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Q1ACE3 (NDHH_CHAVU) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
NAD(P)H-quinone oxidoreductase subunit H, chloroplastic

EC=1.6.5.-
Alternative name(s):
NAD(P)H dehydrogenase subunit H
NADH-plastoquinone oxidoreductase 49 kDa subunit
NADH-plastoquinone oxidoreductase subunit H
Gene names
Name:ndhH
Encoded onPlastid; Chloroplast
OrganismChara vulgaris (Common stonewort)
Taxonomic identifier55564 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaCharophyceaeCharalesCharaceaeChara

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient By similarity. HAMAP MF_01358

Catalytic activity

NAD(P)H + plastoquinone = NAD(P)+ + plastoquinol. HAMAP MF_01358

Subunit structure

NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus By similarity.

Subcellular location

Plastidchloroplast thylakoid membrane; Peripheral membrane protein; Stromal side By similarity HAMAP MF_01358.

Sequence similarities

Belongs to the complex I 49 kDa subunit family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentChloroplast
Membrane
Plastid
Thylakoid
   LigandNAD
NADP
Plastoquinone
   Molecular functionOxidoreductase
   PTMQuinone
Gene Ontology (GO)
   Biological processtransport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity, acting on NADH or NADPH

Inferred from electronic annotation. Source: InterPro

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391NAD(P)H-quinone oxidoreductase subunit H, chloroplastic HAMAP MF_01358
PRO_0000357974

Sequences

Sequence LengthMass (Da)Tools
Q1ACE3 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 96DF816AB25324BD

FASTA39145,306
        10         20         30         40         50         60 
MLIRKTNSMI VSMGPHHPSM HGVLRLIITL DGENVIDCEP VLGYLHRGME KIAENRTIIQ 

        70         80         90        100        110        120 
YLPYVTRWDY LATMFTEAIT INAPEKLANI QVPKRASYIR VIMLELSRIA SHLLWLGPFM 

       130        140        150        160        170        180 
ADIGAQTPFF YILREREMIY DLFESATGMR MMHNYFRIGG VAVDLPYGWI DKCLDFCEYF 

       190        200        210        220        230        240 
LPKVNEYENL ITQNPIFLKR VEGIGVINKE EAINWGLSGP MLRASGMEWD LRKVDHYECY 

       250        260        270        280        290        300 
DELDWSVQWE KRGDCLARYI VRVGEMRESV KIIQQALKAI PGGPYENLEA RKLNTKKSTQ 

       310        320        330        340        350        360 
WNDFEYQFIS KKSSPTFKIP KQEHYVRLEA SKGELGIFLI GDDNIFPWRW KIRPPGFINL 

       370        380        390 
QVLPPLVNGM KLADIMTILG SIDIIMGEVD R 

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References

[1]"The chloroplast genome sequence of Chara vulgaris sheds new light into the closest green algal relatives of land plants."
Turmel M., Otis C., Lemieux C.
Mol. Biol. Evol. 23:1324-1338(2006) [PubMed: 16611644] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ229107 Genomic DNA. Translation: ABA61910.1.
RefSeqYP_635804.1. NC_008097.1.

3D structure databases

ProteinModelPortalQ1ACE3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4100280.

Phylogenomic databases

ProtClustDBCHL00017.

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]
PfamPF00346. Complex1_49kDa. 1 hit.
[Graphical view]
TIGRFAMsTIGR01962. NuoD. 1 hit.
PROSITEPS00535. COMPLEX1_49K. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNDHH_CHAVU
AccessionPrimary (citable) accession number: Q1ACE3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 11, 2006
Last modified: September 21, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families