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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Lemna minor (Common duckweed)
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 bindingi233ZincUniRule annotation1
Metal bindingi236ZincUniRule annotation1
Metal bindingi252ZincUniRule annotation1
Metal bindingi255ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri233 – 255C4-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
OrganismiLemna minor (Common duckweed)
Taxonomic identifieri4472 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAraceaeLemnoideaeLemna

Subcellular locationi

  • Plastidchloroplast stroma UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003591471 – 491Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST491

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

ProteinModelPortaliA9L9A5.
SMRiA9L9A5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini229 – 491CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST263

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri233 – 255C4-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.

A9L9A5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKLWLNSMF SNGKLEHKYR LSRSMDSLGP IRYSSGSEDP VLNAMDNKVS
60 70 80 90 100
SWNDSGSCNF SNVEHFLDII DIWSFISDDT FLVRDSNGDS FSIYFDIENQ
110 120 130 140 150
IFEIDNDSTF INELESSFSS YLDSSSMNSG SKKSSRYYYR YMYDTQSSWN
160 170 180 190 200
NHINSCIDSY LRYEISIDSY ISGETHNYSD NYVYNFICNE SISGNESRNS
210 220 230 240 250
AIRTSVNGSD FNIRGRSNDL DINKKYRHLW VQCENCYGLN YKQFFRSRLN
260 270 280 290 300
ICEHCGYHLK MSSSERIELL IDPGTWDPLD ENMVSTDPIE FHSEEEPYRD
310 320 330 340 350
RIDSYQKKTG LTEAVQTGIG ELNGIPIAIG VMDFQFMGGS MGSVVGEKIT
360 370 380 390 400
RLIEYATNKS LPVIIVCASG GARMQEGSLS LMQMAKISSA LYNYQLNKKL
410 420 430 440 450
FYVAILTSPT TGGVTASFGM LGDIIIAEPN AYIAFAGKRV IEQTLNKTVP
460 470 480 490
DGSQAAEYLF QKGLFDLIVP RNLLKGVLGE LFQLHGFFPL T
Length:491
Mass (Da):55,585
Last modified:February 5, 2008 - v1
Checksum:iBB66D81F23FEF787
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ400350 Genomic DNA. Translation: ABD48504.1.
RefSeqiYP_001595517.1. NC_010109.1.

Genome annotation databases

GeneIDi5787590.

Similar proteinsi

Entry informationi

Entry nameiACCD_LEMMI
AccessioniPrimary (citable) accession number: A9L9A5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: February 5, 2008
Last modified: May 10, 2017
This is version 44 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