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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Barbarea verna (Early yellowrocket) (Erysimum vernum)
Status
Reviewed-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.IEP:

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.IEP:

Cofactori

Zn2+IEP:Note: Binds 1 zinc ion per subunit.IEP:

Pathwayi: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.IEP:
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 bindingi227ZincIEP:1
Metal bindingi230ZincIEP:1
Metal bindingi243ZincIEP:1
Metal bindingi246ZincIEP:1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri227 – 246C4-typeIEP:Add BLAST20

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
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, chloroplasticIEP: (EC:6.4.1.2IEP:)
Short name:
ACCase subunit betaIEP:
Short name:
Acetyl-CoA carboxylase carboxyltransferase subunit betaIEP:
Gene namesi
Name:accDIEP:
Encoded oniPlastid; Chloroplast
OrganismiBarbarea verna (Early yellowrocket) (Erysimum vernum)
Taxonomic identifieri50458 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCardamineaeBarbarea

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_00003591231 – 487Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST487

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).HMP:

Structurei

3D structure databases

ProteinModelPortaliA4QKB4.
SMRiA4QKB4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini223 – 487CoA carboxyltransferase N-terminalIEP:Add BLAST265

Sequence similaritiesi

Belongs to the AccD/PCCB family.IEP:

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri227 – 246C4-typeIEP:Add BLAST20

Keywords - Domaini

Zinc-finger

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.

A4QKB4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKSWFNLMF SKGELEYRGE LSKAMDSFAP SEKTTISQDR FIYDMDKNFY
60 70 80 90 100
GWGERSSYSN NVDLLVSSKD IRNFISDDTF FIRDSNKNSY SIYFDIKKQK
110 120 130 140 150
FEIDNDLSDL EFFFYSYCSS SYLNNRSKGD NDLHYDPYIK DTKYNCTNHI
160 170 180 190 200
NSCIDSYFRS HICIDSHFLS DSKNSNENYI YNFICSESGK IRERKNYKIR
210 220 230 240 250
TNRNRSNLIS SKDFAITQNY NKLWIQCDNC YGLMYKKVKM NVCEQCGHYL
260 270 280 290 300
KMSSSERIEL SIDPGTWNPM DEDMVSADPI KFHSREEPYK NRIDSAQKTT
310 320 330 340 350
GLTDAVQTGT GQLNGIPVAL GVMDFQFMGG SMGSVVGEKI TRLIEYATNQ
360 370 380 390 400
CLPLILVCSS GGARMQEGSL SLMQMAKISS VLCDYQSSQK LFYISILTSP
410 420 430 440 450
TTGGVTASFG MLGDIIIAEP YAYIAFAGKR VIEQTLKKAV PEGSQAAESL
460 470 480
LRKGLLDAIV PRNPLKGVLS ELFQLHAFFP LTKNSIK
Length:487
Mass (Da):55,415
Last modified:May 15, 2007 - v1
Checksum:i55CAB10CD571F2CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009370 Genomic DNA. Translation: BAF50119.1.
RefSeqiYP_001123295.1. NC_009269.1.

Genome annotation databases

GeneIDi4961857.

Similar proteinsi

Entry informationi

Entry nameiACCD_BARVE
AccessioniPrimary (citable) accession number: A4QKB4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: May 15, 2007
Last modified: November 22, 2017
This is version 45 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