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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Clostridium perfringens D str. JGS1721
Status
Unreviewed-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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

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)
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 functionLigaseImported, TransferaseUniRule annotationImported
Biological processFatty acid biosynthesisUniRule annotation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-bindingUniRule annotation, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayi
UPA00655;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 annotationImported
ORF Names:CJD_1504Imported
OrganismiClostridium perfringens D str. JGS1721Imported
Taxonomic identifieri488537 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000003188 Componenti: Unassembled WGS sequence

Subcellular locationi

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

ProteinModelPortaliB1V5B3
SMRiB1V5B3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 292CoA carboxyltransferase N-terminalInterPro annotationAdd BLAST257

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-fingerUniRule annotation

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
IPR020893 Cyt_c_oxidase_su5b_Zn_BS
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
PS00848 COX5B_1, 1 hit

Sequencei

Sequence statusi: Complete.

B1V5B3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIKNLLNKRK YITVSSVELN DTELNEDEKP NIPSGMWSKC EKCAKILYTE
60 70 80 90 100
DLRENFNVCP NCGHHFKLGA YERIKYLTDE NTFVEFDKKM VGRNPLDFNG
110 120 130 140 150
YEEKIKGYQK KSHVIEGVVT GEAYIAQRKV VLCVMDSNFM MGSMGTAVGE
160 170 180 190 200
KITRAIEYAT KNRLPLIIFT CSGGARMQEG IYSLMQMAKV SGAIYRHGRE
210 220 230 240 250
NLLYITVLTN PTTGGVTASF AMEGDIILSE PGCLVGFAGR RVIEGTINEK
260 270 280 290
LPDDFQTAEF LLEKGFIDKI VQRKDLKQVI TSLLRMHEVD YE
Length:292
Mass (Da):33,030
Last modified:May 20, 2008 - v1
Checksum:i070DC36700B4F026
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ABOO01000031 Genomic DNA Translation: EDT71035.1
RefSeqiWP_003458574.1, NZ_ABOO01000031.1

Genome annotation databases

EnsemblBacteriaiEDT71035; EDT71035; CJD_1504
GeneIDi29571556

Similar proteinsi

Entry informationi

Entry nameiB1V5B3_CLOPF
AccessioniPrimary (citable) accession number: B1V5B3
Entry historyiIntegrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: June 20, 2018
This is version 54 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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