Skip Header

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

Q3ALN0 (ACCA_SYNSC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:Syncc9605_0730
OrganismSynechococcus sp. (strain CC9605) [Complete proteome] [HAMAP]
Taxonomic identifier110662 [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_1000062693

Sequences

Sequence LengthMass (Da)Tools
Q3ALN0 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 8D2865F2C6E8BD3D

FASTA32936,497
        10         20         30         40         50         60 
MPRRPLLEFE KPLVELEQQI EQIRQLARDS EVDVSQQLQQ LESLAARRRQ EIFQGLTPAQ 

        70         80         90        100        110        120 
KIQVARHPQR PSTLDFIQMF CDDWVELHGD RRGNDDQALI GGVGRVGNRA VMLIGHQKGR 

       130        140        150        160        170        180 
DTKENVARNF GMAAPGGYRK AMRLMDHADR FRLPILTFID TPGAYAGLEA EEQGQGEAIA 

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

       250        260        270        280        290        300 
KAPDAAAALR ITGRDLLELG VVDEVLEEPS GGNNWAPLEA GENLRAAIER HLEQLLSLSE 

       310        320 
QQLREARYSK FRAMGRFLEK TSQDVDKAA 

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9605."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9605.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000110 Genomic DNA. Translation: ABB34502.1.
RefSeqYP_381057.1. NC_007516.1.

3D structure databases

ProteinModelPortalQ3ALN0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3ALN0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3735352.
GenomeReviewsGene locus Syncc9605_0730 in contig CP000110_GR.
KEGGsyd:Syncc9605_0730.
NMPDRfig|110662.3.peg.1897.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0825.
HOGENOMHBG286557.
OMAGRDTKDN.
PhylomeDBQ3ALN0.
ProtClustDBPRK05724.

Enzyme and pathway databases

BioCycSSP1131:SYNCC9605_0730-MONOMER.

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_SYNSC
AccessionPrimary (citable) accession number: Q3ALN0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 44 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