ID PANC_THET8 Reviewed; 276 AA. AC Q5SHF5; P83701; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 105. 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=TTHA1775; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT. RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of pantothenate synthetase from Thermus thermophilus RT HB8."; RL Submitted (JUN-2003) to the PDB data bank. 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:0000305|Ref.2}. 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 -!- MISCELLANEOUS: PDB 1UFV apparently has a Val-49-Ala mutation. 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; AP008226; BAD71598.1; -; Genomic_DNA. DR RefSeq; WP_011173797.1; NC_006461.1. DR RefSeq; YP_145041.1; NC_006461.1. DR PDB; 1UFV; X-ray; 2.05 A; A/B=1-276. DR PDB; 1V8F; X-ray; 1.90 A; A/B=1-276. DR PDBsum; 1UFV; -. DR PDBsum; 1V8F; -. DR AlphaFoldDB; Q5SHF5; -. DR SMR; Q5SHF5; -. DR DrugBank; DB03570; Tris-Hydroxymethyl-Methyl-Ammonium. DR EnsemblBacteria; BAD71598; BAD71598; BAD71598. DR GeneID; 3169469; -. DR KEGG; ttj:TTHA1775; -. DR PATRIC; fig|300852.9.peg.1745; -. DR eggNOG; COG0414; Bacteria. DR HOGENOM; CLU_047148_0_0_0; -. DR PhylomeDB; Q5SHF5; -. DR UniPathway; UPA00028; UER00005. DR EvolutionaryTrace; Q5SHF5; -. DR Proteomes; UP000000532; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; KW Pantothenate biosynthesis; Reference proteome. FT CHAIN 1..276 FT /note="Pantothenate synthetase" FT /id="PRO_0000128283" FT ACT_SITE 32 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 25..32 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 56 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 56 FT /ligand="beta-alanine" FT /ligand_id="ChEBI:CHEBI:57966" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 143..146 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 149 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 172 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 180..183 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:1V8F" FT HELIX 7..13 FT /evidence="ECO:0007829|PDB:1V8F" FT STRAND 19..24 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 30..42 FT /evidence="ECO:0007829|PDB:1V8F" FT STRAND 44..50 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:1V8F" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 70..79 FT /evidence="ECO:0007829|PDB:1V8F" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 90..93 FT /evidence="ECO:0007829|PDB:1V8F" FT STRAND 100..104 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 107..110 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 113..116 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 120..135 FT /evidence="ECO:0007829|PDB:1V8F" FT STRAND 138..143 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 147..160 FT /evidence="ECO:0007829|PDB:1V8F" FT STRAND 165..169 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 182..186 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 189..194 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 197..210 FT /evidence="ECO:0007829|PDB:1V8F" FT HELIX 215..226 FT /evidence="ECO:0007829|PDB:1V8F" FT STRAND 233..240 FT /evidence="ECO:0007829|PDB:1V8F" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:1V8F" FT STRAND 256..263 FT /evidence="ECO:0007829|PDB:1V8F" FT STRAND 266..273 FT /evidence="ECO:0007829|PDB:1V8F" SQ SEQUENCE 276 AA; 30695 MW; 975B6B82D162AE40 CRC64; MRTVSTVAEL RAALPREGVG FVPTMGYLHR GHLALVERAR RENPFVVVSV FVNPLQFGPG EDYHRYPRDL ERDRALLQEA GVDLLFAPGV EEMYPEGFAT RVQVEGPLTA LWEGAVRPGH FQGVATVVAR LFLLVQPQRA YFGEKDYQQL LVVRRMVRDL GFPVEVVGVP TVREEDGLAL SSRNVYLSPE TRKKAPVLYR ALLAMREVAG QGGSVAEALR AGEEALRAVP EFRKDYLAIV HPETLLPLSD WVAGARGIVA GRFPEARLID NLEVYP //