ID PANCY_PROMA Reviewed; 519 AA. AC Q7V9S8; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 14-DEC-2022, entry version 99. DE RecName: Full=Bifunctional pantoate ligase/cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_01349}; DE Includes: DE RecName: Full=Pantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_01349}; DE Short=PS {ECO:0000255|HAMAP-Rule:MF_01349}; DE EC=6.3.2.1 {ECO:0000255|HAMAP-Rule:MF_01349}; DE AltName: Full=Pantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_01349}; DE AltName: Full=Pantoate-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01349}; DE Includes: DE RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_01349}; DE Short=CK {ECO:0000255|HAMAP-Rule:MF_01349}; DE EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_01349}; DE AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_01349}; DE Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_01349}; GN Name=panC/cmk {ECO:0000255|HAMAP-Rule:MF_01349}; GN OrderedLocusNames=Pro_1746; OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120). OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=167539; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SARG / CCMP1375 / SS120; RX PubMed=12917486; DOI=10.1073/pnas.1733211100; RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.; RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a RT nearly minimal oxyphototrophic genome."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003). 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_01349}. CC -!- FUNCTION: Catalyzes the transfer of a phosphate group from ATP to CC either CMP or dCMP to form CDP or dCDP and ADP, respectively. CC {ECO:0000255|HAMAP-Rule:MF_01349}. 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_01349}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01349}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, CC ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01349}; 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_01349}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01349}. CC -!- SIMILARITY: In the N-terminal section; belongs to the pantothenate CC synthetase family. {ECO:0000255|HAMAP-Rule:MF_01349}. CC -!- SIMILARITY: In the C-terminal section; belongs to the cytidylate kinase CC family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01349}. 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; AE017126; AAQ00790.1; -; Genomic_DNA. DR RefSeq; NP_876137.1; NC_005042.1. DR RefSeq; WP_011125895.1; NC_005042.1. DR AlphaFoldDB; Q7V9S8; -. DR SMR; Q7V9S8; -. DR STRING; 167539.Pro_1746; -. DR EnsemblBacteria; AAQ00790; AAQ00790; Pro_1746. DR GeneID; 54201073; -. DR KEGG; pma:Pro_1746; -. DR PATRIC; fig|167539.5.peg.1844; -. DR eggNOG; COG0283; Bacteria. DR eggNOG; COG0414; Bacteria. DR HOGENOM; CLU_037427_0_0_3; -. DR OMA; IDHVFLM; -. DR OrthoDB; 1661843at2; -. DR UniPathway; UPA00028; UER00005. DR Proteomes; UP000001420; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA. DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA. 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd02020; CMPK; 1. DR CDD; cd00560; PanC; 1. DR Gene3D; 3.30.1300.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00238; Cytidyl_kinase_type1; 1. DR HAMAP; MF_00158; PanC; 1. DR HAMAP; MF_01349; PanCY; 1. DR InterPro; IPR003136; Cytidylate_kin. DR InterPro; IPR011994; Cytidylate_kinase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003721; Pantoate_ligase. DR InterPro; IPR024894; Pantoate_ligase/cytidylate_kin. DR InterPro; IPR042176; Pantoate_ligase_C. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF02224; Cytidylate_kin; 1. DR Pfam; PF02569; Pantoate_ligase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR00017; cmk; 1. DR TIGRFAMs; TIGR00018; panC; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Ligase; Multifunctional enzyme; KW Nucleotide-binding; Pantothenate biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1..519 FT /note="Bifunctional pantoate ligase/cytidylate kinase" FT /id="PRO_0000239790" FT REGION 1..282 FT /note="Pantoate--beta-alanine ligase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349" FT REGION 283..519 FT /note="Cytidylate kinase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349" FT ACT_SITE 37 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349" FT BINDING 30..37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349" FT BINDING 66 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349" FT BINDING 66 FT /ligand="beta-alanine" FT /ligand_id="ChEBI:CHEBI:57966" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349" FT BINDING 155..158 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349" FT BINDING 161 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349" FT BINDING 192..195 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349" SQ SEQUENCE 519 AA; 58064 MW; 268B7AFEF6EA074C CRC64; MNLTILRTKT ALEDWCRQKH NHEINFVPTM GGLHQGHQEL IKTARSFCKR KHSSQVLVSI FINPLQFDLE EDFKKYPRTF ENDCKIAYEA GANAIWAPSF ESVFPNGEEA HFKIQVPFSL NKYLCGASRE GHFDGVATVV VRLLALVRPN RIFLGEKDWQ QLVILRQLIN DLGLPVLIHS IPTKRDQDGL PCSSRNVNLS KEERKKVVAL PAVLQQAAQA FQENKPINLN NMKTTLEEHD LKVEYLETVD LKNLNPVNHD ESKLCLLAAA VHCGNTRLID HGFLMKRNPI VAIDGPAGAG KSTVTKKFAQ KLGLIYLDTG AMYRAVTWLI QENNIDPQNS SELELILNDI NLDICLSNTG NQQVLINGKD ITTLIRSPTV TSQVSLVAAI GSVREKLTSQ QKELGSKGGL VAEGRDIGTA VFPDAELKIF LTATAQERAK RRAIDLKKQG FSTPSLSELE KQIKERDRLD SSREIAPLSK AKDAQELITD GMNIEEVVEL LINIFREKIP QEVWPTNAT //