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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: -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

[Biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + 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 alpha (accA), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), 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 functionTransferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-3168-MONOMER
UniPathwayiUPA00655; UER00711

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaUniRule annotation (EC:2.1.3.15UniRule 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_sf
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: April 25, 2018
This is version 97 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
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Main funding by: National Institutes of Health