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, chloroplastic

Gene

accD

Organism
Cicer arietinum (Chickpea) (Garbanzo)
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, chloroplastic (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic (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 bindingi183ZincUniRule annotation1
Metal bindingi186ZincUniRule annotation1
Metal bindingi202ZincUniRule annotation1
Metal bindingi205ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri183 – 205C4-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 beta, chloroplasticUniRule 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
Encoded oniPlastid; Chloroplast
OrganismiCicer arietinum (Chickpea) (Garbanzo)
Taxonomic identifieri3827 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeCicereaeCicer

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003591301 – 460Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST460

Proteomic databases

PRIDEiB5LMN4

Interactioni

Subunit structurei

Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and 2 subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).By similarity

Structurei

3D structure databases

SMRiB5LMN4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini179 – 460CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST282

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri183 – 205C4-typeUniRule annotationAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

KOiK01963

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.

B5LMN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKWWFNSML FNKKLEYRCG LSKSIDSFGP IEKKSEEPSI VTDNDSYSHV
60 70 80 90 100
DYLVDVSNRQ NFLSDKTFLV RDRNSYSYSI FFAIENKILE IDYDSQFNWK
110 120 130 140 150
NIINSCIENY LRSQICIDSD ILDNSFKYND NDSDVYSYIC GKVTNSSQST
160 170 180 190 200
STDVITITND SEKESFNDDD DFTQKYKHLW VQCESCYGLN YKKFFKSKMN
210 220 230 240 250
ICEHCGDHLK MSSSDRIELL IDPGTWNPRD EDMVSLDPIE FDPIELDPIE
260 270 280 290 300
LDPIELDSED EPYKTRLDSY QKRTGLSEAV QTGTGQINGI PVAIGIMDFQ
310 320 330 340 350
FMGGSMGSVV GEKITRLIEY ATNQLLPLII VCASGGARMQ EGSLSLMQMA
360 370 380 390 400
KISSALYNYQ INQKLFYVAI LTSPTTGGVT ASFGMLGDII IAEPNAYIAF
410 420 430 440 450
AGKRVIEQTL NTEVPEGSQS AEFLFEKGLF DSIVPRNLLK EVLGELFQFH
460
GFFPLTQNGN
Length:460
Mass (Da):52,180
Last modified:October 14, 2008 - v1
Checksum:iE4367D4A23506C8D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU835853 Genomic DNA Translation: ACH41080.1
RefSeqiYP_002149743.1, NC_011163.1

Genome annotation databases

GeneIDi6797490
KEGGicam:6797490

Similar proteinsi

Entry informationi

Entry nameiACCD_CICAR
AccessioniPrimary (citable) accession number: B5LMN4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 14, 2008
Last modified: June 20, 2018
This is version 44 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health