ID PANC_CAUVC Reviewed; 285 AA. AC Q9A6C8; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 112. 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=CC_2166; OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=190650; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19089 / CB15; RX PubMed=11259647; DOI=10.1073/pnas.061029298; RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R., RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O., RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.; RT "Complete genome sequence of Caulobacter crescentus."; RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001). 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; AE005673; AAK24137.1; -; Genomic_DNA. DR PIR; E87517; E87517. DR RefSeq; NP_420969.1; NC_002696.2. DR RefSeq; WP_010920027.1; NC_002696.2. DR AlphaFoldDB; Q9A6C8; -. DR SMR; Q9A6C8; -. DR STRING; 190650.CC_2166; -. DR EnsemblBacteria; AAK24137; AAK24137; CC_2166. DR KEGG; ccr:CC_2166; -. DR PATRIC; fig|190650.5.peg.2184; -. DR eggNOG; COG0414; Bacteria. DR HOGENOM; CLU_047148_0_2_5; -. DR BioCyc; CAULO:CC2166-MONOMER; -. DR UniPathway; UPA00028; UER00005. DR Proteomes; UP000001816; 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 3: Inferred from homology; KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; KW Pantothenate biosynthesis; Reference proteome. FT CHAIN 1..285 FT /note="Pantothenate synthetase" FT /id="PRO_0000128218" FT ACT_SITE 40 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 33..40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 64 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 64 FT /ligand="beta-alanine" FT /ligand_id="ChEBI:CHEBI:57966" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 150..153 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 156 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 179 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 187..190 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" SQ SEQUENCE 285 AA; 30052 MW; C5B89BCD51D8DFA8 CRC64; MTSPIIVRTV AEMREHVRAW KAAGQRVAVV PTMGALHEGH LSLVRLAQQH AERVIATVFV NPKQFAPHED FDAYPRGEAA DAEKLALVGC DLLFAPNATE MYAPGFSTLV SVSGVSEPLE GAARPQFFGG VATVVAKLFI QSQADVAVFG EKDYQQLQVV RRMARDLDIP VEIIGAPTAR AEDGLALSSR NAYLSAEERA AAVALPTAMK AAAAAVAQGG PIEDAERSAV AALQAAGFGQ VDYVEIREAS DLSRLGPGPI GEASGRILVA AWLGKTRLID NMAVG //