ID   PANC_SALTY              Reviewed;         284 AA.
AC   Q8ZRR1;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Pantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_00158};
DE            Short=PS {ECO:0000255|HAMAP-Rule:MF_00158};
DE            EC=6.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00158};
DE   AltName: Full=Pantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00158};
DE   AltName: Full=Pantoate-activating enzyme {ECO:0000255|HAMAP-Rule:MF_00158};
GN   Name=panC {ECO:0000255|HAMAP-Rule:MF_00158};
GN   OrderedLocusNames=STM0181;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in
CC       an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC       {ECO:0000255|HAMAP-Rule:MF_00158}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00158};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong
CC       mechanism. {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00158}.
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DR   EMBL; AE006468; AAL19145.1; -; Genomic_DNA.
DR   RefSeq; NP_459186.1; NC_003197.2.
DR   RefSeq; WP_000905344.1; NC_003197.2.
DR   PDB; 3MUE; X-ray; 2.70 A; A/B/C/D=1-284.
DR   PDBsum; 3MUE; -.
DR   AlphaFoldDB; Q8ZRR1; -.
DR   SMR; Q8ZRR1; -.
DR   STRING; 99287.STM0181; -.
DR   PaxDb; 99287-STM0181; -.
DR   GeneID; 1251699; -.
DR   KEGG; stm:STM0181; -.
DR   PATRIC; fig|99287.12.peg.191; -.
DR   HOGENOM; CLU_047148_0_0_6; -.
DR   OMA; CNHKLEP; -.
DR   PhylomeDB; Q8ZRR1; -.
DR   BioCyc; SENT99287:STM0181-MONOMER; -.
DR   UniPathway; UPA00028; UER00005.
DR   EvolutionaryTrace; Q8ZRR1; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IBA:GO_Central.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IBA:GO_Central.
DR   CDD; cd00560; PanC; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.30.1300.10; Pantoate-beta-alanine ligase, C-terminal domain; 1.
DR   HAMAP; MF_00158; PanC; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR003721; Pantoate_ligase.
DR   InterPro; IPR042176; Pantoate_ligase_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   NCBIfam; TIGR00018; panC; 1.
DR   PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1.
DR   PANTHER; PTHR21299:SF1; PANTOATE--BETA-ALANINE LIGASE; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis; Reference proteome.
FT   CHAIN           1..284
FT                   /note="Pantothenate synthetase"
FT                   /id="PRO_0000128266"
FT   ACT_SITE        37
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         61
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         61
FT                   /ligand="beta-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57966"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         149..152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         155
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         186..189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           7..19
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           35..47
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           65..69
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           75..84
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   STRAND          88..91
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           95..98
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   TURN            112..116
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           118..122
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           126..141
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   STRAND          144..149
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           153..165
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   STRAND          171..175
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           189..191
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           195..200
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           203..216
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   HELIX           222..236
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   STRAND          239..247
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   TURN            248..250
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   STRAND          259..269
FT                   /evidence="ECO:0007829|PDB:3MUE"
FT   STRAND          272..281
FT                   /evidence="ECO:0007829|PDB:3MUE"
SQ   SEQUENCE   284 AA;  31858 MW;  219D5B538BE37E1D CRC64;
     MLIIETLPLL RQHIRRLRQE GKRVALVPTM GNLHDGHMKL VDEAKARADV VIVSIFVNPM
     QFDRPDDLVR YPRTLQEDCE KLNKRKVDYV FAPAVEEIYP HGLEGQTYVD VPGLSTMLEG
     ASRPGHFRGV STIVSKLFNL IQPDIACFGE KDFQQLALIR KMVADMSYDI EIVGVPIIRA
     KDGLALSSRN AYLTAEQRKI APGLYNVMNS IAEKLIAGNR ELQEIIAIAE QELNEKGFRA
     DDIQIRDADT LLELTETSKR AVILAAAWLG QARLIDNQSV TLAQ
//