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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha

Gene

accA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

Enzyme regulationi

Inhibited by pyrrolidine dione antibiotics moiramide B (CPD1) and CPD2.1 Publication

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. Biotin carboxylase 2 (accC2), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Biotin carboxylase 1 (accC1), 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

Antibiotic resistance, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU29200-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:BSU29200
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi199 – 1991G → S: Resistant to the pyrrolidine dione antibiotic CPD2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 325325Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaPRO_0000146773Add
BLAST

Proteomic databases

PaxDbiO34847.

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

STRINGi224308.Bsubs1_010100015931.

Structurei

3D structure databases

ProteinModelPortaliO34847.
SMRiO34847. Positions 1-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AccA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0825. LUCA.
HOGENOMiHOG000273832.
InParanoidiO34847.
KOiK01962.
OMAiHSVYTVA.
PhylomeDBiO34847.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00823. AcetylCoA_CT_alpha. 1 hit.
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.

O34847-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPRLEFEKP VIELQTKIAE LKKFTQDSDM DLSAEIERLE DRLAKLQDDI
60 70 80 90 100
YKNLKPWDRV QIARLADRPT TLDYIEHLFT DFFECHGDRA YGDDEAIVGG
110 120 130 140 150
IAKFHGLPVT VIGHQRGKDT KENLVRNFGM PHPEGYRKAL RLMKQADKFN
160 170 180 190 200
RPIICFIDTK GAYPGRAAEE RGQSEAIAKN LFEMAGLRVP VICIVIGEGG
210 220 230 240 250
SGGALGLGVG NHLHMLENST YSVISPEGAA ALLWKDSSLA KKAAETMKIT
260 270 280 290 300
APDLKELGII DHMIKEVKGG AHHDVKLQAS YMDETLKQSL KTLLKLSEEE
310 320
LVQQRYEKYK AIGKVSVEDQ YIGVN
Length:325
Mass (Da):36,334
Last modified:January 1, 1998 - v1
Checksum:i9B177DEE4A5B5864
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008220 Genomic DNA. Translation: AAC00341.1.
AL009126 Genomic DNA. Translation: CAB14880.1.
PIRiG69580.
RefSeqiNP_390798.1. NC_000964.3.
WP_003229417.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14880; CAB14880; BSU29200.
GeneIDi936367.
KEGGibsu:BSU29200.
PATRICi18977734. VBIBacSub10457_3055.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008220 Genomic DNA. Translation: AAC00341.1.
AL009126 Genomic DNA. Translation: CAB14880.1.
PIRiG69580.
RefSeqiNP_390798.1. NC_000964.3.
WP_003229417.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliO34847.
SMRiO34847. Positions 1-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015931.

Proteomic databases

PaxDbiO34847.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14880; CAB14880; BSU29200.
GeneIDi936367.
KEGGibsu:BSU29200.
PATRICi18977734. VBIBacSub10457_3055.

Phylogenomic databases

eggNOGiCOG0825. LUCA.
HOGENOMiHOG000273832.
InParanoidiO34847.
KOiK01962.
OMAiHSVYTVA.
PhylomeDBiO34847.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.
BioCyciBSUB:BSU29200-MONOMER.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00823. AcetylCoA_CT_alpha. 1 hit.
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...

Entry informationi

Entry nameiACCA_BACSU
AccessioniPrimary (citable) accession number: O34847
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 117 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.