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P74638 (ACCA_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:sll0728
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechocystis

Protein attributes

Sequence length326 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
Reference 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 – 326326Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_0000146783

Sequences

Sequence LengthMass (Da)Tools
P74638 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 9683F4A8C1D391E6

FASTA32636,042
        10         20         30         40         50         60 
MSKSERRVFL LDFEKPLYEL EEKINQIREL AEEKNVDVSE QLSQLESRAE QLRQEIFSNL 

        70         80         90        100        110        120 
NPSQRLQLAR HPRRPSTLDY IQAIADDWFE MHGDRGGYDD PALVGGVARL GTRPVVIMGH 

       130        140        150        160        170        180 
QKGRDTKDNV ARNFGMAAPN GYRKALRLME HADRFGMPII TFIDTPGAWA GIDAEKLGQG 

       190        200        210        220        230        240 
EAIAVNLREM FRLDVPILCT VIGEGGSGGA LGIGVGDRVL MLENAVYTVA TPEACAAILW 

       250        260        270        280        290        300 
KDAKKSDKAA IALKITADDL AKLQIIDGII PEPKGAAHAN PLGAAAKLKE ALLFHLNTLA 

       310        320 
QLTPQERKQL RYDKFRHLGQ FLETAV 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA18754.1.
PIRS76842.
RefSeqNP_442942.1. NC_000911.1.

3D structure databases

ProteinModelPortalP74638.
SMRP74638. Positions 10-320.
ModBaseSearch...

Protein-protein interaction databases

IntActP74638. 3 interactions.
STRINGP74638.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID951971.
GenomeReviewsGene locus sll0728 in contig BA000022_GR.
KEGGsyn:sll0728.
NMPDRfig|1148.1.peg.3043.
PATRIC23843692. VBISynSp132158_3376.

Phylogenomic databases

eggNOGCOG0825.
HOGENOMHBG286557.
OMAGRDTKDN.
PhylomeDBP74638.
ProtClustDBPRK05724.

Enzyme and pathway databases

BioCycSSP1148:SLL0728-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_SYNY3
AccessionPrimary (citable) accession number: P74638
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families