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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
Status
Reviewed-Annotation score: -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

[Biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + 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 beta (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA)
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 bindingi40ZincUniRule annotation1
Metal bindingi43ZincUniRule annotation1
Metal bindingi59ZincUniRule annotation1
Metal bindingi62ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri40 – 62C4-typeUniRule annotationAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
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:2.1.3.15UniRule annotation)
Short name:
ACCase subunit betaUniRule annotation
Short name:
Acetyl-CoA carboxylase carboxyltransferase subunit betaUniRule annotation
Gene namesi
Name:accDUniRule annotation
Ordered Locus Names:CKL_0111
OrganismiClostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
Taxonomic identifieri431943 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000002411 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003897281 – 291Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaAdd BLAST291

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

STRINGi431943.CKL_0111

Structurei

3D structure databases

ProteinModelPortaliA5N4F0
SMRiA5N4F0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 291CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST256

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri40 – 62C4-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_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.

A5N4F0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNKFFKKTK YITVSQRALG DIHDDFTKKP SIPNGMWVKC DGCGKVLYKN
60 70 80 90 100
DMEKNNKVCY HCGYHFRMNA LERLELILDK ESFYEFDKDI TAANPIEFKG
110 120 130 140 150
YEDKIKNMQN KTNIKEAVIT GKGTIGREEA VVCIMDSNFM MGSMGSVVGE
160 170 180 190 200
KITRAVEKSI ELKLPLIIFT TSGGARMQEG IFSLMQMAKV SGAISRLNEE
210 220 230 240 250
GLLYLSVLTD PTTGGVTASF AMIGDIILAE PGALIGFAGK RVIEQTIKQK
260 270 280 290
LPEGFQKAEF LLQHGFIDNI VSRENLKETL RKILVIHGRG N
Length:291
Mass (Da):32,521
Last modified:July 10, 2007 - v1
Checksum:iC63D8054E92972EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000673 Genomic DNA Translation: EDK32181.1
RefSeqiWP_011988707.1, NC_009706.1

Genome annotation databases

EnsemblBacteriaiEDK32181; EDK32181; CKL_0111
KEGGickl:CKL_0111

Similar proteinsi

Entry informationi

Entry nameiACCD_CLOK5
AccessioniPrimary (citable) accession number: A5N4F0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: July 10, 2007
Last modified: May 23, 2018
This is version 65 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, Reference proteome

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