AC   MF_00446;
DC   Protein; auto
TR   HAMAP; MF_00446; -; 1; level=0
XX
Names: PanD
XX
ID   PAND
DE   RecName: Full=Aspartate 1-decarboxylase;
DE            EC=4.1.1.11;
DE   AltName: Full=Aspartate alpha-decarboxylase;
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase beta chain;
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase alpha chain;
DE   Flags: Precursor;
GN   Name=panD;
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CC   -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate
CC       to produce beta-alanine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:57966; EC=4.1.1.11;
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC       Note=Binds 1 pyruvoyl group covalently per subunit.;
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-
CC       alanine from L-aspartate: step 1/1.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme, which is
CC       activated by self-cleavage at a specific serine bond to produce a beta-
CC       subunit with a hydroxyl group at its C-terminus and an alpha-subunit
CC       with a pyruvoyl group at its N-terminus.
CC   -!- SIMILARITY: Belongs to the PanD family.
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DR   Pfam; PF02261; Asp_decarbox; 1; trigger=no
DR   NCBIfam; TIGR00223; PanD; 1; trigger=no
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KW   Autocatalytic cleavage
KW   Cytoplasm
KW   Decarboxylase
KW   Lyase
KW   Pantothenate biosynthesis
KW   Pyruvate
KW   Schiff base
KW   Zymogen
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GO   GO:0004068; F:aspartate 1-decarboxylase activity
GO   GO:0015940; P:pantothenate biosynthetic process
GO   GO:0005737; C:cytoplasm
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FT   From: PAND_ECOLI (P0A790)
FT   CHAIN           Nter..24
FT                   /note="Aspartate 1-decarboxylase beta chain"
FT   CHAIN           25..Cter
FT                   /note="Aspartate 1-decarboxylase alpha chain"
FT   BINDING         73..75
FT                   /ligand="substrate"
FT   Condition: G-[AGPS]-[AT]
FT   ACT_SITE        25
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT   Condition: S
FT   ACT_SITE        58
FT                   /note="Proton donor"
FT   Condition: Y
FT   BINDING         57
FT                   /ligand="substrate"
FT   Condition: T
FT   MOD_RES         25
FT                   /note="Pyruvic acid (Ser)"
FT   Condition: S
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Size: 111-180;
Related: None;
Template: P0A790; P56065;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in PAEAT, FRACC, GLOVI, POLSJ, RHILO
Plasmid: in PAEAT, RHILO
Comments: None
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# Revision 1.41 2023/06/01
//