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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Lactobacillus brevis (strain ATCC 367 / JCM 1170)
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)
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 bindingi29ZincUniRule annotation1
Metal bindingi32ZincUniRule annotation1
Metal bindingi47ZincUniRule annotation1
Metal bindingi50ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri29 – 50C4-typeUniRule annotationAdd BLAST22

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

BioCyciLBRE387344:G1G6Z-909-MONOMER
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:LVIS_0927
OrganismiLactobacillus brevis (strain ATCC 367 / JCM 1170)
Taxonomic identifieri387344 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
Proteomesi
  • UP000001652 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003897601 – 277Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaAdd BLAST277

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

STRINGi387344.LVIS_0927

Structurei

3D structure databases

ProteinModelPortaliQ03RW0
SMRiQ03RW0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 277CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST253

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri29 – 50C4-typeUniRule annotationAdd BLAST22

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4107QTG Bacteria
COG0777 LUCA
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
PROSITEiView protein in PROSITE
PS50980 COA_CT_NTER, 1 hit

Sequencei

Sequence statusi: Complete.

Q03RW0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPAKFKTPS QKSLNRRMAS IPDGLVRRCP VCHTTFLTDH WEPTRLCPAC
60 70 80 90 100
GYGFRLTAMQ RIKLTMDTFQ ETNAQLTVPD RYTDAAYQAK VARGRQLTGL
110 120 130 140 150
NESVLTGFGT IDHQSTAIGV MDAFFVMGSL GTATGEKITR LFDEATAKRL
160 170 180 190 200
PVILFTASGG ARMQEGIHSL MQMAKVSAAV ARHSQAGLLY IVVLCDPTTG
210 220 230 240 250
GVTASFAMQG DLILAEPHAL VGFAGRRVIE QTIHQTPPAD FQRAETVLQH
260 270
GFIDAIVARP QLKQRLADLL RLHKGES
Length:277
Mass (Da):30,265
Last modified:November 14, 2006 - v1
Checksum:iB4C7888512AB6D07
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000416 Genomic DNA Translation: ABJ64062.1
RefSeqiWP_011667652.1, NC_008497.1

Genome annotation databases

EnsemblBacteriaiABJ64062; ABJ64062; LVIS_0927
GeneIDi4413816
KEGGilbr:LVIS_0927
PATRICifig|387344.15.peg.902

Similar proteinsi

Entry informationi

Entry nameiACCD_LACBA
AccessioniPrimary (citable) accession number: Q03RW0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: November 14, 2006
Last modified: May 23, 2018
This is version 72 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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