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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Draba nemorosa (Woodland whitlowgrass)
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.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 bindingi229ZincUniRule annotation1
Metal bindingi232ZincUniRule annotation1
Metal bindingi245ZincUniRule annotation1
Metal bindingi248ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri229 – 248C4-typeUniRule annotationAdd 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, 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 annotation
Encoded oniPlastid; Chloroplast
OrganismiDraba nemorosa (Woodland whitlowgrass)
Taxonomic identifieri171822 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeArabideaeDraba

Subcellular locationi

  • Plastidchloroplast stroma UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003591361 – 489Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST489

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

ProteinModelPortaliA4QL28.
SMRiA4QL28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini225 – 489CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST265

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri229 – 248C4-typeUniRule annotationAdd 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.
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.

A4QL28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKSWFNFMF SKGELEYRSG LNKAMDSFAP IEKTTIKKDR FIYDMDKNFY
60 70 80 90 100
GWGERSSYYN NVDLLVSSKD IRNFISDDTF FVRDSNKNSY SIYFDIKKNK
110 120 130 140 150
FEINNDLSDL EFFFYSYCSS SYLNNRSKSD NDLHYDPYVK NTKSNCNNHI
160 170 180 190 200
NSCIDSYFRS HICIDSYFLS DSTNSNESYI YNFICSESGK IRESKNYKIR
210 220 230 240 250
TKTNRNRNNL MNSKDFDITK NYNQLWIQCD NCYGLMYKKV EMNVCEECGH
260 270 280 290 300
YLKMTSSERI ELLIDPGTWN PMDEDMVSAD PIKFHSREEP YKNRIDSAQK
310 320 330 340 350
KTGLTDAVQT GTGQLNGIPV ALGVMDFQFM GGSMGSVVGE KITRLIEYAT
360 370 380 390 400
NQCLPLILVC SSGGARMQEG SLSLMQMAKI SSVLCDYQSS KKLFYISILT
410 420 430 440 450
SPTTGGVTAS FGMLGDIIIA EPYAYIAFAG KRVIEQTLKK AVPEGSQAAE
460 470 480
SLLRKGLLDA IVPRNPLKGV VSELFQLHAF FPLNKTEIK
Length:489
Mass (Da):55,845
Last modified:May 15, 2007 - v1
Checksum:i10C89E02355E8E76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009373 Genomic DNA. Translation: BAF50383.1.
RefSeqiYP_001123559.1. NC_009272.1.

Genome annotation databases

GeneIDi4964714.

Similar proteinsi

Entry informationi

Entry nameiACCD_DRANE
AccessioniPrimary (citable) accession number: A4QL28
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: May 15, 2007
Last modified: May 10, 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