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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha

Gene

accA

Organism
Helicobacter pylori UM114
Status
Unreviewed-Annotation score: -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 annotationSAAS annotation

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

[Biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA.UniRule annotationSAAS annotation

Pathwayi: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.UniRule annotationSAAS 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

Keywordsi

Molecular functionLigaseImported, TransferaseUniRule annotationSAAS annotation
Biological processFatty acid biosynthesisUniRule annotationSAAS annotation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

UniPathwayi
UPA00655;UER00711

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaUniRule annotationSAAS annotation (EC:2.1.3.15UniRule annotationSAAS annotation)
Short name:
ACCase subunit alphaUniRule annotation
Short name:
Acetyl-CoA carboxylase carboxyltransferase subunit alphaUniRule annotation
Gene namesi
Name:accAUniRule annotation
ORF Names:N207_02170Imported
OrganismiHelicobacter pylori UM114Imported
Taxonomic identifieri1355531 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000015605 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

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 annotationSAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 286CoA carboxyltransferase C-terminalInterPro annotationAdd BLAST251

Sequence similaritiesi

Belongs to the AccA family.UniRule annotationSAAS annotation

Phylogenomic databases

OrthoDBiPOG091H0647

Family and domain databases

HAMAPiMF_00823 AcetylCoA_CT_alpha, 1 hit
InterProiView protein in InterPro
IPR001095 Acetyl_CoA_COase_a_su
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
PANTHERiPTHR42853 PTHR42853, 1 hit
PfamiView protein in Pfam
PF03255 ACCA, 1 hit
PRINTSiPR01069 ACCCTRFRASEA
SUPFAMiSSF52096 SSF52096, 1 hit
TIGRFAMsiTIGR00513 accA, 1 hit
PROSITEiView protein in PROSITE
PS50989 COA_CT_CTER, 1 hit

Sequencei

Sequence statusi: Complete.

T0ESY3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAIYLDFENH IKEIQNEIEL ALIRGDEDAK EILEKRLDKE VKSIYSNLTD
60 70 80 90 100
FQKLQLARHP DRPYAMDYID LILKDKYEIF GDRHYNDDKA IVCFIGKIDN
110 120 130 140 150
VPVVVIGEEK GRGTKNKLLR NFGMPNPCGY RKALKMAKFA EKFNLPILML
160 170 180 190 200
VDTAGAYPGI GAEERGQSEA IAKNLQEFAS LKVPTISVII GEGGSGGALA
210 220 230 240 250
IAVADKLAMM EYSIFSVISP EGCAAILWDD PSKTEVAIKA MKITPRDLKE
260 270 280 290 300
AGLIDDIILE PSKGAHRDKF SAANTIKEYF LDALRTIQQD PHFLDNRYQK
310
LMSLGSFVES MD
Length:312
Mass (Da):34,924
Last modified:October 16, 2013 - v1
Checksum:iB98E333E170F0817
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AUSS01000032 Genomic DNA Translation: EPZ92559.1
RefSeqiWP_021310353.1, NZ_AUSS01000032.1

Genome annotation databases

EnsemblBacteriaiEPZ92559; EPZ92559; N207_02170
PATRICifig|1355531.3.peg.1213

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AUSS01000032 Genomic DNA Translation: EPZ92559.1
RefSeqiWP_021310353.1, NZ_AUSS01000032.1

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiEPZ92559; EPZ92559; N207_02170
PATRICifig|1355531.3.peg.1213

Phylogenomic databases

OrthoDBiPOG091H0647

Enzyme and pathway databases

UniPathwayi
UPA00655;UER00711

Family and domain databases

HAMAPiMF_00823 AcetylCoA_CT_alpha, 1 hit
InterProiView protein in InterPro
IPR001095 Acetyl_CoA_COase_a_su
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
PANTHERiPTHR42853 PTHR42853, 1 hit
PfamiView protein in Pfam
PF03255 ACCA, 1 hit
PRINTSiPR01069 ACCCTRFRASEA
SUPFAMiSSF52096 SSF52096, 1 hit
TIGRFAMsiTIGR00513 accA, 1 hit
PROSITEiView protein in PROSITE
PS50989 COA_CT_CTER, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiT0ESY3_HELPX
AccessioniPrimary (citable) accession number: T0ESY3
Entry historyiIntegrated into UniProtKB/TrEMBL: October 16, 2013
Last sequence update: October 16, 2013
Last modified: July 18, 2018
This is version 35 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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