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B0B7I1 (ACCA_CHLT2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:CTL0517
OrganismChlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) [Complete proteome] [HAMAP]
Taxonomic identifier471472 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length324 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 – 324324Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_1000134472

Sequences

Sequence LengthMass (Da)Tools
B0B7I1 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 4AB8EAE5FEC574AF

FASTA32436,374
        10         20         30         40         50         60 
MELLPHEKQV VEYEKTIAEF KEKNKENSLL SSSEIQKLDK RLDRLKEKIY SDLTPWERVQ 

        70         80         90        100        110        120 
ICRHPSRPRT VNYIEGMCEE FVELCGDRTF RDDPAVVGGF AKIQGQRFML IGQEKGCDTK 

       130        140        150        160        170        180 
SRMHRNFGML CPEGFRKALR LAKMAEKFGL PIIFLVDTPG AFPGLTAEER GQGWAIATNL 

       190        200        210        220        230        240 
FELARLATPI IVIVIGEGCS GGALGMAIGD VVAMLEHSYY SVISPEGCAS ILWKDPKKNS 

       250        260        270        280        290        300 
DAAAMLKMHG EDLKGFAIVD AVIKEPIGGA HHNPAATYRS VQEYVLQEWV KLKDLPVEEL 

       310        320 
LEKRYQKFRT IGLYETSSES DSEA 

« Hide

References

[1]"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates."
Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.
Genome Res. 18:161-171(2008) [PubMed: 18032721] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 434/Bu / ATCC VR-902B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM884176 Genomic DNA. Translation: CAP03957.1.
RefSeqYP_001654594.1. NC_010287.1.

3D structure databases

ProteinModelPortalB0B7I1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0B7I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5858233.
GenomeReviewsGene locus CTL0517 in contig AM884176_GR.
KEGGctb:CTL0517.
PATRIC20376580. VBIChlTra32542_0556.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG286557.
OMAGRDTKDN.
ProtClustDBPRK05724.

Enzyme and pathway databases

BioCycCTRA471472:CTL0517-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_CHLT2
AccessionPrimary (citable) accession number: B0B7I1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 35 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