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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.UniRule annotation

Catalytic activityi

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

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Enzyme regulationi

Inhibited by pyrrolidine dione antibiotic moiramide B (CPD1); in vivo the effects are not seen unless the efflux MexAB-OprM system is inactive.

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), Biotin carboxylase (accC)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi31ZincUniRule annotation1
Metal bindingi34ZincUniRule annotation1
Metal bindingi50ZincUniRule annotation1
Metal bindingi53ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri31 – 53C4-typeUniRule annotationAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaUniRule annotation (EC:6.4.1.2UniRule annotation)
Short name:
ACCase subunit betaUniRule annotation
Short name:
Acetyl-CoA carboxylase carboxyltransferase subunit betaUniRule annotation
Gene namesi
Name:accDUniRule annotation
Ordered Locus Names:PA3112
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3112.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003590331 – 290Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaAdd BLAST290

Proteomic databases

PaxDbiQ9HZA7.
PRIDEiQ9HZA7.

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

STRINGi208964.PA3112.

Structurei

3D structure databases

ProteinModelPortaliQ9HZA7.
SMRiQ9HZA7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 290CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST264

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri31 – 53C4-typeUniRule annotationAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4107QTG. Bacteria.
COG0777. LUCA.
HOGENOMiHOG000021670.
InParanoidiQ9HZA7.
KOiK01963.
OMAiPEGLWIK.
PhylomeDBiQ9HZA7.

Family and domain databases

HAMAPiMF_01395. AcetylCoA_CT_beta. 1 hit.
InterProiView protein in InterPro
IPR034733. AcCoA_carboxyl.
IPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR029045. ClpP/crotonase-like_dom.
IPR011762. COA_CT_N.
PfamiView protein in Pfam
PF01039. Carboxyl_trans. 1 hit.
PRINTSiPR01070. ACCCTRFRASEB.
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR00515. accD. 1 hit.
PROSITEiView protein in PROSITE
PS50980. COA_CT_NTER. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HZA7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNWLVDKLI PSIMRSESQK SSVPEGLWHK CPSCEAVLYR PELEKTLDVC
60 70 80 90 100
PKCDHHMRIN ARTRLDIFLD EDGREELGAD LEPVDRLKFR DSKKYKDRLA
110 120 130 140 150
AAQKDTGEKD ALIAMSGKLQ GMPVVACAFE FSFMGGSMGA IVGERFVRAA
160 170 180 190 200
NVALEKRCPL ICFSASGGAR MQEALISLMQ MAKTSAVLAR LREEGIPFVS
210 220 230 240 250
VLTDPVYGGV SASLAMLGDV IVGEPKALIG FAGPRVIEQT VREKLPEGFQ
260 270 280 290
RSEFLLEHGA IDMIVHRAEL RPRLANLLSA FTHSPSPVSA
Length:290
Mass (Da):31,843
Last modified:March 1, 2001 - v1
Checksum:i3FFB8A0C59FAC2AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB031231 Genomic DNA. Translation: BAB13795.1.
AE004091 Genomic DNA. Translation: AAG06500.1.
PIRiC83257.
RefSeqiNP_251802.1. NC_002516.2.
WP_003104199.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG06500; AAG06500; PA3112.
GeneIDi877680.
KEGGipae:PA3112.
PATRICifig|208964.12.peg.3264.

Similar proteinsi

Entry informationi

Entry nameiACCD_PSEAE
AccessioniPrimary (citable) accession number: Q9HZA7
Secondary accession number(s): Q7DJF5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: March 1, 2001
Last modified: July 5, 2017
This is version 94 of the entry and version 1 of the sequence. See 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