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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha

Gene

accA

Organism
Staphylococcus aureus (strain USA300)
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

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 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

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:SAUSA300_1646
OrganismiStaphylococcus aureus (strain USA300)
Taxonomic identifieri367830 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000001939 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000626781 – 314Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaAdd BLAST314

Proteomic databases

PRIDEiQ2FG38.

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

Structurei

Secondary structure

1314
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Helixi6 – 16Combined sources11
Helixi33 – 49Combined sources17
Helixi53 – 60Combined sources8
Helixi68 – 75Combined sources8
Beta strandi77 – 81Combined sources5
Beta strandi86 – 88Combined sources3
Beta strandi94 – 101Combined sources8
Beta strandi104 – 111Combined sources8
Helixi117 – 122Combined sources6
Helixi124 – 126Combined sources3
Helixi130 – 145Combined sources16
Beta strandi150 – 157Combined sources8
Helixi163 – 167Combined sources5
Helixi170 – 182Combined sources13
Beta strandi188 – 197Combined sources10
Helixi198 – 202Combined sources5
Beta strandi208 – 213Combined sources6
Beta strandi219 – 221Combined sources3
Helixi223 – 230Combined sources8
Helixi234 – 236Combined sources3
Helixi237 – 244Combined sources8
Helixi248 – 253Combined sources6
Beta strandi256 – 261Combined sources6
Helixi268 – 270Combined sources3
Helixi272 – 288Combined sources17
Turni289 – 292Combined sources4
Helixi295 – 307Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F9IX-ray1.98A/C1-314[»]
ProteinModelPortaliQ2FG38.
SMRiQ2FG38.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2FG38.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 289CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST258

Sequence similaritiesi

Belongs to the AccA family.UniRule annotation
Contains 1 CoA carboxyltransferase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000273832.
KOiK01962.
OMAiHSVYTVA.

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.

Q2FG38-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDFEKPLFE IRNKIESLKE SQDKNDVDLQ EEIDMLEASL ERETKKIYTN
60 70 80 90 100
LKPWDRVQIA RLQERPTTLD YIPYIFDSFM ELHGDRNFRD DPAMIGGIGF
110 120 130 140 150
LNGRAVTVIG QQRGKDTKDN IYRNFGMAHP EGYRKALRLM KQAEKFNRPI
160 170 180 190 200
FTFIDTKGAY PGKAAEERGQ SESIATNLIE MASLKVPVIA IVIGEGGSGG
210 220 230 240 250
ALGIGIANKV LMLENSTYSV ISPEGAAALL WKDSNLAKIA AETMKITAHD
260 270 280 290 300
IKQLGIIDDV ISEPLGGAHK DIEQQALAIK SAFVAQLDSL ESLSRDEIAN
310
DRFEKFRNIG SYIE
Length:314
Mass (Da):35,070
Last modified:March 21, 2006 - v1
Checksum:iEC1C58F163948B0F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000255 Genomic DNA. Translation: ABD21607.1.

Genome annotation databases

EnsemblBacteriaiABD21607; ABD21607; SAUSA300_1646.
KEGGisaa:SAUSA300_1646.
PATRICi19592735. VBIStaAur129981_1797.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000255 Genomic DNA. Translation: ABD21607.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F9IX-ray1.98A/C1-314[»]
ProteinModelPortaliQ2FG38.
SMRiQ2FG38.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ2FG38.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD21607; ABD21607; SAUSA300_1646.
KEGGisaa:SAUSA300_1646.
PATRICi19592735. VBIStaAur129981_1797.

Phylogenomic databases

HOGENOMiHOG000273832.
KOiK01962.
OMAiHSVYTVA.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.

Miscellaneous databases

EvolutionaryTraceiQ2FG38.

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_STAA3
AccessioniPrimary (citable) accession number: Q2FG38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 21, 2006
Last modified: November 2, 2016
This is version 73 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

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.