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A1EA64 (NU1C_AGRST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismAgrostis stolonifera (Creeping bentgrass)
Taxonomic identifier63632 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaePoeaeAgrostidinaeAgrostis

Protein attributes

Sequence length362 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 – 362362NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic HAMAP MF_01350
PRO_0000275575

Regions

Transmembrane29 – 4921Helical; Potential
Transmembrane103 – 12321Helical; Potential
Transmembrane128 – 14821Helical; Potential
Transmembrane164 – 18421Helical; Potential
Transmembrane202 – 22221Helical; Potential
Transmembrane247 – 26721Helical; Potential
Transmembrane303 – 32321Helical; Potential
Transmembrane335 – 35521Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
A1EA64 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: E6A0CA94AAC8F60D

FASTA36240,211
        10         20         30         40         50         60 
MIIDRVEVET INSFSKLELL KEVYGLISIL PILTLLLGIT IEVLVIVWLE REISASIQQR 

        70         80         90        100        110        120 
IGPEYAGPLG LLQAIADGTK LLLKEDILPS RGDIPLFSIG PSIAVISILL SFLVIPLGYH 

       130        140        150        160        170        180 
FVLADLSIGV FLWIAISSIA PIGLLMAGYS SNNKYSFLGG LRAAAQSISY EIPLTFCVLA 

       190        200        210        220        230        240 
ISLLSNSSST VDIVEAQSKY GFFGWNIWRQ PIGFLVFLIS SLAECERLPF DLPEAEEELV 

       250        260        270        280        290        300 
AGYQTEYSGI KYGLFYLVSY LNLLVSSLFV TVLYLGGWNL SIPYISFFDF FQMNNAVGIL 

       310        320        330        340        350        360 
EMTIGIFITL TKAYLFLFIS ITIRWTLPRM RMDQLLNLGW KFLLPISLGN LLLTTSSQLV 


SL 

« Hide

References

[1]"Complete chloroplast genome sequences of Hordeum vulgare, Sorghum bicolor and Agrostis stolonifera, and comparative analyses with other grass genomes."
Saski C., Lee S.-B., Fjellheim S., Guda C., Jansen R.K., Luo H., Tomkins J., Rognli O.A., Daniell H., Clarke J.L.
Theor. Appl. Genet. 115:571-590(2007) [PubMed: 17534593] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Penn A-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF115543 Genomic DNA. Translation: ABK79636.1.
RefSeqYP_874792.1. NC_008591.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4525041.

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_AGRST
AccessionPrimary (citable) accession number: A1EA64
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: January 23, 2007
Last modified: June 28, 2011
This is version 23 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