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Reviewed, UniProtKB/Swiss-Prot A2T388 (NU1C_ANGEV)

Last modified June 16, 2009. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
OrganismAngiopteris evecta (Mule's foot fern) (Giant fern)
Taxonomic identifier13825 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaMoniliformopsesFilicophytaMarattiopsidaMarattialesMarattiaceaeAngiopteris

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Sequence similarities

Belongs to the complex I subunit 1 family.

Ontologies

Keywords
   Cellular componentChloroplast
Membrane
Plastid
Thylakoid
   DomainTransmembrane
   LigandNAD
NADP
Plastoquinone
   Molecular functionOxidoreductase
   PTMQuinone
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: HAMAP

   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 – 369369NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic HAMAP MF_01350
PRO_0000298864

Regions

Transmembrane29 – 4921 Potential
Transmembrane97 – 11721 Potential
Transmembrane129 – 14921 Potential
Transmembrane167 – 18721 Potential
Transmembrane205 – 22521 Potential
Transmembrane255 – 27521 Potential
Transmembrane305 – 32521 Potential
Transmembrane348 – 36821 Potential

Sequences

Sequence LengthMass (Da)Tools
A2T388-1 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: CEED504F2B4792FF

FASTA36940,604
        10         20         30         40         50         60 
MVLDITGVEK QGIILFSESE LSKEFLELIW IIVSILTTIV GVTLGVLVIV WLERKISAGI 

        70         80         90        100        110        120 
QQRIGPEYAG PLGIIQALAD GIKLLLKEDV IPARGDIWLF NVGPAIVVIP VFLSYLVIPF 

       130        140        150        160        170        180 
GKHIILADLG IGVFFWIAVS SIAPLGLLMA GYGSNNKYSF LGGLRAAAQS ISYEIPLALC 

       190        200        210        220        230        240 
VLSISLLSNS LSTVDIVDAQ SKYGLLGWNL WRQPIGFLIF FISSLAECER LPFDPPEAEE 

       250        260        270        280        290        300 
ELVAGYQTEY SGIKFGLFYV GSYLNLLVSS LFVTVLYLGG WDLSIPFLPT SNQLTWILTN 

       310        320        330        340        350        360 
GTFDIINAII GIIITLTKAY LFLFVSIMTR WTLPRVRIDQ LLDLGWKFLL PVALGNLLLT 


ASFQILLLD 

« Hide

References

[1]"The complete plastid genome sequence of Angiopteris evecta (G. Forst.) Hoffm. (Marattiaceae)."
Roper J.M., Hansen S.K., Wolf P.G., Karol K.G., Mandoli D.F., Everett K.D.E., Kuehl J.V., Boore J.L.
Am. Fern J. 97:95-106(2007)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

DQ821119 Genomic DNA. Translation: ABG79655.1.
RefSeqYP_001023756.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4788147.

Family and domain databases

HAMAPMF_01350.
[Tree]
InterProIPR001694. NADH_UbQ_OxRdtase_su1.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNU1C_ANGEV
AccessionPrimary (citable) accession number: A2T388
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: March 6, 2007
Last modified: June 16, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents