Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Clostridium perfringens D str. JGS1721
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 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 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
ORF Names:CJD_1504Imported
OrganismiClostridium perfringens D str. JGS1721Imported
Taxonomic identifieri488537 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000003188 Componenti: Unassembled WGS sequence

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

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.
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: September 27, 2017
This is version 51 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteomeImported