Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha

Gene

accA

Organism
Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1)
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)
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

BioCyciPCAR338963:GKDU-1364-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:Pcar_1223
OrganismiPelobacter carbinolicus (strain DSM 2380 / Gra Bd 1)
Taxonomic identifieri338963 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
Proteomesi
  • UP000002534 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 – 317317Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaPRO_0000223798Add
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

STRINGi338963.Pcar_1223.

Structurei

3D structure databases

ProteinModelPortaliQ3A585.
SMRiQ3A585. Positions 3-313.
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.

Q3A585-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQFYLDFEKP LVELEQKLSE LRDYSTDEVD FSGEIQRLEK KAEKLRREIF
60 70 80 90 100
SNLNRWQVTQ LARHVNRPFT LDFVEHVFTD WFEVHGDRNF RDDPALVCGF
110 120 130 140 150
ARLDGQPCAV IGHQKGRDTK EKVYRNFGMP NPEGYRKALR VMQMAEQFGL
160 170 180 190 200
PIFTFVDTPG AFPGIGAEER GQAEAIARNL REMAALKVPV IVTVTGEGGS
210 220 230 240 250
GGALAVAVGN RVLMMENAVY SVISPEGCAA ILWKDGAKGP VAAEALKLTA
260 270 280 290 300
GDIQNLGCVI DEVIPEPLGG AHSDHKAAAE QVRICLKKHL DDLKDLSSDE
310
LREQRYQKLR AMTMVQE
Length:317
Mass (Da):35,431
Last modified:November 22, 2005 - v1
Checksum:i13504BC99D4D709F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000142 Genomic DNA. Translation: ABA88472.1.
RefSeqiWP_011340946.1. NC_007498.2.

Genome annotation databases

EnsemblBacteriaiABA88472; ABA88472; Pcar_1223.
KEGGipca:Pcar_1223.
PATRICi22888556. VBIPelCar86875_1351.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000142 Genomic DNA. Translation: ABA88472.1.
RefSeqiWP_011340946.1. NC_007498.2.

3D structure databases

ProteinModelPortaliQ3A585.
SMRiQ3A585. Positions 3-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi338963.Pcar_1223.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA88472; ABA88472; Pcar_1223.
KEGGipca:Pcar_1223.
PATRICi22888556. VBIPelCar86875_1351.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.
BioCyciPCAR338963:GKDU-1364-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. "Complete sequence of Pelobacter carbinolicus DSM 2380."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2380 / Gra Bd 1.

Entry informationi

Entry nameiACCA_PELCD
AccessioniPrimary (citable) accession number: Q3A585
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: November 22, 2005
Last modified: December 9, 2015
This is version 77 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.