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Reviewed, UniProtKB/Swiss-Prot Q3ATN9 (ACCA_CHLCH)

Last modified June 16, 2009. Version 27. 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: Cag_0363
OrganismChlorobium chlorochromatii (strain CaD3) [Complete proteome] [HAMAP]
Taxonomic identifier340177 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length334 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 – 334334Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_1000062602

Sequences

Sequence LengthMass (Da)Tools
Q3ATN9-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: F4A42A4FF3B49911

FASTA33437,453
        10         20         30         40         50         60 
MSAKVVLDFE KPLFELEAKL HEMRECLRNT TRDQSPADAD LLYGDIEALE RKVELLRRSI 

        70         80         90        100        110        120 
YKNLTRWQKV QLARHPERPY SLDYIYMMTT GFVELAGDRH FSDDKAIIGG FARLEDEAAG 

       130        140        150        160        170        180 
FSQSVMMIGH QKGRDTKTNL YRNFGMAQPE GYRKALRLMK LAEKFRKPII TLIDTPGAFP 

       190        200        210        220        230        240 
GIEAEERGQA EAIARNLMEM AQLTVPVICV IIGEGASGGA IGLGVGNRIL MAENSWYSVI 

       250        260        270        280        290        300 
SPESCSSILW RSWNFKEQAA EALQPTAEDL LAQGIVDRIV PEPLGGAHTD PDAMGATLKA 

       310        320        330 
MLIEELQQLL PKEPQLLVRE RIEKFSAMGV WNEV 

« Hide

References

[1]"Complete sequence of Chlorobium chlorochromatii CaD3."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000108 Genomic DNA. Translation: ABB27636.1.
RefSeqYP_378679.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3748008.
GenomeReviewsGene locus Cag_0363 in contig CP000108_GR.
KEGGcch:Cag_0363.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3ATN9.
OMAQ3ATN9. HSVYTVA.

Enzyme and pathway databases

BioCycCCHL340177:CAG_0363-MON.

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_CHLCH
AccessionPrimary (citable) accession number: Q3ATN9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 22, 2005
Last modified: June 16, 2009
This is version 27 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