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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

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 (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 bindingi225ZincUniRule annotation1
Metal bindingi228ZincUniRule annotation1
Metal bindingi244ZincUniRule annotation1
Metal bindingi247ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri225 – 247C4-typeUniRule annotationAdd BLAST23

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
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
Proteomesi
  • UP000011115 Componenti: Unassembled WGS sequence

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_00002775801 – 490Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST490

Expressioni

Tissue specificityi

RNA expressed in leaf, root, stem, and tuber; the least expression occurs in stems. RNA persists even in senescent leaves.1 Publication

Inductioni

Not induced by light.

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

SMRiQ2VEG8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini221 – 490CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST270

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri225 – 247C4-typeUniRule annotationAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoidiQ2VEG8
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.

Q2VEG8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERWWFNSML FKKEFERRCG LNKSMGSLGP IENTSEDPNL KMKNIHSCSN
60 70 80 90 100
VDYLFGVKDI WNFISDDTFL VSDRNGDSYS IYFDIENQIF EVDNDHSFLS
110 120 130 140 150
ELESSFSSYR NSSYLNNGFR GEDPYYNSYM SYMYDTQYSW NNHINSCIDN
160 170 180 190 200
YLQSQICIDT SIISGSESYG DSYIYRAICS GESLNSSENE GSSRRTRTKG
210 220 230 240 250
SDLTIRESSN DLEVTQKYKH LWVQCENCYG LNYKKFLKSK MNICEQCGYH
260 270 280 290 300
LKMSSSDRIE LLIDPGTWDP MDEDMVSLDP IEFHSEEEPY KDRIDSYQRK
310 320 330 340 350
TGLTEAVQTG IGQLNGIPVA IGVMDFQFMG GSMGSVVGEK ITRLIEHAAN
360 370 380 390 400
QNLPLIIVCA SGGARMQEGS LSLMQMAKIS SALYDYQLNK KLFYVSILTS
410 420 430 440 450
PTTGGVTASF GMLGDIIIAE PNAYIAFAGK RVIEQTLNKT VPEGSQAAEY
460 470 480 490
LFQKGLFDLI VPRNLLKSVL SELFKLHAFF PLNQKSSKIK
Length:490
Mass (Da):55,596
Last modified:January 20, 2009 - v3
Checksum:iDFD4751300F86C5B
GO

Sequence cautioni

The sequence AAC23997 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence ABB90050 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence ABD47066 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti399T → K in ABB90050 (PubMed:16835751).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069288 Genomic DNA Translation: AAC23997.1 Different initiation.
DQ231562 Genomic DNA Translation: ABB90050.1 Different initiation.
DQ386163 Genomic DNA Translation: ABD47066.1 Different initiation.
PIRiT07012
RefSeqiYP_635648.1, NC_008096.2

Genome annotation databases

GeneIDi4099986
KEGGisot:4099986

Similar proteinsi

Entry informationi

Entry nameiACCD_SOLTU
AccessioniPrimary (citable) accession number: Q2VEG8
Secondary accession number(s): O78323
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: January 20, 2009
Last modified: April 25, 2018
This is version 53 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health