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HAMAP annotation rule: MF_00446

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General rule information

Accession MF_00446
Dates 1-JUN-2001 (Created)
4-DEC-2008 (Last updated, Version 26)
Data class Protein
Predictors HAMAP; MF_00446; [distribution of match scores in UniProtKB];[seed alignment for MF_00446]


Propagated annotation

Identifier, protein and gene names
Identifier PAND
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;
Gene name panD
Comments
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.
Cross-references
Pfam PF02261; Asp_decarbox; 1;
TIGRFAMs TIGR00223; panD; 1;
Keywords
Autocatalytic cleavage, Cytoplasm, Decarboxylase, Lyase, Pantothenate biosynthesis, Pyruvate, Schiff base, Zymogen.
Gene Ontology
GO:0004068; Molecular function: aspartate 1-decarboxylase activity.
GO:0015940; Biological process: pantothenate biosynthetic process.
GO:0005737; Cellular component: cytoplasm.
Features
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  


Additional information

Size range: 111-180 amino acids
Related UniRules: None
Template: P0A790 (PAND_ECOLI); P56065 (PAND_HELPY): [Recover all]
Scope: Bacteria
Archaea
Fusion: Nter: None; Cter: None
Duplicate: in ARTAT, FRASC, GLOVI, POLSJ, RHILO
Plasmid encoded: in ARTAT, RHILO

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UniProtKB rule member sequences



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