ID PANC_KORVE Reviewed; 291 AA. AC Q1IHA8; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 87. 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=Acid345_4743; OS Koribacter versatilis (strain Ellin345). OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae; OC Koribacter. OX NCBI_TaxID=204669; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin345; RX PubMed=19201974; DOI=10.1128/aem.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). 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; CP000360; ABF43742.1; -; Genomic_DNA. DR RefSeq; WP_011525538.1; NC_008009.1. DR AlphaFoldDB; Q1IHA8; -. DR SMR; Q1IHA8; -. DR STRING; 204669.Acid345_4743; -. DR EnsemblBacteria; ABF43742; ABF43742; Acid345_4743. DR KEGG; aba:Acid345_4743; -. DR eggNOG; COG0414; Bacteria. DR HOGENOM; CLU_047148_0_0_0; -. DR OrthoDB; 9773087at2; -. DR UniPathway; UPA00028; UER00005. DR Proteomes; UP000002432; 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..291 FT /note="Pantothenate synthetase" FT /id="PRO_0000305381" 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 61 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 61 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 176 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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" SQ SEQUENCE 291 AA; 31878 MW; 5250848795BD6034 CRC64; MRVVRTIAEM QAICRTLHRE GKSIGLVPTM GALHAGHISL VRTARTQNDS VVVSIFVNPI QFGPNEDLAK YPRTFEQDCA QLDHEGVDFV FSPGVEEMYP EGTATFVHVD GLSEKLDGRS RPGHFKGVTT VVSKLFHIIP ADHAYFGQKD AAQVAVIRKM VRDQNFDIDL MICPIVREKD GLALSSRNAY LDPTQRQQAL VLHRALMRVQ MLADTGHTDA YYLAEAGRAV IAEEPGAKLD YLEIVDPNTL EPITEIGKGA LVAVAAQIGN TRLIDNLVLQ AAGNARGPRT S //