ID PANC_RUEPO Reviewed; 285 AA. AC Q5LWR2; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 95. 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=SPO0103; OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter OS pomeroyi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Roseobacteraceae; Ruegeria. OX NCBI_TaxID=246200; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3; RX PubMed=15602564; DOI=10.1038/nature03170; RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M., RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.; RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine RT environment."; RL Nature 432:910-913(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3; RX PubMed=25780504; DOI=10.1186/1944-3277-9-11; RA Rivers A.R., Smith C.B., Moran M.A.; RT "An updated genome annotation for the model marine bacterium Ruegeria RT pomeroyi DSS-3."; RL Stand. Genomic Sci. 9:11-11(2014). 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; CP000031; AAV93434.1; -; Genomic_DNA. DR RefSeq; WP_011045876.1; NC_003911.12. DR AlphaFoldDB; Q5LWR2; -. DR SMR; Q5LWR2; -. DR STRING; 246200.SPO0103; -. DR PaxDb; 246200-SPO0103; -. DR KEGG; sil:SPO0103; -. DR eggNOG; COG0414; Bacteria. DR HOGENOM; CLU_047148_0_0_5; -. DR OrthoDB; 9773087at2; -. DR UniPathway; UPA00028; UER00005. DR Proteomes; UP000001023; 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_0000305555" FT ACT_SITE 39 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 32..39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 63 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 63 FT /ligand="beta-alanine" FT /ligand_id="ChEBI:CHEBI:57966" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 149..152 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 155 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 178 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 186..189 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" SQ SEQUENCE 285 AA; 30411 MW; 1E87D9953E657AD8 CRC64; MSAPILRKLA DLRAATAGWK RAGESIGVVP TMGALHDGHL SLVAAAKAGC DRVVVTIFVN PKQFNNPEDL AKYPRTELAD ASKLAPYGVD AIYVPDPDQI YPEGFATTVS VSGLTDVMEG ACRPGHFDGV ATVVAKLFLQ TGADQAYFGE KDYQQMMLVT RMAQDLDIPI TVVGCPTVRE ASGLAMSSRN MRLSAEGLER AGRLHPVMRQ VAERLAAGAS FGDLAPGARE ALGAAGFVDI EYFDLRAADS LRALDRPTEP ARLLVAAWLD GVRLIDNIAV SQLND //