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Reviewed, UniProtKB/Swiss-Prot Q3V4X9 (NU1C_ACOCL)

Last modified June 16, 2009. Version 21. 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
OrganismAcorus calamus (Sweet flag)
Taxonomic identifier4465 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAcoraceaeAcorus

Protein attributes

Sequence length365 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 – 365365NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic HAMAP MF_01350
PRO_0000240014

Regions

Transmembrane29 – 4921 Potential
Transmembrane106 – 12621 Potential
Transmembrane129 – 14921 Potential
Transmembrane250 – 27021 Potential
Transmembrane302 – 32221 Potential
Transmembrane338 – 35821 Potential

Sequences

Sequence LengthMass (Da)Tools
Q3V4X9-1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 4D4EAF4C235A69AE

FASTA36540,097
        10         20         30         40         50         60 
MIIATTEIQA INSFSRSESL SLKEVYGLIW LLVPIFTLIL VIIIGVLVIV WLEREISAGI 

        70         80         90        100        110        120 
QQRIGPEYAG PLGILQALAD GTKLLFKEDL LPSRGDISLF SLGPSIAVIS TLLSYLVIPF 

       130        140        150        160        170        180 
GYHLVLADLS IGVFLWIAIS SIAPIGLLMS GYGSNNKYSF SGGLRAAAQS ISYEIPLTLC 

       190        200        210        220        230        240 
VLSISLLSNS SSTVDIVEAQ SKYGFWGWNL WRQPIGFLVF LVSSLAECER LPFDLPEAEE 

       250        260        270        280        290        300 
ELVAGYQTEY SGIKFGLFYV ASYLNLLVSS LFVTVLYLGG WNLSIPYIFI PELFGKNKTG 

       310        320        330        340        350        360 
GIFGMTIGIL ITLAKAYLFL FISIATRWTL PRLRIDQLLN LGWKFLLPIS LGNLLLTTSS 


QLVSL 

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References

[1]"Analysis of Acorus calamus chloroplast genome and its phylogenetic implications."
Goremykin V.V., Holland B., Hirsch-Ernst K.I., Hellwig F.H.
Mol. Biol. Evol. 22:1813-1822(2005) [PubMed: 15930156] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AJ879453 Genomic DNA. Translation: CAI53849.1.
RefSeqYP_319818.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3677516.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNU1C_ACOCL
AccessionPrimary (citable) accession number: Q3V4X9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: October 11, 2005
Last modified: June 16, 2009
This is version 21 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