PANCY_PROMS
ID PANCY_PROMS Reviewed; 509 AA.
AC A2BTH1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=A9601_17991;
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=146891;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000551; ABM71082.1; -; Genomic_DNA.
DR RefSeq; WP_011819204.1; NC_008816.1.
DR AlphaFoldDB; A2BTH1; -.
DR SMR; A2BTH1; -.
DR STRING; 146891.A9601_17991; -.
DR EnsemblBacteria; ABM71082; ABM71082; A9601_17991.
DR KEGG; pmb:A9601_17991; -.
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; UP000002590; 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; Transferase.
FT CHAIN 1..509
FT /note="Bifunctional pantoate ligase/cytidylate kinase"
FT /id="PRO_0000333295"
FT REGION 1..275
FT /note="Pantoate--beta-alanine ligase"
FT REGION 276..509
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 149..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 155
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 186..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
SQ SEQUENCE 509 AA; 58242 MW; AE119B900F9AC659 CRC64;
MKKLIIRKTE EIENWRKDID SEINFIPTMG NLHDGHIKLI STAKNDNSNI NLVSIFINPL
QFDNKLDLEN YPKTIDNDIN ISFSNGADAI FIPSNEDIYP PNNNISFLKA PIELSSALCG
LNRIGHFDGV CTVVYRLLNL IKPKNLYLGE KDWQQLLILK NLVLRKKLNI AIKSIPTQRD
FDGIPLSSRN VHLSKNERKL ISFFSRELLE AKKNFQKEKK INLKEIIKKL SEKKISIEYL
EHLHPYTLQK AKIEDNISLL AGAIRCGETR LIDHVFLMKR RPIIAIDGPA GSGKSTVTKL
IAKKLKLLYL DTGAMYRALS WLIIKENIDF KKENKLQNIL KDISIVFKSN TSSHQDVYVN
NYCVTEEIRS QKISSIVSKI SSIKEVREFL VEEQRKIGES GGLVAEGRDI GTTVFPHAEL
KIFLTASIDE RAKRRKSDKN SKDLQEIDLH KLKELIKQRD SEDSNRKISP LIKANDAIEI
ITDGYSINEV VDKIIDLYND KIPKESEIK
