| Accession |
MF_01395 |
| Dates |
27-NOV-2008 (Created) 12-NOV-2009 (Last updated, Version 4) |
| Protein name |
| RecName: |
Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta; Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta; Short=ACCase subunit beta; EC=6.4.1.2; |
|
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 (By similarity).
CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA.
case <FTGroup:1>
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
end case
PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
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) (By similarity).
case <OC:Bacteria>
SUBCELLULAR LOCATION: Cytoplasm (Probable).
else case <OG:Chloroplast>
SUBCELLULAR LOCATION: Plastid, chloroplast stroma (Probable).
end case
SIMILARITY: Belongs to the accD/PCCB family.
case <FTGroup:1>
end case
case <OC:Bacteria>
end case
GO:0003989; Molecular function: acetyl-CoA carboxylase activity.
GO:0006633; Biological process: fatty acid biosynthetic process.
case <OC:Bacteria>
else case <OG:Chloroplast>
GO:0009570; Cellular component: chloroplast stroma.
end case
case <FTGroup:1>
end case
case not <OC:Mycobacterium>
| From: ACCD_ECOLI (P0A9Q5) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| ZN_FING (Optional) |
|
27 |
|
49 |
|
C4-type (By similarity) |
|
C-x(1,2)-C-x(12,18)-C-x(1,2)-C |
|
|
| |
| METAL (Optional) |
|
27 |
|
27 |
|
Zinc (By similarity) |
|
C |
|
1 |
| METAL (Optional) |
|
30 |
|
30 |
|
Zinc (By similarity) |
|
C |
|
1 |
| METAL (Optional) |
|
46 |
|
46 |
|
Zinc (By similarity) |
|
C |
|
1 |
| METAL (Optional) |
|
49 |
|
49 |
|
Zinc (By similarity) |
|
C |
|
1 |
end case
case <OC:Bacteria>
| Size range: |
254-346 amino acids |
end case
case <OG:Chloroplast>
| Size range: |
288-700 amino acids |
end case
| Related UniRules: |
None |
| Template: |
P0A9Q5 (ACCD_ECOLI); Q5HF73 (ACCD_STAAC); Q2MI91 (ACCD_SOLLC); P18823 (ACCD_PEA): [Recover all] |
| Scope: |
Bacteria
Plastid |
| Fusion: |
Nter: None; Cter: MF_00823 (accA) |
| Duplicate: |
in EUBE2, LACPJ, LACPL, LYSSC, ROSCS, ROSS1, VIBHB, VIBPA |
| Plasmid encoded: |
in EUBE2 |
| Comments: |
A few Firmicutes encode a fusion between accD and accA (CLOTE, EUBR3, FRAAA, FRASC, 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. |
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