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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Lactuca sativa (Garden lettuce)
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 bindingi248ZincUniRule annotation1
Metal bindingi251ZincUniRule annotation1
Metal bindingi267ZincUniRule annotation1
Metal bindingi270ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri248 – 270C4-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
OrganismiLactuca sativa (Garden lettuce)
Taxonomic identifieri4236 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeCichorioideaeCichorieaeLactucinaeLactuca

Subcellular locationi

  • Plastidchloroplast stroma UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003591461 – 508Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST508

Proteomic databases

PRIDEiQ332W9.

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

SMRiQ332W9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini244 – 508CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST265

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri248 – 270C4-typeUniRule annotationAdd BLAST23

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.

Q332W9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRWWFNSML FKKEFEHRCR LSKSMGSLGP IENASESKDP NRNDTDKNIQ
60 70 80 90 100
GWGGHDNYSN VDLFFGVKDI RNFFSDDTFL VKDSNGDSYS IYFDIENHIF
110 120 130 140 150
EIANDHPFCS ELESSFYRNS SDLNNGSKSK NPDHDRYMDD TQYTWNNHIN
160 170 180 190 200
SCIDSYLQYQ ICIDNYIVSG NDNSSNNNSS NENSSNENSS NENSSNENSS
210 220 230 240 250
NDYISSSISS QSENSSQNED ITTSDQTIPE SSTHMGVTQQ YRHLWVQCEN
260 270 280 290 300
CYGLNYKKFF KSKMHLCEQC GYHLKMSSSD RIELLIDPGT WEPMDEDMVS
310 320 330 340 350
LDPIEFHSEE EPYKNRIDSY QRNTGLTEAV QTGRGQLNGI TVAIGVMDFQ
360 370 380 390 400
FMGGSMGSVV GEKITRLIEY ATKEFLPLII VCASGGARMQ EGSVSLMQMA
410 420 430 440 450
KISSALYDYQ SNKKLFYVPI LTSPTTGGVT ASFGMLGDII IAEPNAYIAF
460 470 480 490 500
AGKRVIEQTL NKTVPEGSQA AEYLFQKGLF DLIVPRNPLK SVLSELFQLH

TFFPLNQN
Length:508
Mass (Da):57,502
Last modified:January 20, 2009 - v2
Checksum:iF666A233170B0852
GO

Sequence cautioni

The sequence ABD47242 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAE47603 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ383816 Genomic DNA. Translation: ABD47242.1. Different initiation.
AP007232 Genomic DNA. Translation: BAE47603.1. Different initiation.
RefSeqiYP_398338.1. NC_007578.1.

Genome annotation databases

GeneIDi3772810.

Similar proteinsi

Entry informationi

Entry nameiACCD_LACSA
AccessioniPrimary (citable) accession number: Q332W9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: May 10, 2017
This is version 46 of the entry and version 2 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