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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

Enzyme regulationi

Inhibited by pyrrolidine dione antibiotics moiramide B (CPD1) and CPD2.

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. Biotin carboxylase 2 (accC2), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Biotin carboxylase 1 (accC1), 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 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

BioCyciBSUB:BSU29210-MONOMER.
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
Synonyms:yttI
Ordered Locus Names:BSU29210
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003896861 – 290Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaAdd BLAST290

Proteomic databases

PaxDbiC0SP93.

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

STRINGi224308.Bsubs1_010100015936.

Structurei

3D structure databases

ProteinModelPortaliC0SP93.
SMRiC0SP93.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 290CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST263

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

eggNOGiENOG4108IEY. Bacteria.
COG0777. LUCA.
HOGENOMiHOG000021671.
InParanoidiC0SP93.
KOiK01963.
OMAiPEGLWIK.
PhylomeDBiC0SP93.

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.

C0SP93-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKDIFTKKK KYASVPSDQA KHDVPEGIMT KCPKCKKIML TKELDKNMRV
60 70 80 90 100
CMNCDYHFPM NAKQRIESLM DEQSFEEFNQ GMLSENPLGF PGYLEKLEKD
110 120 130 140 150
REKTSLNEAV VTGKGTIGGH PAVVAVMDSS FRMGSMGSVV GEKITLAIEK
160 170 180 190 200
AKADKVPFII FTASGGARMQ EGVLSLMQMA KTSSALKLFS EEQGLIISVM
210 220 230 240 250
THPTTGGVSA SFASLGDYNF AEPGALIGFA GRRIIEQTIG EKLPEDFQTA
260 270 280 290
EFLLKHGQLD AVIHRDDMKK TLENLLDMHQ TGGDIEWLQD
Length:290
Mass (Da):32,035
Last modified:May 5, 2009 - v1
Checksum:iE2580113272A9165
GO

Sequence cautioni

The sequence AAC00340 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008220 Genomic DNA. Translation: AAC00340.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB14881.2.
PIRiG70001.
RefSeqiNP_390799.2. NC_000964.3.
WP_003223544.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14881; CAB14881; BSU29210.
GeneIDi936186.
KEGGibsu:BSU29210.
PATRICifig|224308.179.peg.3172.

Similar proteinsi

Entry informationi

Entry nameiACCD_BACSU
AccessioniPrimary (citable) accession number: C0SP93
Secondary accession number(s): O34571, Q795V4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: May 5, 2009
Last modified: November 22, 2017
This is version 56 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

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families