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A9L9F3 (NDHH_LEMMI) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 27. 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
OrganismLemna minor (Common duckweed)
Taxonomic identifier4472 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAraceaeLemnoideaeLemna

Protein attributes

Sequence length395 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 – 395395NAD(P)H-quinone oxidoreductase subunit H, chloroplastic HAMAP MF_01358
PRO_0000357999

Sequences

Sequence LengthMass (Da)Tools
A9L9F3 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: AC3ECFD2881DDE4E

FASTA39545,780
        10         20         30         40         50         60 
MTGPTTNTKN DLMIVNMGPQ HPSMHGVLRL IVTLDGEDVI DCEPILGYLH RGMEKIAENR 

        70         80         90        100        110        120 
TIVQYLPYVT RWDYLATMFT EAITVNAPEQ LGNIQVPQRA SYIRVIMLEL SRIASHLLWL 

       130        140        150        160        170        180 
GPFMADIGAQ TPFFYIFRER ELIYDLFEAA TGMRMMHNYF RIGGVAADLP YGWIDKCLDF 

       190        200        210        220        230        240 
CDYFLTGIDE YEKLITRNPI FLERVEGIGI ISGEEAINWG LSGPMLRASG ISWDLRKVDQ 

       250        260        270        280        290        300 
YECYNEFDWE VQWQKEGDSL ARYLVRMSEM RESIKIIQQA LEGIPGGPYE NLEVRRFDKT 

       310        320        330        340        350        360 
KDSEWNDFEY RFISKKPSPN FELSKQELYV RVEAPKGELG IFLIGDQNVF PWRWKIRPPG 

       370        380        390 
FINLQILPQL VKRMKLADIM TILGSIDIIM GEVDR 

« Hide

References

[1]"Complete sequence of the Duckweed (Lemna minor) chloroplast genome: structural organization and phylogenetic relationships to other angiosperms."
Mardanov A.V., Ravin N.V., Kuznetsov B.B., Samigullin T.H., Antonov A.S., Kolganova T.V., Skyabin K.G.
J. Mol. Evol. 66:555-564(2008) [PubMed: 18463914] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ400350 Genomic DNA. Translation: ABD48552.1.
RefSeqYP_001595565.1. NC_010109.1.

3D structure databases

ProteinModelPortalA9L9F3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5787523.

Phylogenomic databases

ProtClustDBCHL00017.

Family and domain databases

HAMAPMF_01358. NDH1_NuoD.
[Tree]
InterProIPR001135. NADH_Q_OxRdtase_suD.
IPR014029. NADH_UbQ_OxRdtase_49kDa_CS.
IPR022885. NDH1_su_D/H.
[Graphical view]
PfamPF00346. Complex1_49kDa. 1 hit.
[Graphical view]
PROSITEPS00535. COMPLEX1_49K. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNDHH_LEMMI
AccessionPrimary (citable) accession number: A9L9F3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: February 5, 2008
Last modified: September 21, 2011
This is version 27 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