVGPWGTLQ 

        70         80         90        100        110        120 
AFADLLKFVF KEPVIPSGAN KGVFLLAPLV SAVLAISAWA VIPVNQGWAI ANVNVGILYV 

       130        140        150        160        170        180 
FAISSLEVYG VIMGGWASNS KYPFLGALRS AAQMVSYEVS IGFVIVTVLL TAGSLNLSDI 

       190        200        210        220        230        240 
VLSQHDGIGT RLGLPNTFLD WNWLALFPMF IIFFISALAE TNRPPFDLVE AESELVAGHM 

       250        260        270        280        290        300 
VEYSSTPFLL FFLGEYVAIV LMCALATILF LGGWLPPFDF VPFTWVPGVI WFVLKVCFVF 

       310        320        330        340 
FGISMVKAFV PRYRYDQLMR LGWKVFLPIS LFMVVATAAF LKITGFA 

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References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB48751.1.
RefSeqNP_102965.1. NC_002678.2.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1225628.
GenomeReviewsGene locus mll1361 in contig BA000012_GR.
KEGGmlo:mll1361.
NMPDRfig|266835.1.peg.1070.
PATRIC22476370. VBIMesLot2464_1096.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG727670.
OMAAGFMVEY.
ProtClustDBPRK06076.

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. False negative.
PS00668. COMPLEX1_ND1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUOH_RHILO
AccessionPrimary (citable) accession number: Q98KR3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 1, 2001
Last modified: January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families