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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta 2

Gene

accD2

Organism
Lysinibacillus sphaericus (strain C3-41)
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 2 (accD2), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta 1 (accD1)
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 bindingi30ZincUniRule annotation1
Metal bindingi33ZincUniRule annotation1
Metal bindingi49ZincUniRule annotation1
Metal bindingi52ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri30 – 52C4-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 beta 2UniRule annotation (EC:6.4.1.2UniRule annotation)
Short name:
ACCase subunit beta 2UniRule annotation
Short name:
Acetyl-CoA carboxylase carboxyltransferase subunit beta 2UniRule annotation
Gene namesi
Name:accD2UniRule annotation
Ordered Locus Names:Bsph_4132
OrganismiLysinibacillus sphaericus (strain C3-41)
Taxonomic identifieri444177 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus
Proteomesi
  • UP000002164 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003897881 – 285Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta 2Add BLAST285

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

STRINGi444177.Bsph_4132.

Structurei

3D structure databases

ProteinModelPortaliB1HX17.
SMRiB1HX17.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 285CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST260

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri30 – 52C4-typeUniRule annotationAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4107QTG. Bacteria.
COG0777. LUCA.
HOGENOMiHOG000021671.
KOiK01963.
OMAiPEGLWIK.
OrthoDBiPOG091H04JK.

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.

B1HX17-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIRSLFSGN RKKKEDGQEK AFPEGLMTKC PECRHIQLTK ELEKNHKVCT
60 70 80 90 100
KCSHHFKMTA QERVDYFLDE GSFVSMDDHL QTSNPLNFPA YVEKISADQE
110 120 130 140 150
KTGLNEAVLT GVGTLDGEEI VVAIMDSHFR MGSMGSVVGE KITRAVEKAT
160 170 180 190 200
ELGVPFIIFT ASGGARMQEG VLSLMQMAKT SVALKRHSDQ GLLFISILTH
210 220 230 240 250
PTTGGVSASF ASVGDINIAE PQALIGFAGR RVIEETVREK LPNDFQTAEF
260 270 280
LLEHGQLDAI FPRKDLRKQV SLLVKMHTKG GVQHV
Length:285
Mass (Da):31,415
Last modified:April 29, 2008 - v1
Checksum:i04BAE21335716FEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000817 Genomic DNA. Translation: ACA41593.1.

Genome annotation databases

EnsemblBacteriaiACA41593; ACA41593; Bsph_4132.
KEGGilsp:Bsph_4132.

Similar proteinsi

Entry informationi

Entry nameiACCD2_LYSSC
AccessioniPrimary (citable) accession number: B1HX17
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: April 29, 2008
Last modified: June 7, 2017
This is version 60 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

Documents

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