Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q3M9K9 (NU1C_ANAVT)

Last modified June 16, 2009. Version 29. 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
    EC=1.6.5.-
Alternative name(s):
    NAD(P)H dehydrogenase I subunit 1
    NDH-1 subunit 1
    NDH-A
Gene names
Name: ndhA
Ordered Locus Names: Ava_2714
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic 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-1 is composed of at least 11 different subunits By similarity.

Subcellular location

Cellular thylakoid membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the complex I subunit 1 family.

Ontologies

Keywords
   Cellular componentMembrane
Thylakoid
   DomainTransmembrane
   LigandNAD
NADP
Plastoquinone
   Molecular functionOxidoreductase
   PTMQuinone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: HAMAP

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 372372NAD(P)H-quinone oxidoreductase subunit 1 HAMAP MF_01350
PRO_0000240035

Regions

Transmembrane27 – 4721 Potential
Transmembrane65 – 8521 Potential
Transmembrane97 – 11721 Potential
Transmembrane128 – 14821 Potential
Transmembrane166 – 18621 Potential
Transmembrane204 – 22421 Potential
Transmembrane266 – 28621 Potential
Transmembrane308 – 32821 Potential
Transmembrane347 – 36721 Potential

Sequences

Sequence LengthMass (Da)Tools
Q3M9K9-1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: C66CF9A01C7D60C5

FASTA37240,262
        10         20         30         40         50         60 
MNSGIDLQGT FIKSLMDLGI PPGTAKAIWM PLPMILMLIG ATVGVLVCVW LERKISAAAQ 

        70         80         90        100        110        120 
QRIGPEYIGP LGLLAPVADG LKLVFKEDIV PAQADPWLFT LGPILVVLPV FLSYLIVPFG 

       130        140        150        160        170        180 
QNIVITNIGT GIFLWIALSS IQPIGLLMAG YSSNNKYSLL GGLRAAAQSI SYEIPLALSV 

       190        200        210        220        230        240 
LAIVMMSNSL STVDIVNQQS GYGILGWNIW RQPLGFLIFW IAALAECERL PFDLPEAEEE 

       250        260        270        280        290        300 
LVAGYQTEYS GMKFALFYLS SYVNLVLSAL LVAVLYLGGW DFPIPINVLA NLVGVSEANP 

       310        320        330        340        350        360 
VLQVVSAALG ITMTLVKAYF LVFIAILLRW TVPRVRIDQL LDLGWKFLLP VGLVNLLLTA 

       370 
ALKLAFPVAF GG 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000117 Genomic DNA. Translation: ABA22327.1.
RefSeqYP_323222.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3682212.
GenomeReviewsGene locus Ava_2714 in contig CP000117_GR.
KEGGava:Ava_2714.
NMPDRfig|240292.3.peg.1051.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3M9K9.
OMAQ3M9K9. FGGWLGP.

Enzyme and pathway databases

BioCycAVAR240292:AVA_2714-MON.

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_ANAVT
AccessionPrimary (citable) accession number: Q3M9K9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: October 25, 2005
Last modified: June 16, 2009
This is version 29 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