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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Oenothera elata subsp. hookeri (Hooker's evening primrose) (Oenothera hookeri)
Status
Reviewed-Annotation score: -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

[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 bindingi247ZincUniRule annotation1
Metal bindingi250ZincUniRule annotation1
Metal bindingi266ZincUniRule annotation1
Metal bindingi269ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri247 – 269C4-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
OrganismiOenothera elata subsp. hookeri (Hooker's evening primrose) (Oenothera hookeri)
Taxonomic identifieri85636 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsMyrtalesOnagraceaeOnagroideaeOnagreaeOenothera

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_00001997871 – 517Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST517

Proteomic databases

PRIDEiQ9MTL3

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

ProteinModelPortaliQ9MTL3
SMRiQ9MTL3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini243 – 514CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST272

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri247 – 269C4-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_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.

Q9MTL3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPTKPEGPK KPNKSNEEAE ELEGDNKEDL EGPKKPNKSN EEAEELEGDN
60 70 80 90 100
KEDLEGPKKP NKSNEEAEEL EGDKQKDKKD GIFVLNYDDE YEEDLEYDDE
110 120 130 140 150
YEEDLEYDDE YEEDLEYDDE EYDDEYEEDL EGDNKPHKED LEGDNKPHKE
160 170 180 190 200
DLEGDNKPHK EDLEGDKQKE EEEKQKEEEE KLKDCPWHWF HQIYPKHWGC
210 220 230 240 250
PHRKHRDRKS VPAKERELVP AQSTKRDTDP DSEASLKSNY AHLWVHCKLC
260 270 280 290 300
SGFNYKKILK SKNNVCEQCG SHLKMHSSDR IDLMLDPKTW APMHEGLLSL
310 320 330 340 350
DPIEFHSEKD PYKDRVASYK RKTGLSEAIQ TGRGYLKRIH LGIGLMDFQF
360 370 380 390 400
MGGSMGSVVG ERITRLVEYA TNRVLPLILV CASGGARMQE GSLSLMQMAK
410 420 430 440 450
ISSALSDYQF NRTVFYVALL TSPTTGGVTA SFGMLGDIIL AEPNAYIAFA
460 470 480 490 500
GKRVIEQTLN IEVPEGSQTA EYLFDKGLFD QIVPRNPLKG SLSELFNFHG
510
FVTLNSQVIN IYNYLYS
Length:517
Mass (Da):59,318
Last modified:March 18, 2008 - v2
Checksum:i10B67C3400C24C60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ271079 Genomic DNA Translation: CAB67165.2
RefSeqiNP_084700.2, NC_002693.2

Genome annotation databases

GeneIDi802793

Entry informationi

Entry nameiACCD_OENEH
AccessioniPrimary (citable) accession number: Q9MTL3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 6, 2003
Last sequence update: March 18, 2008
Last modified: May 23, 2018
This is version 82 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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