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PANCY_TRIEI
ID   PANCY_TRIEI             Reviewed;         528 AA.
AC   Q110U9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, 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=Tery_2799;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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; CP000393; ABG51975.1; -; Genomic_DNA.
DR   RefSeq; WP_011612336.1; NC_008312.1.
DR   AlphaFoldDB; Q110U9; -.
DR   SMR; Q110U9; -.
DR   STRING; 203124.Tery_2799; -.
DR   EnsemblBacteria; ABG51975; ABG51975; Tery_2799.
DR   KEGG; ter:Tery_2799; -.
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   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; IPR004821; Cyt_trans-like.
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; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR00018; panC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Ligase; Multifunctional enzyme;
KW   Nucleotide-binding; Pantothenate biosynthesis; Transferase.
FT   CHAIN           1..528
FT                   /note="Bifunctional pantoate ligase/cytidylate kinase"
FT                   /id="PRO_0000333303"
FT   REGION          1..293
FT                   /note="Pantoate--beta-alanine ligase"
FT   REGION          294..528
FT                   /note="Cytidylate kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   ACT_SITE        41
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         65
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         65
FT                   /ligand="beta-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57966"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         160..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         166
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         197..200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
SQ   SEQUENCE   528 AA;  58427 MW;  EC536758F6078812 CRC64;
     MRLFTTIAGL NCYLNLLRNE QKKSPDTIGL VPTMGALHKG HLSLIKRARE ENTITVVSIF
     INPLQFAPRE DFKEYPRQLE IDKEFCEKEG VDVIFAPTPE TMGMKNALST DAQDSTTTVV
     SPSHMTSIMC GVSRPNFFQG VATIVTKLLN IVKPNNAYFG QKDAQQLAII KQLVKDLSLP
     VNIVYCPIIR EASGLAISSR NQYLTPEQKE QASMLYASLC YGRKIFLENQ DTPNILETVE
     NAVKEKLASQ PVLKLEYLEI VDPETLKPLE NIQNIGLLAI AAYIGSCRLI DNILLRNRKP
     IIAIDGPAGA GKSTVTKLVG QSLGLLYLDT GAMYRAVTWM VLQSGVPVTD QAQVAELVSQ
     CQISFNSPEN NHVVINGQDV TVAIRSREVT NNVSIVAAQP TVRYFMVKQQ QQFGAKGGIV
     AEGRDIGSHV FPNAELKIFL TASLKERSRR RLVELKQKGQ TNISLEEVEK EIICRDQKDT
     NRKISPLRKS SDAVEISTDG LSIGEVTQKI VDIFKTTCYG KSSVNNII
 
 
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