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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi29ZincUniRule annotation1
Metal bindingi32ZincUniRule annotation1
Metal bindingi48ZincUniRule annotation1
Metal bindingi51ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri29 – 51C4-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:YpAngola_A0359
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003591061 – 304Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaAdd BLAST304

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

3D structure databases

ProteinModelPortaliA9R7U5.
SMRiA9R7U5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 294CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST270

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri29 – 51C4-typeUniRule annotationAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000021670.
KOiK01963.
OMAiPEGLWIK.

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.

A9R7U5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWIERILNK SNITQTRKAS IPEGVWTKCD SCGQVLYRAE LERNLEVCPK
60 70 80 90 100
CDHHMRMSAR ARLHMLLDAG SEVELGSELE PKDILKFRDS KKYKDRISAA
110 120 130 140 150
QKDTGEKDAL VAMKGTLQGM PIVAASFEFA FMGGSMASVV GARFVRAVEQ
160 170 180 190 200
ALEDNCPLVC FSSSGGARMQ EALMSLMQMA KTSAALAKMQ ERGLPYISVL
210 220 230 240 250
TDPTMGGVSA SLAMLGDINI AEPKALIGFA GPRVIEQTVR EKLPPGFQRS
260 270 280 290 300
EFLIEKGAID MIVRRPVMRQ TLASILSKLT HQPQPSVVES KADTVAQPEN

QADV
Length:304
Mass (Da):33,274
Last modified:February 5, 2008 - v1
Checksum:i366F008E722A3B00
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000901 Genomic DNA. Translation: ABX85339.1.
RefSeqiWP_002209729.1. NZ_CP009935.1.

Genome annotation databases

EnsemblBacteriaiABX85339; ABX85339; YpAngola_A0359.
KEGGiypg:YpAngola_A0359.
PATRICifig|349746.12.peg.1308.

Similar proteinsi

Entry informationi

Entry nameiACCD_YERPG
AccessioniPrimary (citable) accession number: A9R7U5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: February 5, 2008
Last modified: June 7, 2017
This is version 64 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families