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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Porphyra purpurea (Red seaweed) (Ulva purpurea)
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), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA)
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 bindingi34ZincUniRule annotation1
Metal bindingi37ZincUniRule annotation1
Metal bindingi53ZincUniRule annotation1
Metal bindingi56ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri34 – 56C4-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
OrganismiPorphyra purpurea (Red seaweed) (Ulva purpurea)
Taxonomic identifieri2787 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaBangiophyceaeBangialesBangiaceaePorphyra

Subcellular locationi

  • Plastidchloroplast stroma UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001997931 – 288Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST288

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

ProteinModelPortaliP51198.
SMRiP51198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 288CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST259

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri34 – 56C4-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.

P51198-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSNWPLKK EQSKAHNIKS TKQITIPDGL WVKCFDCGLL MYSKVLKRNL
60 70 80 90 100
KVCPQCSYHF QASSNERIDQ LIDQGSWEPM DVHLISTDPL GFKDQKLYSQ
110 120 130 140 150
RLKDTAFKTS LQDAVQTGVG TMLGQKVCLG IMDFRFMGGS MGSVVGEKLT
160 170 180 190 200
RLLEKATQER LPAIILCASG GARMQEGMLS LMQMAKISSA LEMHKKENLL
210 220 230 240 250
YLSVLTSPTT GGVTASFAML GDLIIAEPKA LIAFAGRRVI EQTIKEDLPD
260 270 280
NFQSSEYLFE HGFLDLIVPR TQLRSKLIQI LHLHTNNN
Length:288
Mass (Da):32,169
Last modified:October 1, 1996 - v1
Checksum:iC2FD4C8A04D8E261
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38804 Genomic DNA. Translation: AAC08084.1.
PIRiS73119.
RefSeqiNP_053808.1. NC_000925.1.

Genome annotation databases

GeneIDi809822.

Similar proteinsi

Entry informationi

Entry nameiACCD_PORPU
AccessioniPrimary (citable) accession number: P51198
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 10, 2017
This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families