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A1XG10 (NU1C_NUPAD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 28. 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 1, chloroplastic

EC=1.6.5.-
Alternative name(s):
NAD(P)H dehydrogenase subunit 1
Short name=NDH subunit 1
NADH-plastoquinone oxidoreductase subunit 1
Gene names
Name:ndhA
Encoded onPlastid; Chloroplast
OrganismNuphar advena (Common spatterdock) (Nuphar lutea subsp. advena)
Taxonomic identifier77108 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytabasal MagnoliophytaNymphaealesNymphaeaceaeNuphar

Protein attributes

Sequence length361 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_01350

Catalytic activity

NAD(P)H + plastoquinone = NAD(P)+ + plastoquinol. HAMAP MF_01350

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; Multi-pass membrane protein By similarity HAMAP MF_01350.

Sequence similarities

Belongs to the complex I subunit 1 family.

Ontologies

Keywords
   Cellular componentChloroplast
Membrane
Plastid
Thylakoid
   DomainTransmembrane
Transmembrane helix
   LigandNAD
NADP
Plastoquinone
   Molecular functionOxidoreductase
   PTMQuinone
Gene Ontology (GO)
   Cellular componentchloroplast thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic HAMAP MF_01350
PRO_0000298876

Regions

Transmembrane25 – 4521Helical; Potential
Transmembrane102 – 12221Helical; Potential
Transmembrane125 – 14521Helical; Potential
Transmembrane251 – 27121Helical; Potential
Transmembrane298 – 31821Helical; Potential
Transmembrane334 – 35421Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
A1XG10 [UniParc].

Last modified February 20, 2007. Version 2.
Checksum: 9182FA4204DA5DC8

FASTA36139,751
        10         20         30         40         50         60 
MIIEEAQAIN SFFRSESSKE VYGLIWLLVP ILTLVLGITI GVLVIVWLER KISAGIQRRI 

        70         80         90        100        110        120 
GPEYAGPLGI LQALADGVKL LFKEDLLPSR GDIRLFSVGP SIAVVSILLS YSVIPFGHHL 

       130        140        150        160        170        180 
VLTDLSIGVS LWIAISSIAP IGLLMSGYGS NNKYSFSGGL RAAAQSISYE IPLTPCVLSI 

       190        200        210        220        230        240 
SLLSNSSSTV DIVEAQSKYG FWGWNLWRQP IGFIVFIISS LAECERLPFD LPEAEEELVA 

       250        260        270        280        290        300 
GYQTEYSGIK FGLFYVASYL NLLVSSLFVT ILYLGGWNLS IPYIPITELF EKNQTSEVFG 

       310        320        330        340        350        360 
TTISLLITLA KAYLFLFIPI STRWTLPRMR MDQLLNLGWK SLLPIALGNL LLTTSSQLVS 


L 

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References

[1]"Comparative chloroplast genomics: analyses including new sequences from the angiosperms Nuphar advena and Ranunculus macranthus."
Raubeson L.A., Peery R., Chumley T.W., Dziubek C., Fourcade H.M., Boore J.L., Jansen R.K.
BMC Genomics 8:174-174(2007) [PubMed: 17573971] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ354691 Genomic DNA. Translation: ABC60514.2.
RefSeqYP_001001589.2. NC_008788.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4699613.

Phylogenomic databases

ProtClustDBCHL00032.

Family and domain databases

HAMAPMF_01350. NDH1_NuoH.
[Tree]
InterProIPR001694. NADH_UbQ_OxRdtase_su1/FPO.
IPR018086. NADH_UbQ_OxRdtase_su1_CS.
[Graphical view]
PANTHERPTHR11432. Resp_NADH_DH_1. 1 hit.
PfamPF00146. NADHdh. 1 hit.
[Graphical view]
PROSITEPS00667. COMPLEX1_ND1_1. 1 hit.
PS00668. COMPLEX1_ND1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNU1C_NUPAD
AccessionPrimary (citable) accession number: A1XG10
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: February 20, 2007
Last modified: June 28, 2011
This is version 28 of the entry and version 2 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