ID   PANC_SHELP              Reviewed;         282 AA.
AC   A3QHQ2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Shew_3134;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000606; ABO25000.1; -; Genomic_DNA.
DR   RefSeq; WP_011866930.1; NC_009092.1.
DR   AlphaFoldDB; A3QHQ2; -.
DR   SMR; A3QHQ2; -.
DR   STRING; 323850.Shew_3134; -.
DR   EnsemblBacteria; ABO25000; ABO25000; Shew_3134.
DR   KEGG; slo:Shew_3134; -.
DR   eggNOG; COG0414; Bacteria.
DR   HOGENOM; CLU_047148_0_0_6; -.
DR   OMA; CNHKLEP; -.
DR   OrthoDB; 1661843at2; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000001558; 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; 3.30.1300.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR21299:SF1; PTHR21299:SF1; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR00018; panC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis; Reference proteome.
FT   CHAIN           1..282
FT                   /note="Pantothenate synthetase"
FT                   /id="PRO_0000305547"
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   282 AA;  30921 MW;  C4421AAB5C366BC3 CRC64;
     MYTTQDIAAI RTQVRQWKRA GETVAFVPTM GNLHQGHITL VTEALKRADH VVVSIFVNPM
     QFGQNEDLDA YPRTLAADQA ALEAAGAELL FTPTPAIIYP KGMDKQTFVE VPGLSEELCG
     ASRPGHFRGV ATIVCKLFNI VQPDVALFGK KDFQQLMVIK AMVEDLSLPI EIVGVDTIRE
     SSGLAMSSRN GYLSEAQKQQ AAQLKRTLDE MAEAIAKGQA IPNVVRHAQE QLHQAGFKPD
     YLSVRNAADL REAQDSDKQL VILAAAFMGS TRLIDNLSFE RA