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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Bacillus thuringiensis subsp. konkukian (strain 97-27)
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 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 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:BT9727_4330
OrganismiBacillus thuringiensis subsp. konkukian (strain 97-27)
Taxonomic identifieri281309 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001301 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003896881 – 289Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaAdd BLAST289

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

ProteinModelPortaliQ6HCT1.
SMRiQ6HCT1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 289CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST262

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-finger

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.
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.

Q6HCT1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRDLFVKKK KYAAIPSEQV RKDVPDGVMT KCPKCKKIMY TKEVLKNLKV
60 70 80 90 100
CVNCGYHHPM NAWERLDSIL DEGSFREYDK EMVSLNPLEF PDYEEKLESD
110 120 130 140 150
RKKTELNEAV VTGEGTIDDM LVVVAVMDSR FRMGSMGSVV GEKIARAVEK
160 170 180 190 200
AYDLQVPFII FTASGGARMQ EGILSLMQMA KTSVALKKHS NAGGLFISVM
210 220 230 240 250
THPTTGGVSA SFASLGDYNL AEPGALIGFA GRRVIEQTVR EKLPEDFQTA
260 270 280
EFLLEHGQLD AVVHRDDMRE SLRKILEVHQ GGEMAVWQS
Length:289
Mass (Da):32,282
Last modified:July 19, 2004 - v1
Checksum:iC2BB1257A711B7F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017355 Genomic DNA. Translation: AAT59085.1.
RefSeqiWP_000942870.1. NC_005957.1.
YP_038645.1. NC_005957.1.

Genome annotation databases

EnsemblBacteriaiAAT59085; AAT59085; BT9727_4330.
GeneIDi2855989.
KEGGibtk:BT9727_4330.
PATRICifig|281309.8.peg.4616.

Similar proteinsi

Entry informationi

Entry nameiACCD_BACHK
AccessioniPrimary (citable) accession number: Q6HCT1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: July 19, 2004
Last modified: June 7, 2017
This is version 80 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