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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)
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 bindingi38ZincUniRule annotation1
Metal bindingi41ZincUniRule annotation1
Metal bindingi57ZincUniRule annotation1
Metal bindingi60ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri38 – 60C4-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:CLI_3820
OrganismiClostridium botulinum (strain Langeland / NCTC 10281 / Type F)
Taxonomic identifieri441772 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000002410 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003897251 – 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

ProteinModelPortaliA7GJJ0.
SMRiA7GJJ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 289CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST256

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri38 – 60C4-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_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.

A7GJJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKNLFRKTK YITVSQKNIE SYKRENTPTI PDGMWVKCNK CGDILYQNDL
60 70 80 90 100
EKNYMVCNLC GNHFRIGVKE RIKYLFDKDT FKEWDYKIKT ENPLDFKGYD
110 120 130 140 150
EKIEHIKEKT NLSEAVTTGK GKIAGMEAVV CIMDSKFMMG SMGCVVGEKI
160 170 180 190 200
TRAIERAIKL RLPVIIFTAS GGARMQEGIL SLMQMAKVSS ALAKLDEEGL
210 220 230 240 250
LYVCVLTDPT TGGVTASFAM LGDIILAEPD GLIGFAGKRV IEQTINEKLP
260 270 280
EDFQKSEFLL EHGFIDKIVP RSDLRKVLAK LINMHQNSF
Length:289
Mass (Da):32,643
Last modified:September 11, 2007 - v1
Checksum:iE2288B1E6A0D1BDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000728 Genomic DNA. Translation: ABS39400.1.
RefSeqiWP_012101204.1. NC_009699.1.

Genome annotation databases

EnsemblBacteriaiABS39400; ABS39400; CLI_3820.
KEGGicbf:CLI_3820.

Similar proteinsi

Entry informationi

Entry nameiACCD_CLOBL
AccessioniPrimary (citable) accession number: A7GJJ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: September 11, 2007
Last modified: November 22, 2017
This is version 61 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