Skip Header

Contribute Send feedback
Read comments (?) or add your own

B1NWK5 (NDHH_MANES) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 25. 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
OrganismManihot esculenta (Cassava) (Jatropha manihot)
Taxonomic identifier3983 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeManihoteaeManihot

Protein attributes

Sequence length393 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 – 393393NAD(P)H-quinone oxidoreductase subunit H, chloroplastic HAMAP MF_01358
PRO_0000358004

Sequences

Sequence LengthMass (Da)Tools
B1NWK5 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 185AB2B5F5B4D16D

FASTA39345,492
        10         20         30         40         50         60 
MNVPATRKDL MIVNMGPHHP SMHGVLRLIV TLDGEDVIDC EPILGYLHRG MEKIAENRTI 

        70         80         90        100        110        120 
IQYLPYVTRW DYLATMFTEA ITVNGPELLG NIQVPKRAGY IRVIMLELSR IASHLLWLGP 

       130        140        150        160        170        180 
FMADIGAQTP FFYIFREREL VYDLFEAATG MRMMHNFFRI GGVASDLPHG WIDKCLDFCD 

       190        200        210        220        230        240 
YFLTGVTEYQ KLITRNPIFL ERVEGVGIVG TEEAINWGLS GPMLRASGVQ WDLRKVDHYE 

       250        260        270        280        290        300 
CYDEFDWEIQ WQKEGDSLAR YLVRIGEMLE SIKIIQQALE GIPGGPYENL ETRRFDRERD 

       310        320        330        340        350        360 
SEWNDFEYRF ISKKTSPTFE LPKQELYVRV EAPKGELGIF LIGDQSGFPW RWKIRPPGFI 

       370        380        390 
NLQILPELVK RMKLADIMTI LGSIDIIMGE VDR 

« Hide

References

[1]"The complete nucleotide sequence of the cassava (Manihot esculenta) chloroplast genome and the evolution of atpF in Malpighiales: RNA editing and multiple losses of a group II intron."
Daniell H., Wurdack K.J., Kanagaraj A., Lee S.-B., Saski C., Jansen R.K.
Theor. Appl. Genet. 116:723-737(2008) [PubMed: 18214421] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. TME3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU117376 Genomic DNA. Translation: ABV66209.1.
RefSeqYP_001718492.1. NC_010433.1.

3D structure databases

ProteinModelPortalB1NWK5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5999966.

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_MANES
AccessionPrimary (citable) accession number: B1NWK5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 29, 2008
Last modified: September 21, 2011
This is version 25 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