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Q9PGJ2 (NUOD_XYLFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 71. 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 D
EC=1.6.99.5
Alternative name(s):
NADH dehydrogenase I subunit D
NDH-1 subunit D
Gene names
Name:nuoD
Ordered Locus Names:XF_0308
OrganismXylella fastidiosa [Complete proteome] [HAMAP]
Taxonomic identifier2371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

Protein attributes

Sequence length435 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 By similarity. HAMAP MF_01358

Catalytic activity

NADH + quinone = NAD+ + quinol. HAMAP MF_01358

Subunit structure

NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex By similarity.

Subcellular location

Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP MF_01358.

Sequence similarities

Belongs to the complex I 49 kDa subunit family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell inner membrane
Cell membrane
Membrane
   LigandNAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMQuinone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtransport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

NADH 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 – 435435NADH-quinone oxidoreductase subunit D HAMAP MF_01358
PRO_0000371953

Sequences

Sequence LengthMass (Da)Tools
Q9PGJ2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1CF6B142B2248AEB

FASTA43549,391
        10         20         30         40         50         60 
MNQIRQAPAT SASNATESKQ EIRNYTMNFG PQHPAAHGVL RLILEMDGET VVRADPHIGL 

        70         80         90        100        110        120 
LHRGTEKLAE SKPFNQSIGY MDRLDYVSMM CNEHAYVRAI ETLIGIQAPE RAQYIRTMFD 

       130        140        150        160        170        180 
EITRILNHLM WLGSNALDLG AMAVMLYAFR EREELMDVYE AISGARMHAA YYRPGGVYRD 

       190        200        210        220        230        240 
LPDTMPKYKQ SRWHKGKALK RLNAAREGSM LDFLEHFADT FPQRIDEYET LLTDNRIWKQ 

       250        260        270        280        290        300 
RTVGVGVIEP DVAKAWGMTG VMLRGSGVAW DLRKKQPYAK YDAVDFDIPL GTCGDCYDRY 

       310        320        330        340        350        360 
LCRVAEMRES NRIIKQCVQW LKVNPGQVMV ENFKVAPPKR ESMKDDMEAL IHHFKLFSEG 

       370        380        390        400        410        420 
YCVPAGETYS AVEAPKGEFG CYLISDGANK PFRVHLRAPG FAHLSSMDAV VRGYMLADVV 

       430 
AMIGTYDLVF GEVDR

« 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: AAF83119.1.
PIRF82821.
RefSeqNP_297599.1. NC_002488.3.

3D structure databases

HSSPHSSP built from PDB template 2FUG based on UniProtKB Q56220.
ProteinModelPortalQ9PGJ2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1125836.
GenomeReviewsGene locus XF_0308 in contig AE003849_GR.
KEGGxfa:XF0308.
NMPDRfig|160492.1.peg.306.
PATRIC24130579. VBIXylFas578_0336.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG459705.
OMAMADVITI.
ProtClustDBPRK06075.

Enzyme and pathway databases

BioCycXFAS160492:XF0308-MONOMER.

Family and domain databases

HAMAPMF_01358. NDH1_NuoD.
[Tree]
InterProIPR010219. NADH_DH_1_suD.
IPR001135. NADH_Q_OxRdtase_suD.
IPR014029. NADH_UbQ_OxRdtase_49kDa_CS.
IPR022885. NDH1_su_D/H.
[Graphical view]
KOK00333.
PfamPF00346. Complex1_49kDa. 2 hits.
[Graphical view]
TIGRFAMsTIGR01962. NuoD. 1 hit.
PROSITEPS00535. COMPLEX1_49K. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUOD_XYLFA
AccessionPrimary (citable) accession number: Q9PGJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 71 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

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