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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Ceratophyllum demersum (Rigid hornwort) (Coontail)
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 bindingi226ZincUniRule annotation1
Metal bindingi229ZincUniRule annotation1
Metal bindingi245ZincUniRule annotation1
Metal bindingi248ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri226 – 248C4-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
OrganismiCeratophyllum demersum (Rigid hornwort) (Coontail)
Taxonomic identifieri4428 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaCeratophyllalesCeratophyllaceaeCeratophyllum

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_00003591281 – 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

SMRiA8SEB2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini222 – 491CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST270

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri226 – 248C4-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.

A8SEB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKWWFNLIL SNEELEHRCR LSKSMARPRP IGNTNGSQDP SINDRDKNGS
60 70 80 90 100
DSGNYSFSNL DHLFDVKDNL SFIYDDTFLV RDSNGDSYSI YFDIENLIFE
110 120 130 140 150
IDNDSFFLSK LESSFSNYLN SGSKNYNRYY DSYMYDTKYS WNNHINSYID
160 170 180 190 200
SYLCSEIRID SYISSGIYNY SENYIYSYVW NGENVSTIKS RSSSIRTSAN
210 220 230 240 250
SSDINLKGRY NDFDINIKYR HLWVQCDNCY GLNYKKIFSS KMNICEQCGY
260 270 280 290 300
HLKMSSSERI ELSIDSGTWD PMNEDMVSTD PIEFHSEEEP YRDRIDSYQI
310 320 330 340 350
KTGLTEAVQT GIGQLNGMPI AIGVMDFQFM GGSMGSVVGE KITRLIEYAT
360 370 380 390 400
NRSLPVIIVC ASGGARMQEG SLSLMQMAKI SSALYNYQLN KKLFYVSILT
410 420 430 440 450
SPTTGGVTAS FGMLGDIIIA EPNAYIAFAG KRVIEQTLNK TVPEGSQAAE
460 470 480 490
YSFHKGLFDS IVPRNLLKGA LSELLQLHGF FPLNHNSQVK R
Length:491
Mass (Da):55,871
Last modified:January 20, 2009 - v2
Checksum:iD4A32B0F63690A5C
GO

Sequence cautioni

The sequence ABQ81459 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF614270 Genomic DNA Translation: ABQ81459.1 Different initiation.
RefSeqiYP_001542456.1, NC_009962.1

Genome annotation databases

GeneIDi5729449

Similar proteinsi

Entry informationi

Entry nameiACCD_CERDE
AccessioniPrimary (citable) accession number: A8SEB2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: May 23, 2018
This is version 39 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

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