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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 (By similarity). Is up-regulated upon chromoplast differentiation, presumably for fatty acid biosynthesis.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), 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 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
OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifieri4081 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
Proteomesi
  • UP000004994 Componenti: Chloroplast

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Chloroplast, Chromoplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002774211 – 490Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST490

Proteomic databases

PaxDbiQ2MI91.

Expressioni

Tissue specificityi

Expressed in leaves, ripening and mature fruit.

Developmental stagei

Transcription is reduced upon fruit development; as fruit ripens and chloroplasts differentitate into chromoplasts transcripts increase again. Protein levels also increase in chromoplasts (at protein level).1 Publication

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

Protein-protein interaction databases

STRINGi4081.Solyc01g007340.2.1.

Structurei

3D structure databases

SMRiQ2MI91.
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

eggNOGiENOG410IN75. Eukaryota.
COG0777. LUCA.
InParanoidiQ2MI91.
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.
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.

Q2MI91-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERWWFNSML FKKEFERRCG LNKSMGSLGP IENTSEDPNL KVKNIHSCSN
60 70 80 90 100
VDYLFGVKDI WNFISNDTFL VSDRNGDSYS IYFDIENHIF EVDNDHSFLS
110 120 130 140 150
ELESSFYSYR NSSYLNNGFR GEDPYYNSYM SYMYDTQYSW NNHINSCIDN
160 170 180 190 200
YLQSQICIDT SIISGSESNG DSYIYRAICS GQSLNSSENE GSSRRTRTKD
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
QNLPLMIVCA 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):55,674
Last modified:January 20, 2009 - v2
Checksum:i7F80CA6C3C9AEBC4
GO

Sequence cautioni

The sequence ABC56309 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAJ32402 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ347959 Genomic DNA. Translation: ABC56309.1. Different initiation.
AM087200 Genomic DNA. Translation: CAJ32402.1. Different initiation.
RefSeqiAP_004937.1. AC_000188.1.
XP_004228575.1. XM_004228527.3.
YP_008563097.1. NC_007898.3.

Genome annotation databases

GeneIDi101258479.
3950389.
KEGGisly:101258479.
sly:3950389.

Similar proteinsi

Entry informationi

Entry nameiACCD_SOLLC
AccessioniPrimary (citable) accession number: Q2MI91
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: January 20, 2009
Last modified: May 10, 2017
This is version 60 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families