AC   MF_01395;
DC   Protein; auto
TR   HAMAP; MF_01395; -; 1; level=0
XX
Names: AcetylCoA_CT_beta
XX
ID   ACCD
case <OG:Chloroplast>
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic;
DE            Short=ACCase subunit beta;
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta;
DE            EC=2.1.3.15;
GN   Name=accD;
else
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta;
DE            Short=ACCase subunit beta;
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta;
DE            EC=2.1.3.15;
GN   Name=accD;
end case
XX
CC   -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC       Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its
CC       carrier protein (BCCP) and then the CO(2) group is transferred by the
CC       transcarboxylase to acetyl-CoA to form malonyl-CoA.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC         CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC         Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
end case
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1.
case <OG:Chloroplast>
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC       carboxyl carrier protein, biotin carboxylase and two subunits each of
CC       ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
else
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC       carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC       subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta
CC       (AccD).
end case
case <OC:Bacteria>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
else case <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
end case
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family.
XX
DR   PROSITE; PS50980; COA_CT_NTER; 1; trigger=yes
DR   Pfam; PF01039; Carboxyl_trans; 1; trigger=no
DR   PRINTS; PR01070; ACCCTRFRASEB; 1; trigger=no
DR   NCBIfam; TIGR00515; AccD; 1; trigger=no
XX
KW   ATP-binding
KW   Fatty acid biosynthesis
KW   Fatty acid metabolism
KW   Lipid biosynthesis
KW   Lipid metabolism
KW   Nucleotide-binding
KW   Transferase
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
KW   Zinc-finger
end case
case <OC:Bacteria>
KW   Cytoplasm
end case
XX
GO   GO:0016743; F:carboxyl- or carbamoyltransferase activity
GO   GO:0006633; P:fatty acid biosynthetic process
case <OC:Bacteria>
GO   GO:0005737; C:cytoplasm
else case <OG:Chloroplast>
GO   GO:0009570; C:chloroplast stroma
end case
case <FTGroup:1>
GO   GO:0008270; F:zinc ion binding
end case
XX
FT   From: ACCD_ECOLI (P0A9Q5)
case not <OC:Mycobacterium>
FT   ZN_FING         27..49
FT                   /note="C4-type"
FT   Optional; Condition: C-x(1,2)-C-x(12,18)-C-x(1,2)-C
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: C
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: C
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: C
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: C
end case
XX
case <OC:Bacteria>
Size: 254-346;
end case
case <OG:Chloroplast>
Size: 288-700;
end case
Related: None;
Template: P0A9Q5; Q5HF73; Q2MI91; P18823;
Scope:
 Bacteria
 Plastid
Fusion:
 Nter: None
 Cter: MF_00823 (accA)
Duplicate: in EUBE2, LACPJ, LACPL, LYSSC, ROSCS, ROSS1, VIBC1, VIBPA
Plasmid: in EUBE2
Comments: A few Bacillota encode a fusion between AccD and AccA (CLOTE,
 EUBR3, FRAAA, FRACC, FRASN, NATTJ) as do a few Actinomycetota (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.
XX
# Revision 1.24 2023/06/01
//