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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Gossypium darwinii (Darwin's cotton) (Gossypium barbadense var. darwinii)
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, 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 bindingi232ZincUniRule annotation1
Metal bindingi237ZincUniRule annotation1
Metal bindingi253ZincUniRule annotation1
Metal bindingi256ZincUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigaseUniRule annotation, 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 beta, chloroplasticUniRule 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:GodaCp030Imported
Encoded oniPlastid; ChloroplastImported
OrganismiGossypium darwinii (Darwin's cotton) (Gossypium barbadense var. darwinii)Imported
Taxonomic identifieri34276 [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

Structurei

3D structure databases

ProteinModelPortaliH2B8E5.
SMRiH2B8E5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini230 – 497CoA 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.

H2B8E5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKSWFNLIL SKGELEYRCG LSKSMDSRLG PVENTTVNED PTRNDTDKNI
60 70 80 90 100
HDCSDSSSYY SKVDHLVDVK DIRNFISDDT FLIRDSNQDR YSIYFDSENQ
110 120 130 140 150
IFELNNDHSF LSELESFFYS YHNSSYMNNG SKNDEPHYHF NLYDNDTNCG
160 170 180 190 200
WNNHINSCID SYLRSQICID SSILSGSDNS NDNYISNYIC GEGGNSSEGK
210 220 230 240 250
NFDIITRENG NDLTLKESSN DLDLYKDLWV QCECENCYGV NYKKSLNSKM
260 270 280 290 300
NICEQCGYHL KMRSSDRIEL SIDPGTWGPM DEDMISLDPI EFQSEEELYK
310 320 330 340 350
DRIDFYQRKT GLTEAIQTGT GQLNGIPIAI GVMDFQFMGG SMGSVVGEKI
360 370 380 390 400
TRLIEYATNN FLPLILVCAS GGARMQEGSL SLMQMAKISS ALYDYQSNKK
410 420 430 440 450
LFYVSILTSP TTGGVTASFG MLGDIIIAEP NAYIAFAGKR VIEQTLNKTI
460 470 480 490
PEGSQAAEYL FHKGLFDPIV PRNPLKGVLS ELVQLHGFFP LNQNSIK
Length:497
Mass (Da):56,087
Last modified:March 21, 2012 - v1
Checksum:i82AB188DB240CDFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ325741 Genomic DNA. Translation: ADV38884.1.
RefSeqiYP_005087798.1. NC_016670.1.

Genome annotation databases

GeneIDi11538638.

Similar proteinsi

Entry informationi

Entry nameiH2B8E5_GOSDA
AccessioniPrimary (citable) accession number: H2B8E5
Entry historyiIntegrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: November 22, 2017
This is version 37 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation