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Q9PGI8 (NUOH_XYLFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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
Synonyms:nqo8
Ordered Locus Names:XF_0312
OrganismXylella fastidiosa [Complete proteome] [HAMAP]
Taxonomic identifier2371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

Protein attributes

Sequence length363 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.

Sequence caution

The sequence AAF83123.1 differs from that shown. Reason: Erroneous initiation.

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 – 363363NADH-quinone oxidoreductase subunit H HAMAP MF_01350
PRO_0000244966

Regions

Transmembrane62 – 8221Helical; Potential
Transmembrane94 – 11421Helical; Potential
Transmembrane127 – 14721Helical; Potential
Transmembrane166 – 18621Helical; Potential
Transmembrane202 – 22221Helical; Potential
Transmembrane239 – 25719Helical; Potential
Transmembrane264 – 28623Helical; Potential
Transmembrane293 – 31321Helical; Potential
Transmembrane339 – 35921Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q9PGI8 [UniParc].

Last modified July 11, 2006. Version 2.
Checksum: A6DAC053D9B9B6B8

FASTA36340,558
        10         20         30         40         50         60 
MNTWFLNVVD PLHQWFLGFG DIGVVLWTVL KILMIAIPLI VSVAFYVVWE RKLIGWMHVR 

        70         80         90        100        110        120 
HGPMYVGMGL FQAFADVFKL LFKEVLYPSK AHKAIFVIAP LLTLAPSFAA WAVVPFDTKL 

       130        140        150        160        170        180 
VLSNANVGLL YLLAMTSLGV YGIILAGWAS NSKYAFLGAM RSAAQVVSYE IAMGFALVGV 

       190        200        210        220        230        240 
MIAAGSLNLS QIVMAQAGSS GFFDWFLIPL FPLFIVYWVS GVAETNRSPF DVVEGESEIV 

       250        260        270        280        290        300 
AGHMVEYSGS VFALFFLAEY ANMILVSFLI SIFFLGGWLS PIQGWVSGQV SPLIDWVWNG 

       310        320        330        340        350        360 
GWPWLLFKVL FFASAYIWFR ASFPRYRYDQ IMRLGWKVFI PLTIVWIAVT ALMVFSGVIQ 


KGV

« Hide

References

[1]"The genome sequence of the plant pathogen Xylella fastidiosa."
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. expand/collapse author list , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
Nature 406:151-159(2000) [PubMed: 10910347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9a5c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003849 Genomic DNA. Translation: AAF83123.1. Different initiation.
PIRB82822.
RefSeqNP_297603.2. NC_002488.3.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1125840.
GenomeReviewsGene locus XF_0312 in contig AE003849_GR.
KEGGxfa:XF0312.
NMPDRfig|160492.1.peg.310.
PATRIC24130587. VBIXylFas578_0340.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG727670.
OMAYLWVRAT.
ProtClustDBPRK06076.

Enzyme and pathway databases

BioCycXFAS160492:XF0312-MONOMER.

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_XYLFA
AccessionPrimary (citable) accession number: Q9PGI8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 11, 2006
Last modified: January 25, 2012
This is version 69 of the entry and version 2 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

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