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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha

Gene

accA

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.UniRule annotation

Pathwayi: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciANTHRA:ACCA-MONOMER.
BANT260799:GJAJ-4552-MONOMER.
BANT261594:GJ7F-4707-MONOMER.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaUniRule annotation (EC:6.4.1.2UniRule annotation)
Short name:
ACCase subunit alphaUniRule annotation
Short name:
Acetyl-CoA carboxylase carboxyltransferase subunit alphaUniRule annotation
Gene namesi
Name:accAUniRule annotation
Ordered Locus Names:BA_4845, GBAA_4845, BAS4494
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaPRO_0000223727Add
BLAST

Interactioni

Subunit structurei

Acetyl-CoA carboxylase is a 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).UniRule annotation

Protein-protein interaction databases

STRINGi198094.BA_4845.

Structurei

3D structure databases

ProteinModelPortaliQ81KY9.
SMRiQ81KY9. Positions 4-312.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AccA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QM9. Bacteria.
COG0825. LUCA.
HOGENOMiHOG000273832.
KOiK01962.
OMAiHSVYTVA.
OrthoDBiEOG6HQSSF.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00823. AcetylCoA_CT_alpha.
InterProiIPR001095. Acetyl_CoA_COase_a_su.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
[Graphical view]
PfamiPF03255. ACCA. 1 hit.
[Graphical view]
PRINTSiPR01069. ACCCTRFRASEA.
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR00513. accA. 1 hit.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q81KY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELEFEKPV VELRNKIREL KDYTKNSQMD FSEEIRILED KLENLEEDIY
60 70 80 90 100
GNMKVWDRVQ IARHAERPTT LDYIEHLFTD FFECHGDRLF GDDAAIVGGI
110 120 130 140 150
AKYKGMPVTV IGHQRGKDTK ENIRRNFGMP HPEGYRKALR LMKQAEKFNR
160 170 180 190 200
PIICFIDTKG AYPGKAAEER GQSEAIARNL FEMAGLTVPV ICIVIGEGGS
210 220 230 240 250
GGALGLGVGD YIHMLENSTY SVITPEGAAA ILWKDAGKAK EAAEAMRITA
260 270 280 290 300
ADLKELGVID EIIPEAKGGA HRNVLKQSEN IDLMLRKTFE QLNGISKDEL
310 320
IEKRYEKYMK IGQVSFSNAS IWIK
Length:324
Mass (Da):36,470
Last modified:June 1, 2003 - v1
Checksum:i25A45F26634206E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP28534.1.
AE017334 Genomic DNA. Translation: AAT33964.1.
AE017225 Genomic DNA. Translation: AAT56792.1.
RefSeqiNP_847048.1. NC_003997.3.
WP_000818794.1. NZ_LHUO01000006.1.
YP_030742.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP28534; AAP28534; BA_4845.
AAT33964; AAT33964; GBAA_4845.
AAT56792; AAT56792; BAS4494.
GeneIDi1083998.
2851550.
KEGGiban:BA_4845.
bar:GBAA_4845.
bat:BAS4494.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP28534.1.
AE017334 Genomic DNA. Translation: AAT33964.1.
AE017225 Genomic DNA. Translation: AAT56792.1.
RefSeqiNP_847048.1. NC_003997.3.
WP_000818794.1. NZ_LHUO01000006.1.
YP_030742.1. NC_005945.1.

3D structure databases

ProteinModelPortaliQ81KY9.
SMRiQ81KY9. Positions 4-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_4845.

Protocols and materials databases

DNASUi1083998.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP28534; AAP28534; BA_4845.
AAT33964; AAT33964; GBAA_4845.
AAT56792; AAT56792; BAS4494.
GeneIDi1083998.
2851550.
KEGGiban:BA_4845.
bar:GBAA_4845.
bat:BAS4494.

Phylogenomic databases

eggNOGiENOG4107QM9. Bacteria.
COG0825. LUCA.
HOGENOMiHOG000273832.
KOiK01962.
OMAiHSVYTVA.
OrthoDBiEOG6HQSSF.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.
BioCyciANTHRA:ACCA-MONOMER.
BANT260799:GJAJ-4552-MONOMER.
BANT261594:GJ7F-4707-MONOMER.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00823. AcetylCoA_CT_alpha.
InterProiIPR001095. Acetyl_CoA_COase_a_su.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
[Graphical view]
PfamiPF03255. ACCA. 1 hit.
[Graphical view]
PRINTSiPR01069. ACCCTRFRASEA.
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR00513. accA. 1 hit.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
    Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
    , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
    Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames / isolate Porton.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.
  3. "Complete genome sequence of Bacillus anthracis Sterne."
    Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sterne.

Entry informationi

Entry nameiACCA_BACAN
AccessioniPrimary (citable) accession number: Q81KY9
Secondary accession number(s): Q6HSE6, Q6KLP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: June 1, 2003
Last modified: January 20, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.