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Reviewed, UniProtKB/Swiss-Prot Q253Y8 (ACCA_CHLFF)

Last modified June 16, 2009. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
      Short name=Acetyl-CoA carboxylase carboxyltransferase subunit alpha
      Short name=ACCase subunit alpha
    EC=6.4.1.2
Gene names
Name: accA
Ordered Locus Names: CF0628
OrganismChlamydophila felis (strain Fe/C-56) [Complete proteome] [HAMAP]
Taxonomic identifier264202 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydophila

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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: HAMAP

   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: HAMAP

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_1000062603

Sequences

Sequence LengthMass (Da)Tools
Q253Y8-1 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 3CE8886AAAD41D08

FASTA32436,403
        10         20         30         40         50         60 
MELLPHEKQV VEYEKTIAEF KEKNKKNSLL SSSEIQKLER RLDKLKEKIY SDLTPWERVQ 

        70         80         90        100        110        120 
ICRHPSRPRS VNYIEGMCEE FVELCGDRTF RDDPAVVGGL AKINGQRFML IGQEKGCDTS 

       130        140        150        160        170        180 
SRMHRNFGML CPEGFRKALR LAKMAEKFGL PIVFLVDTPG AFPGLTAEAR GQGWAIANNL 

       190        200        210        220        230        240 
FQLARLKTPI IVLVIGEGCS GGALGMAIGD VIAMLEHSYY SVISPEGCAS ILWKDPKKNS 

       250        260        270        280        290        300 
EAAAMLKMHG EDLKQFAIVD VVIKEPVGGA HHNPSAVYRD VQNFILQEWL RLKDLSIEDL 

       310        320 
LEKRYQKFRT IGLYETSSES GPEA 

« Hide

References

[1]"Genome sequence of the cat pathogen, Chlamydophila felis."
Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H., Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H., Hattori M., Kuhara S., Shirai M.
DNA Res. 13:15-23(2006) [PubMed: 16766509] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP006861 Genomic DNA. Translation: BAE81400.1.
RefSeqYP_515545.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3958640.
GenomeReviewsGene locus CF0628 in contig AP006861_GR.
KEGGcfe:CF0628.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ253Y8.
OMAQ253Y8. PKKNSEA.

Family and domain databases

HAMAPMF_00823.
[Tree]
InterProIPR001095. Acetyl_CoA_COase_a_su.
IPR011763. COA_CT_C.
[Graphical view]
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_CHLFF
AccessionPrimary (citable) accession number: Q253Y8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 18, 2006
Last modified: June 16, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents