ID PANC_FRATT Reviewed; 261 AA. AC Q5NF57; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 97. 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=FTT_1390; OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=177416; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCHU S4 / Schu 4; RX PubMed=15640799; DOI=10.1038/ng1499; RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H., RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D., RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S., RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W., RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.; RT "The complete genome sequence of Francisella tularensis, the causative RT agent of tularemia."; RL Nat. Genet. 37:153-159(2005). 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; AJ749949; CAG46023.1; -; Genomic_DNA. DR RefSeq; WP_003022190.1; NZ_CP010290.1. DR RefSeq; YP_170335.1; NC_006570.2. DR PDB; 3N8H; X-ray; 2.00 A; A/B=1-261. DR PDB; 3QTT; X-ray; 2.60 A; A/B=1-258. DR PDB; 5HG0; X-ray; 2.40 A; A/B=1-261. DR PDBsum; 3N8H; -. DR PDBsum; 3QTT; -. DR PDBsum; 5HG0; -. DR AlphaFoldDB; Q5NF57; -. DR SMR; Q5NF57; -. DR STRING; 177416.FTT_1390; -. DR DNASU; 3191378; -. DR EnsemblBacteria; CAG46023; CAG46023; FTT_1390. DR KEGG; ftu:FTT_1390; -. DR eggNOG; COG0414; Bacteria. DR OrthoDB; 9773087at2; -. DR UniPathway; UPA00028; UER00005. DR EvolutionaryTrace; Q5NF57; -. DR Proteomes; UP000001174; 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 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..261 FT /note="Pantothenate synthetase" FT /id="PRO_0000305450" FT ACT_SITE 36 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 29..36 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 147..150 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 153 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 184..187 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:3N8H" FT HELIX 7..15 FT /evidence="ECO:0007829|PDB:3N8H" FT STRAND 23..28 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 34..46 FT /evidence="ECO:0007829|PDB:3N8H" FT STRAND 48..54 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 64..69 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 74..83 FT /evidence="ECO:0007829|PDB:3N8H" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 94..97 FT /evidence="ECO:0007829|PDB:3N8H" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 117..120 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 124..139 FT /evidence="ECO:0007829|PDB:3N8H" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 151..163 FT /evidence="ECO:0007829|PDB:3N8H" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 186..190 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 193..207 FT /evidence="ECO:0007829|PDB:3N8H" FT HELIX 214..222 FT /evidence="ECO:0007829|PDB:3N8H" FT TURN 223..225 FT /evidence="ECO:0007829|PDB:3N8H" FT STRAND 227..234 FT /evidence="ECO:0007829|PDB:3N8H" FT STRAND 237..244 FT /evidence="ECO:0007829|PDB:3N8H" FT STRAND 247..254 FT /evidence="ECO:0007829|PDB:3N8H" FT TURN 255..257 FT /evidence="ECO:0007829|PDB:3N8H" SQ SEQUENCE 261 AA; 29715 MW; 9EF115B43EDC2FDE CRC64; MIIADNIKQF HSIRNSLIKQ QKIGFVPTMG ALHNGHISLI KKAKSENDVV IVSIFVNPTQ FNNPNDYQTY PNQLQQDIQI LASLDVDVLF NPSEKDIYPD GNLLRIEPKL EIANILEGKS RPGHFSGMLT VVLKLLQITK PNNLYLGEKD YQQVMLIKQL VKDFFINTKI IVCPTQRQPS GLPLSSRNKN LTSTDIEIAN KIYEILRQDD FSNLEELTNK INSTGAKLQY IQKLNNRIFL AFYIGKVRLI DNFLKETGPS C //