(data stored in SCRATCH3701 zone)

SWISSPROT: PANCY_SYNS3

ID   PANCY_SYNS3             Reviewed;         494 AA.
AC   Q0ICW2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 79.
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=sync_0483;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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}.
DR   EMBL; CP000435; ABI45138.1; -; Genomic_DNA.
DR   SMR; Q0ICW2; -.
DR   STRING; 64471.sync_0483; -.
DR   EnsemblBacteria; ABI45138; ABI45138; sync_0483.
DR   KEGG; syg:sync_0483; -.
DR   eggNOG; ENOG4105CAT; Bacteria.
DR   eggNOG; COG0283; LUCA.
DR   eggNOG; COG0414; LUCA.
DR   HOGENOM; HOG000233355; -.
DR   KO; K13799; -.
DR   OMA; LGEKDWQ; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000001961; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-UniRule.
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:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02020; CMPK; 1.
DR   Gene3D; 3.30.1300.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 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;
DR   PRODOM; Q0ICW2.
DR   SWISS-2DPAGE; Q0ICW2.
KW   ATP-binding; Cytoplasm; Kinase; Ligase; Multifunctional enzyme;
KW   Nucleotide-binding; Pantothenate biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..494
FT                   /note="Bifunctional pantoate ligase/cytidylate kinase"
FT                   /id="PRO_0000333300"
FT   NP_BIND         7..14
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   NP_BIND         130..133
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   NP_BIND         167..170
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   REGION          1..258
FT                   /note="Pantoate--beta-alanine ligase"
FT   REGION          259..494
FT                   /note="Cytidylate kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   ACT_SITE        14
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         41
FT                   /note="Beta-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         41
FT                   /note="Pantoate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         136
FT                   /note="Pantoate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         159
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
SQ   SEQUENCE   494 AA;  53594 MW;  E7EDD078F93465E3 CRC64;
     MHFVPTMGGL HHGHASLISA ASCHKSGDVE TLVSVFVNPL QFGPNEDFAR YPRTFEADCE
     LAELSGASAI WCPDESQIYP GGSAESWRIQ APKSLQSRLC GSTRPGHFDG VVTVVCRLLA
     LAKPHQLFLG EKDWQQLTIL RRMVLDLGLA VRVRGVPTVR DGDGLASSSR NRYLNAQQRQ
     QGVLFAQVLS DARSACLHGG TALKPGEVKR RLEEVGLSVE YVDVVDPWFL QPSKSNQSSL
     TLLAAAVRCG STRLIDHAFL MTRSPLVAID GPAGAGKSTV TRAFAERLGL VYLDTGAMYR
     AVTWLVLEQG GDPGDSEAVD LVLNDLKVEL EPLQQGVQVV RVNGHEVTDA IRDPRVTASV
     SAVASHACVR AAMTAQQQRM GKAGGLVAEG RDIGTAVFPD AELKVFLTAT PKERARRRAL
     DLEARGHEVP ALPELEAQIV ERDRLDSTRE VAPLLQADDA IELISDGMSI DQVIDALEDL
     FRRRVGEEVW PTPV
//

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