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B4SG04 (ACCA_PELPB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:Ppha_2672
OrganismPelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1) [Complete proteome] [HAMAP]
Taxonomic identifier324925 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon

Protein attributes

Sequence length335 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 – 335335Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_1000134503

Sequences

Sequence LengthMass (Da)Tools
B4SG04 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 9FFFEC2E523D7ABD

FASTA33537,688
        10         20         30         40         50         60 
MATKVVLDFE KPLFELEAKL DEMRQCLRNS TREQSPSETE MLNHDIETLE LKVDALRRSI 

        70         80         90        100        110        120 
YKNLTRWQKV QLARHPARPY TLDYIHLMTR DFLELAGDRR YSDDKAIIGG FARIEESATG 

       130        140        150        160        170        180 
FSQPVMIIGH QKGRDTKSNL YRNFGMAQPE GYRKALRLMQ LAEKFRKPVI TLIDTPGAFP 

       190        200        210        220        230        240 
GIEAEERGTA EAIARNLYEM AKLTVPVICV IIGEGASGGA IGIGVGDRIL MAENSWYSVI 

       250        260        270        280        290        300 
SPESCSSILW RSWKYKEQAA EALQLTAVDL LSQGIIDRII PEPVGGAHTD PDVMAATLKE 

       310        320        330 
ILIEELKALL PKDPATLVHE RIEKFSSMGV WNEEE 

« Hide

References

[1]"Complete sequence of Pelodictyon phaeoclathratiforme BU-1."
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., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5477 / BU-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001110 Genomic DNA. Translation: ACF44831.1.
RefSeqYP_002019448.1. NC_011060.1.

3D structure databases

ProteinModelPortalB4SG04.
SMRB4SG04. Positions 6-330.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4SG04.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6462075.
GenomeReviewsGene locus Ppha_2672 in contig CP001110_GR.
KEGGpph:Ppha_2672.
PATRIC22906175. VBIPelPha134556_2849.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG286557.
OMAGRDTKDN.
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_PELPB
AccessionPrimary (citable) accession number: B4SG04
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 28 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