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Annotation rule MF_01395
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General rule information [?]

Accession MF_01395
Dates 27-NOV-2008 (Created)
19-NOV-2019 (Last updated, Version 19)
Name AcetylCoA_CT_beta
Scope
Bacteria
Plastid
Templates P0A9Q5 (ACCD_ECOLI); Q5HF73 (ACCD_STAAC); Q2MI91 (ACCD_SOLLC); P18823 (ACCD_PEA): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
ACCD
case <OG:Chloroplast>
Protein name
RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic;
Short=ACCase subunit beta;
Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta;
EC 2.1.3.15;
Gene name
accD
else
Protein name
RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta;
Short=ACCase subunit beta;
Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta;
EC 2.1.3.15;
Gene name
accD
end case

Comments [?]

Function 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 CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic activity RHEA:54728: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
EC 2.1.3.15
case <FTGroup:1>
Cofactor Zn(2+)
Note: Binds 1 zinc ion per subunit.
end case
Pathway Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
case <OG:Chloroplast>
Subunit Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and two subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
else
Subunit Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD).
end case
case <OC:Bacteria>
Subcellular location Cytoplasm.
else case <OG:Chloroplast>
Subcellular location Plastid, chloroplast stroma.
end case
Similarity Belongs to the AccD/PCCB family.

Keywords [?]

case <FTGroup:1>
end case
case <OC:Bacteria>
end case

Gene Ontology [?]

GO:0016743; Molecular function: carboxyl- or carbamoyltransferase activity.
GO:0006633; Biological process: fatty acid biosynthetic process.
case <OC:Bacteria>
GO:0005737; Cellular component: cytoplasm.
else case <OG:Chloroplast>
GO:0009570; Cellular component: chloroplast stroma.
end case
case <FTGroup:1>
GO:0008270; Molecular function: zinc ion binding.
end case

Cross-references [?]

PROSITE PS50980; COA_CT_NTER; 1; trigger=PRU01136;
Pfam PF01039; Carboxyl_trans; 1;
PRINTS PR01070; ACCCTRFRASEB; 1;
TIGRFAMs TIGR00515; AccD; 1;

Features [?]

case not <OC:Mycobacterium>
From: ACCD_ECOLI (P0A9Q5)
Key     From     To       Description   Tag   Condition   FTGroup
ZN_FING (Optional)     27     49       C4-type     C-x(1,2)-C-x(12,18)-C-x(1,2)-C  
METAL (Optional)     27     27       Zinc     C   1
METAL (Optional)     30     30       Zinc     C   1
METAL (Optional)     46     46       Zinc     C   1
METAL (Optional)     49     49       Zinc     C   1
end case

Additional information [?]

case <OC:Bacteria>
Size range 254-346 amino acids
end case
case <OG:Chloroplast>
Size range 288-700 amino acids
end case
Related rules None
Fusion Nter: None; Cter: MF_00823 (accA)
Comments A few Firmicutes encode a fusion between AccD and AccA (CLOTE, EUBR3, FRAAA, FRACC, FRASN, NATTJ) as do a few Actinobacteria (SACEN, SALAI and SALTO). Most plants have 2 forms, the so-called prokaryotic form in their plastids and the eukaryotic form in the cytoplasm. The prokaryotic form is longer than the one found in bacteria. The grass family (Poaceae) have only the eukaryotic form in both locations and an occasional fragment of the other form which may or may not be expressed (see rice). The eukaryotic form consists of a single large protein in which are fused all 4 subunits that are separate in prokaryotes. Not all proteins are able to bind the zinc. Mycobacteria do not seem to have this particular protein; they have 6 accD paralogues however.