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Q0I8N1 (ACCA_SYNS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha

Short name=ACCase subunit alpha
Short name=Acetyl-CoA carboxylase carboxyltransferase subunit alpha
EC=6.4.1.2
Gene names
Name:accA
Ordered Locus Names:sync_1988
OrganismSynechococcus sp. (strain CC9311) [Complete proteome] [HAMAP]
Taxonomic identifier64471 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechococcus

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA By similarity. HAMAP MF_00823

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP MF_00823

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP MF_00823

Subunit structure

Acetyl-CoA carboxylase is an heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD) By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_00823.

Sequence similarities

Belongs to the AccA family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentacetyl-CoA carboxylase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetyl-CoA carboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_1000062691

Sequences

Sequence LengthMass (Da)Tools
Q0I8N1 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 9BE4EDEFC543F1FA

FASTA32936,197
        10         20         30         40         50         60 
MARRPLLEFE KPLIELEQQI EQIRQLARDS EVDVSQQLLQ LETLAARRRE EIFQNLTPAQ 

        70         80         90        100        110        120 
KIQVARHPHR PSTLDFIQMF CDDWVELHGD RRGSDDQALV GGLGRIGDRS VVLLGHQKGR 

       130        140        150        160        170        180 
DTKENVARNF GMATPGGYRK ALRLMEHADR FGLPIFAFID TPGAYAGLLA EEQGQGEAIA 

       190        200        210        220        230        240 
VNLREMFRLR VPIIATVIGE GGSGGALGIG VADRLLMFEH SVYTVASPEA CASILWRDAA 

       250        260        270        280        290        300 
KAPEAAAALR ITGKDLLSLG VVDEVLAEPS GGNNWAPLEA GATLREALER NLSELLALPP 

       310        320 
QELRDQRYRK FRAMGRFIDQ ASSDADSAS 

« Hide

References

[1]"Genome sequence of Synechococcus CC9311: insights into adaptation to a coastal environment."
Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H., Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S., Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R., Paulsen I.T.
Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006) [PubMed: 16938853] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000435 Genomic DNA. Translation: ABI45895.1.
RefSeqYP_731191.1. NC_008319.1.

3D structure databases

ProteinModelPortalQ0I8N1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0I8N1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4260858.
GenomeReviewsGene locus sync_1988 in contig CP000435_GR.
KEGGsyg:sync_1988.
PATRIC23795044. VBISynSp88089_2077.
TIGRsync_1988.

Phylogenomic databases

eggNOGCOG0825.
HOGENOMHBG286557.
OMAGRDTKDN.
PhylomeDBQ0I8N1.
ProtClustDBPRK05724.

Family and domain databases

HAMAPMF_00823. AcetylCoA_CT_alpha.
[Tree]
InterProIPR001095. Acetyl_CoA_COase_a_su.
IPR011763. COA_CT_C.
[Graphical view]
KOK01962.
PANTHERPTHR22855:SF3. Ac-CoA_carboxylA. 1 hit.
PfamPF03255. ACCA. 1 hit.
[Graphical view]
PRINTSPR01069. ACCCTRFRASEA.
TIGRFAMsTIGR00513. AccA. 1 hit.
PROSITEPS50989. COA_CT_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACCA_SYNS3
AccessionPrimary (citable) accession number: Q0I8N1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 3, 2006
Last modified: January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families