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
Gossypium areysianum
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

Lacks conserved residue(s) required for the propagation of feature annotation.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)
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 bindingi234ZincUniRule annotation1
Metal bindingi239ZincUniRule annotation1
Metal bindingi255ZincUniRule annotation1
Metal bindingi258ZincUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferaseUniRule 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

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 annotationImported
ORF Names:GoarCp030Imported
Encoded oniPlastid; ChloroplastImported
OrganismiGossypium areysianumImported
Taxonomic identifieri47636 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsMalvalesMalvaceaeMalvoideaeGossypium

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

ChloroplastImported, Plastid

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).SAAS annotation
Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and two subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).UniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini232 – 499CoA carboxyltransferase N-terminalInterPro annotationAdd BLAST268

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

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
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.

I6M0P7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKSWFNLIL SKGELEYRCG LSKSMDSRLG PVENTTGNED PTRNDTDKNI
60 70 80 90 100
HDCSDSSSYY SKVDHLVDVK DIRNFISDDT FLIRDSNQDR YSIYFDSENQ
110 120 130 140 150
IFELNNDHSF LSELESFFYS YHNSSYMNNG SKNDEPHYHF NLYDNDTNYG
160 170 180 190 200
WNNHINSCID SYLRSQICID SSILSGSDNS NDNYIYNYIC GEGGNSSEGK
210 220 230 240 250
NFDIITRENG NDLTLKESSN DLDLYKDKDL WVQCECENCY GVNYKKSLNS
260 270 280 290 300
KMNICEQCGY HLKMRSSDRI ELSIDPGTWG PMDEDMISLD PIEFQSEEEL
310 320 330 340 350
YKDRIDFYQR KTGLTEAIQT GTGQLNGIPI AIGVMDFQFM GGSMGSVVGE
360 370 380 390 400
KITRLIEYAT NNFLPLILVC ASGGARMQEG SLSLMQMAKI SSALYDYQSN
410 420 430 440 450
KKLFYVSILT SPTTGGVTAS FGMLGDIIIA EPNAYIAFAG KRVIEQTLNK
460 470 480 490
TIPEGSQAAE YLFHKGLFDP IVPRNPLKGV LSELVQLHGF FPLNQNSIK
Length:499
Mass (Da):56,425
Last modified:October 3, 2012 - v1
Checksum:iBCF1723D36F86E51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JN019795 Genomic DNA Translation: AEH43210.1
RefSeqiYP_006503535.1, NC_018112.1

Genome annotation databases

GeneIDi13229894

Similar proteinsi

Entry informationi

Entry nameiI6M0P7_9ROSI
AccessioniPrimary (citable) accession number: I6M0P7
Entry historyiIntegrated into UniProtKB/TrEMBL: October 3, 2012
Last sequence update: October 3, 2012
Last modified: May 23, 2018
This is version 30 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health