ID   PANC_CAMJE              Reviewed;         282 AA.
AC   Q9PIK2; Q0PBL2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   27-MAR-2024, entry version 121.
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=Cj0297c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 11168).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL34448.1; -; Genomic_DNA.
DR   PIR; E81448; E81448.
DR   RefSeq; WP_002778123.1; NZ_SZUC01000004.1.
DR   RefSeq; YP_002343735.1; NC_002163.1.
DR   PDB; 3MXT; X-ray; 1.85 A; A=1-282.
DR   PDB; 3UY4; X-ray; 1.85 A; A=1-282.
DR   PDBsum; 3MXT; -.
DR   PDBsum; 3UY4; -.
DR   AlphaFoldDB; Q9PIK2; -.
DR   SMR; Q9PIK2; -.
DR   IntAct; Q9PIK2; 30.
DR   STRING; 192222.Cj0297c; -.
DR   PaxDb; 192222-Cj0297c; -.
DR   EnsemblBacteria; CAL34448; CAL34448; Cj0297c.
DR   GeneID; 66544703; -.
DR   GeneID; 904621; -.
DR   KEGG; cje:Cj0297c; -.
DR   PATRIC; fig|192222.6.peg.289; -.
DR   eggNOG; COG0414; Bacteria.
DR   HOGENOM; CLU_047148_0_0_7; -.
DR   OrthoDB; 9773087at2; -.
DR   UniPathway; UPA00028; UER00005.
DR   EvolutionaryTrace; Q9PIK2; -.
DR   Proteomes; UP000000799; 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; IPR003721; Pantoate_ligase.
DR   InterPro; IPR042176; Pantoate_ligase_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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..282
FT                   /note="Pantothenate synthetase"
FT                   /id="PRO_0000128216"
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         60
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         60
FT                   /ligand="beta-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57966"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         146..149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         152
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         183..186
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:3MXT"
FT   HELIX           7..19
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   HELIX           35..44
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   STRAND          47..54
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   TURN            67..69
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   HELIX           74..83
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   HELIX           94..97
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   HELIX           115..119
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   HELIX           123..138
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   STRAND          141..146
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   HELIX           147..149
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   HELIX           150..162
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   STRAND          166..172
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   HELIX           185..189
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   HELIX           192..213
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   HELIX           219..231
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   STRAND          236..244
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   TURN            246..248
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   STRAND          259..267
FT                   /evidence="ECO:0007829|PDB:3MXT"
FT   STRAND          270..278
FT                   /evidence="ECO:0007829|PDB:3MXT"
SQ   SEQUENCE   282 AA;  32087 MW;  C8946F933D7B6475 CRC64;
     MQVITSVKEA KQIVKDWKSH QLSIGYVPTM GFLHDGHLSL VKHAKTQDKV IVSIFVNPMQ
     FGPNEDFSSY PRDLERDIKM CQDNGVDMVF IPDATQMYLK NFSTYVDMNT ITDKLCGAKR
     PGHFRGVCTV LTKFFNILNP DIVYMGQKDA QQCVVVRHMV DDLNFDLKIQ ICPIIREEDG
     LAKSSRNVYL SKEERKASLA ISQSIFLAEK LVREGEKNTS KIIQAMKDIL EKEKLIKIDY
     IELVDFNTME NIENITDNVL GAVAAFVGKT RLIDNFLVQG LK
//