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PANCY_SYNS9
ID   PANCY_SYNS9             Reviewed;         483 AA.
AC   Q3AUV1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Syncc9902_1914;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000097; ABB26871.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3AUV1; -.
DR   SMR; Q3AUV1; -.
DR   STRING; 316279.Syncc9902_1914; -.
DR   EnsemblBacteria; ABB26871; ABB26871; Syncc9902_1914.
DR   KEGG; sye:Syncc9902_1914; -.
DR   eggNOG; COG0283; Bacteria.
DR   eggNOG; COG0414; Bacteria.
DR   HOGENOM; CLU_037427_0_0_3; -.
DR   OMA; IDHVFLM; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000002712; 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; 3.30.1300.10; -; 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; SSF52540; 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..483
FT                   /note="Bifunctional pantoate ligase/cytidylate kinase"
FT                   /id="PRO_0000239800"
FT   REGION          1..246
FT                   /note="Pantoate--beta-alanine ligase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   REGION          247..483
FT                   /note="Cytidylate kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   ACT_SITE        11
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         4..11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         34
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         34
FT                   /ligand="beta-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57966"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         124..127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         130
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         161..164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
SQ   SEQUENCE   483 AA;  52124 MW;  32B97AA32D8CBC79 CRC64;
     MPTMGALHAG HGTVIRAASA MGPVLVSVFV NPLQFGPDED LARYPRSLES DLVVAERWGA
     AALWAPSVEQ IYPQGGERHP STIQVPPGLQ KHLCGAARPG HFDGVVTVVA RLLDLVRPRQ
     LWLGEKDWQQ LVILRWLVAH LARPVIVQGV ATVREADGLA LSSRNQYLSP DQRRMAAALP
     EALHAARGDG SDPIPALRGS LSDAGFEVEY VQRVDPCTLQ PCGDETAISL LAAAVRCGST
     RLIDHAFLMT RQPLVAIDGP AGAGKSTVTR AFAERLGLVY LDTGAMYRSV TWLVLERGVN
     PSDGVAIEPL LKDLDVQLQS LPGGVQQVLV NGEDVSSAIR SPDVTASVSA VAAHRCVRQA
     LTVQQKSMGS KGGLVAEGRD IGTAVFPHAD LKVFLTATVT ERARRRALDL EQRGFAVPER
     AELEAQIAER DRLDSTREEA PLMQADDAIE LVTDGMDIDA VIEALVRLFR ERVAEEAWPT
     PQR
 
 
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