ID   PANCY_PROM3             Reviewed;         488 AA.
AC   A2CBX2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 92.
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=P9303_22471;
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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}.
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DR   EMBL; CP000554; ABM78982.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2CBX2; -.
DR   SMR; A2CBX2; -.
DR   STRING; 59922.P9303_22471; -.
DR   KEGG; pmf:P9303_22471; -.
DR   HOGENOM; CLU_037427_0_0_3; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000002274; 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   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.30.1300.10; Pantoate-beta-alanine ligase, C-terminal domain; 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   NCBIfam; TIGR00017; cmk; 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; PF02224; Cytidylate_kin; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Ligase; Multifunctional enzyme;
KW   Nucleotide-binding; Pantothenate biosynthesis; Transferase.
FT   CHAIN           1..488
FT                   /note="Bifunctional pantoate ligase/cytidylate kinase"
FT                   /id="PRO_0000333298"
FT   REGION          1..251
FT                   /note="Pantoate--beta-alanine ligase"
FT   REGION          252..488
FT                   /note="Cytidylate kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   ACT_SITE        8
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         1..8
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         36
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         36
FT                   /ligand="beta-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57966"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         125..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         131
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         162..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
SQ   SEQUENCE   488 AA;  53156 MW;  BF8216EDE9F518EC CRC64;
     MGALHRAHGQ LIKSVQGFGS LQPAAVLVSV FVNPLQFGPA EDFDSYPRDL EADCELASRS
     GASALWAPSV DQVFPGGASS QFRIQVPSHL QAHLCGAIRP GHFDGVVTVV ARLLALVRPE
     VLVLGEKDWQ QLVILRHLVA QLGLPVRVHG VATVRDDDGL ACSSRNRYLM TQQRQQALAL
     PQLLARAARE SQDGRAVDLA GLRCAWEQLG LEVEYVETVD AFNLQPLHAG RKLCLLAAAV
     RCGETRLIDH TFLMSRQPIV AIDGPAGAGK STVTRAFAER LGLLYLDTGA MYRAVTWLTQ
     QHDVDPHDPV AVKTILENLE LELEPSQSGP QKVRINGHDV TEAIRSPEVT SSVSVVAAHG
     CVRKALTAQQ QRMGVRGGLV AEGRDIGTAV FPDAELKVFL TASPAERARR RALDLDNRGF
     PVPDLAELET QIEERDRMDS TREVAPLRQA EDATELISDG MSIEEVIETL IDLFRVQVPE
     EVWPTPGS
//