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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Anthoceros angustus (Hornwort) (Anthoceros formosae)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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.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)
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 bindingi51ZincUniRule annotation1
Metal bindingi54ZincUniRule annotation1
Metal bindingi70ZincUniRule annotation1
Metal bindingi73ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri51 – 73C4-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
OrganismiAnthoceros angustus (Hornwort) (Anthoceros formosae)
Taxonomic identifieri48387 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaAnthocerotophytaAnthocerotopsidaAnthocerotidaeAnthocerotalesAnthocerotaceaeAnthoceros

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_00001997791 – 313Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST313

Proteomic databases

PRIDEiQ31796

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

ProteinModelPortaliQ31796
SMRiQ31796
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 313CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST267

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri51 – 73C4-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.

Q31796-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLMNWFEDR RKFSGLIGAF IEKATKGYIL SERRKDRHIK IDTTKGLWTR
60 70 80 90 100
CDNCENMLYI RFLRQNKRIC EECGYHLQMS STERIESLID RGTWHPMDED
110 120 130 140 150
MVARDALKFS DEDSYKNRVL FYQKRTGLTD AIQTGIGKLN GIPIALGVMD
160 170 180 190 200
FQFMGGSMGS VVGEKITRLI EYGTRESMPV IIVCSSGGAR MQEGTLSLMQ
210 220 230 240 250
MAKISAVLQI HQAQKKLLYI AILTYPTTGG VTASFGMLGD VIIAEPKAYI
260 270 280 290 300
AFAGKRVIEQ TLRQKIPDGS QVAESLFDHG LLDLIVPRNL LRGVLSEIFE
310
LYSSAPCRRS NNS
Length:313
Mass (Da):35,272
Last modified:February 28, 2003 - v2
Checksum:i6881B7B5FF780126
GO

RNA editingi

Edited at positions 50, 59, 78, 87, 104, 132, 139, 146, 149, 160, 170, 177, 185, 198, 208, 223, 226, 228, 243, 246, 252, 260, 264, 277, 285 and 295.2 Publications
The nonsense codons at positions 50, 78, 104, 260 and 264 are modified to sense codons.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB086179 Genomic DNA Translation: BAC55358.1
AB087450 mRNA Translation: BAC55454.1
D43695 Genomic DNA Translation: BAA07797.1 Sequence problems.
PIRiS71147
RefSeqiNP_777422.1, NC_004543.1

Genome annotation databases

GeneIDi2553479

Keywords - Coding sequence diversityi

RNA editing

Similar proteinsi

Entry informationi

Entry nameiACCD_ANTAG
AccessioniPrimary (citable) accession number: Q31796
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 28, 2003
Last modified: July 18, 2018
This is version 90 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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