AC   MF_00158;
DC   Protein; auto
TR   HAMAP; MF_00158; -; 1; level=0
XX
Names: PanC
XX
ID   PANC
DE   RecName: Full=Pantothenate synthetase;
DE            Short=PS;
DE            EC=6.3.2.1;
DE   AltName: Full=Pantoate--beta-alanine ligase;
DE   AltName: Full=Pantoate-activating enzyme;
GN   Name=panC;
XX
CC   -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in
CC       an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP +
CC         diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1;
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong
CC       mechanism.
CC   -!- SIMILARITY: Belongs to the pantothenate synthetase family.
XX
DR   Pfam; PF02569; Pantoate_ligase; 1; trigger=no
DR   NCBIfam; TIGR00018; PanC; 1; trigger=no
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KW   ATP-binding
KW   Cytoplasm
KW   Ligase
KW   Nucleotide-binding
KW   Pantothenate biosynthesis
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GO   GO:0004592; F:pantoate-beta-alanine ligase activity
GO   GO:0015940; P:pantothenate biosynthetic process
GO   GO:0005737; C:cytoplasm
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FT   From: PANC_MYCTU (P9WIL5)
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: M-x(3)-H-x(2)-H
FT   BINDING         158..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-x(2)-D
FT   BINDING         195..198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: x(3)-R
FT   ACT_SITE        47
FT                   /note="Proton donor"
FT   Condition: H
FT   BINDING         72
FT                   /ligand="beta-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57966"
FT   Condition: Q
FT   BINDING         72
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT   Condition: Q
FT   BINDING         164
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT   Condition: Q
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: [VLIGA]
XX
Size: 251-337;
Related: MF_01349!;
Template: P31663; P9WIL5; Q9X713;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in BRADU, FRAAA
Plasmid: in RHIEC, RHIJ3, RUEST
Comments: In Cyanobacteriota this protein is fused C-terminally to
 cytidylate kinase (see Bifunctional pantoate ligase/cytidylate kinase MF_01349).
 Possible sequence error in STRCO; weird insertion; not shown in alignment.
XX
# Revision 1.35 2023/11/28
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