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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472 / W23)
Status
Unreviewed-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 bindingi32ZincUniRule annotation1
Metal bindingi35ZincUniRule annotation1
Metal bindingi51ZincUniRule annotation1
Metal bindingi54ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri32 – 54C4-typeUniRule annotationAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigaseUniRule annotationImported, TransferaseImported
Biological processFatty acid biosynthesisUniRule annotation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-bindingUniRule annotation, 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 annotationImported
Ordered Locus Names:BSUW23_14200Imported
OrganismiBacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472 / W23)Imported
Taxonomic identifieri655816 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000002233 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

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

Structurei

3D structure databases

ProteinModelPortaliE0TWM0.
SMRiE0TWM0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 290CoA carboxyltransferase N-terminalInterPro annotationAdd BLAST263

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri32 – 54C4-typeUniRule annotationAdd BLAST23

Keywords - Domaini

Zinc-fingerUniRule annotation

Phylogenomic databases

HOGENOMiHOG000021671.
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_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.

E0TWM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKDIFTKKK KYASVPSDQA KHDVPEGIMT KCPKCKKIML TKELDKNMRV
60 70 80 90 100
CMNCDYHFPM NAKQRIESLM DEQSFEEFNQ GMLSENPLGF PGYLEKLEKD
110 120 130 140 150
REKTSLNEAV VTGKGTIGGH PAVVAVMDSS FRMGSMGSVV GEKITLAIEK
160 170 180 190 200
AKADKVPFII FTASGGARMQ EGVLSLMQMA KTSSALKLFS EEQGLIISVM
210 220 230 240 250
THPTTGGVSA SFASLGDYNF AEPGALIGFA GRRIIEQTIG EKLPEDFQTA
260 270 280 290
EFLLKHGQLD AVIHRDDMKK TLENLLDMHQ TGGDIEWLQD
Length:290
Mass (Da):32,035
Last modified:November 2, 2010 - v1
Checksum:iE2580113272A9165
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002183 Genomic DNA. Translation: ADM38877.1.
RefSeqiWP_003223544.1. NC_014479.1.

Genome annotation databases

EnsemblBacteriaiADM38877; ADM38877; BSUW23_14200.
KEGGibss:BSUW23_14200.

Similar proteinsi

Entry informationi

Entry nameiE0TWM0_BACPZ
AccessioniPrimary (citable) accession number: E0TWM0
Entry historyiIntegrated into UniProtKB/TrEMBL: November 2, 2010
Last sequence update: November 2, 2010
Last modified: November 22, 2017
This is version 52 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported