| Accession |
MF_00446 |
| Dates |
1-JUN-2001 (Created) 4-DEC-2008 (Last updated, Version 26) |
| Protein name |
| RecName: |
Full=Aspartate 1-decarboxylase; EC=4.1.1.11; |
| AltName: |
Full=Aspartate alpha-decarboxylase; |
| RecName: |
Full=Aspartate 1-decarboxylase beta chain; |
| RecName: |
Full=Aspartate 1-decarboxylase alpha chain; |
| Flags: |
Precursor; |
|
FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine (By similarity).
CATALYTIC ACTIVITY: L-aspartate = beta-alanine + CO(2).
COFACTOR: Pyruvoyl group (By similarity).
PATHWAY: Cofactor biosynthesis; pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
SUBUNIT: Heterooctamer of four alpha and four beta subunits (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus (By similarity).
SIMILARITY: Belongs to the panD family.
GO:0004068; Molecular function: aspartate 1-decarboxylase activity.
GO:0015940; Biological process: pantothenate biosynthetic process.
GO:0005737; Cellular component: cytoplasm.
| From: PAND_ECOLI (P0A790) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| CHAIN |
|
Nter |
|
24 |
|
Aspartate 1-decarboxylase beta chain (By similarity) |
|
|
|
|
| CHAIN |
|
25 |
|
Cter |
|
Aspartate 1-decarboxylase alpha chain (By similarity) |
|
|
|
|
| REGION |
|
73 |
|
75 |
|
Substrate binding (By similarity) |
|
G-[AGS]-[AT] |
|
|
| ACT_SITE |
|
25 |
|
25 |
|
Schiff-base intermediate with substrate; via pyruvic acid (By similarity) |
|
S |
|
|
| ACT_SITE |
|
58 |
|
58 |
|
Proton donor (By similarity) |
|
Y |
|
|
| BINDING |
|
57 |
|
57 |
|
Substrate (By similarity) |
|
T |
|
|
| MOD_RES |
|
25 |
|
25 |
|
Pyruvic acid (Ser) (By similarity) |
|
S |
|
|
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