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 03-AUG-2022, entry version 88.
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}.
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DR EMBL; CP000435; ABI45138.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0ICW2; -.
DR SMR; Q0ICW2; -.
DR STRING; 64471.sync_0483; -.
DR PRIDE; Q0ICW2; -.
DR EnsemblBacteria; ABI45138; ABI45138; sync_0483.
DR KEGG; syg:sync_0483; -.
DR eggNOG; COG0283; Bacteria.
DR eggNOG; COG0414; Bacteria.
DR HOGENOM; CLU_037427_0_0_3; -.
DR OMA; IDHVFLM; -.
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: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..494
FT /note="Bifunctional pantoate ligase/cytidylate kinase"
FT /id="PRO_0000333300"
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 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 41
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 41
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 130..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 136
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 167..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
