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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
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 (CTb), 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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri232 – 256C4-typeUniRule annotationAdd BLAST25

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
OrganismiGossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Taxonomic identifieri3635 [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

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003591411 – 497Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST497

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

ProteinModelPortaliQ2L915
SMRiQ2L915
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini230 – 497CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST268

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri232 – 256C4-typeUniRule annotationAdd BLAST25

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.

Q2L915-1 [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:February 21, 2006 - v1
Checksum:i82AB188DB240CDFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ345959 Genomic DNA Translation: ABC73637.1
RefSeqiYP_538944.1, NC_007944.1

Genome annotation databases

GeneIDi3989158
KEGGighi:3989158

Similar proteinsi

Entry informationi

Entry nameiACCD_GOSHI
AccessioniPrimary (citable) accession number: Q2L915
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: February 21, 2006
Last modified: April 25, 2018
This is version 50 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health