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B8HSZ5 (ACCA_CYAP4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. 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:Cyan7425_0400
OrganismCyanothece sp. (strain PCC 7425 / ATCC 29141) [Complete proteome] [HAMAP]
Taxonomic identifier395961 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesCyanothece

Protein attributes

Sequence length325 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 – 325325Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_1000148738

Sequences

Sequence LengthMass (Da)Tools
B8HSZ5 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: F11E3F511D3E370D

FASTA32535,821
        10         20         30         40         50         60 
MATERKPILL EFEKPLAELE AQINQVRQKS AELGVDVSDQ IRELENNSTQ LRQEIFSKLT 

        70         80         90        100        110        120 
PSQKLQLARH PRRPSTLDYI QAISDEWMEL HGDRYGSDDP AIVAGVARLA GQPVVMLGQQ 

       130        140        150        160        170        180 
KGRDTKDNVA RNFGMASPSG YRKAIRIMEH ADRFGMPILT FIDTPAAWAG IEAEQYGQGE 

       190        200        210        220        230        240 
AIAYNLREMF RLEVPIICTV IGEGGSGGAL GIGVGDRLLM FEHAIYSVAP PEACAAILWR 

       250        260        270        280        290        300 
DAQKAPLAAE ALKITAADLQ KLGLIDEILP EPLGGAHVDP VGATEILKTS LIAHLRQLSQ 

       310        320 
MSSPQRRELR YQKFRRMGIF TQSAA 

« Hide

References

[1]"Complete sequence of chromosome Cyanothece sp. PCC 7425."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L., Sato H., Zhao L., Sherman L., Pakrasi H.B., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7425 / ATCC 29141.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001344 Genomic DNA. Translation: ACL42792.1.
RefSeqYP_002481153.1. NC_011884.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB8HSZ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7286307.
GenomeReviewsGene locus Cyan7425_0400 in contig CP001344_GR.
KEGGcyn:Cyan7425_0400.
PATRIC21561705. VBICyaSp30657_0389.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG286557.
OMAGRDTKDN.
PhylomeDBB8HSZ5.
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_CYAP4
AccessionPrimary (citable) accession number: B8HSZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: January 25, 2012
This is version 26 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