PANCY_PROM9
ID PANCY_PROM9 Reviewed; 510 AA.
AC Q318F2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, 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=PMT9312_1682;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-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; CP000111; ABB50743.1; -; Genomic_DNA.
DR RefSeq; WP_011377224.1; NC_007577.1.
DR AlphaFoldDB; Q318F2; -.
DR SMR; Q318F2; -.
DR STRING; 74546.PMT9312_1682; -.
DR EnsemblBacteria; ABB50743; ABB50743; PMT9312_1682.
DR KEGG; pmi:PMT9312_1682; -.
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; UP000002715; 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; 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; Transferase.
FT CHAIN 1..510
FT /note="Bifunctional pantoate ligase/cytidylate kinase"
FT /id="PRO_0000239789"
FT REGION 1..276
FT /note="Pantoate--beta-alanine ligase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT REGION 277..510
FT /note="Cytidylate kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT ACT_SITE 36
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 61
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 61
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 150..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 156
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 187..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
SQ SEQUENCE 510 AA; 58205 MW; 3F9FC5D467800741 CRC64;
MKKVIIRKTE EIKNWRRNIN SDINFIPTMG NLHNGHKTLI STAKNANSNV NLVSIFVNPL
QFDNKSDLEN YPKTIDNDIK ISFENGADVI FIPSTEEIYP SDNKNITFLK APLELSSSLC
GLNRIGHFDG VCTVVYKLLN LIKPKNLYLG EKDWQQLLIL KNLVLTKKLD VAIKSIPTQR
DFDGIPLSSR NVHLSNNERK LIRFFSHELL VAKENFQQEK KINLKEIIQK LSAQKISIEY
LEHLHPYTLQ ESKVEDNISI LAGAIRCGET RLIDHVFLMK RSPIIAIDGP AGSGKSTVTQ
LIAKKLKLLY LDTGAMYRAL SWLLIKENID YKEEKKLQNI LKDISIVFKS NTNSQQDVFI
NNYCVTEEIR SQEISSIVSK ISSIKEVREF LVEEQRKIGE SGGLVAEGRD IGTTVFPDAE
LKIFLTASID ERAKRRKSDK KSKDSQEIDL HKLKELIKKR DFEDSNREIS PLIKANDAIE
IITDGCSINE VVDKIIDLYN DKIPKETQIR
