PANC_CAMJE
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 03-AUG-2022, entry version 113.
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=Cj0297c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; 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}.
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DR EMBL; AL111168; CAL34448.1; -; Genomic_DNA.
DR PIR; E81448; E81448.
DR RefSeq; WP_002778123.1; NC_002163.1.
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; Q9PIK2; -.
DR PRIDE; Q9PIK2; -.
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 OMA; CNHKLEP; -.
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; 3.30.1300.10; -; 1.
DR Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR21299:SF1; PTHR21299:SF1; 1.
DR Pfam; PF02569; Pantoate_ligase; 1.
DR TIGRFAMs; TIGR00018; panC; 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
