Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q817F2 (ACCA_BACCR)

Last modified November 3, 2009. Version 39. 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: BC_4601
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

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_0000223730

Sequences

Sequence LengthMass (Da)Tools
Q817F2-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 7CE6A4651D05A231

FASTA32436,451
        10         20         30         40         50         60 
MAELEFEKPV VELRNKIREL KDYTKNSQMD FSEEIRILEE KLENLEEDIY GNLKVWDRVQ 

        70         80         90        100        110        120 
IARHAERPTT LDYIEHLFTD FFECHGDRLF GDDAAIVGGI AKYKGMPVTV IGHQRGKDTK 

       130        140        150        160        170        180 
ENIRRNFGMP HPEGYRKALR LMKQAEKFNR PIICFIDTKG AYPGKAAEER GQSEAIARNL 

       190        200        210        220        230        240 
FEMAGLTVPV ICIVIGEGGS GGALGLGVGD YIHMLENSTY SVITPEGAAA ILWKDAGKAK 

       250        260        270        280        290        300 
EAAEAMKITA ADLKELGVID EIIPEARGGA HRNILKQSEN IDLMIQKTFQ QLNGISKDEL 

       310        320 
IEKRYEKYMK IGQVSFSNAS IWIK 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE016877 Genomic DNA. Translation: AAP11508.1.
RefSeqNP_834307.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ817F2.

Genome annotation databases

GeneID1206946.
GenomeReviewsGene locus BC_4601 in contig AE016877_GR.
KEGGbce:BC4601.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ817F2.
OMAHSVYTVA.

Enzyme and pathway databases

BioCycBCER226900:BC_4601-MON.

Family and domain databases

HAMAPMF_00823.
[Tree]
InterProIPR001095. Acetyl_CoA_COase_a_su.
IPR020582. Acetyl_CoA_COase_a_su_cons-reg.
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_BACCR
AccessionPrimary (citable) accession number: Q817F2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 39 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