ID   PANC_SALG2              Reviewed;         284 AA.
AC   B5RHC0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
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}; OrderedLocusNames=SG0185;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM933173; CAR36092.1; -; Genomic_DNA.
DR   RefSeq; WP_000905348.1; NC_011274.1.
DR   AlphaFoldDB; B5RHC0; -.
DR   SMR; B5RHC0; -.
DR   KEGG; seg:SG0185; -.
DR   HOGENOM; CLU_047148_0_0_6; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000008321; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis.
FT   CHAIN           1..284
FT                   /note="Pantothenate synthetase"
FT                   /id="PRO_1000097101"
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"
SQ   SEQUENCE   284 AA;  31864 MW;  F87D729DA2E36717 CRC64;
     MLIIETLPLL RQHIRRLRQE GKRVALVPTM GNLHDGHMKL VDEAKARADV VIVSIFVNPM
     QFDRPDDLVR YPRTLQEDCE KLNKRKVDYV FAPAVEEIYP QGLEGQTYVD VPGLSTMLEG
     ASRPGHFRGV STIVSKLFNL IQPDIACFGE KDFQQLALIR KMVADMSYDI EIVGVPIIRA
     KDGLALSSRN AYLTAEQRKI APGLYNVMNS IAEKLIAGNR ELQEIIAIAE QELNEKGFRA
     DDIQIRDADT LQELTETSKR AVILAAAWLG QARLIDNQSV TLAQ
//