PANCY_PROMP
ID PANCY_PROMP Reviewed; 510 AA.
AC Q7UZR6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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}; OrderedLocusNames=PMM1590;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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; BX548174; CAE20049.1; -; Genomic_DNA.
DR RefSeq; WP_011133218.1; NC_005072.1.
DR AlphaFoldDB; Q7UZR6; -.
DR SMR; Q7UZR6; -.
DR STRING; 59919.PMM1590; -.
DR EnsemblBacteria; CAE20049; CAE20049; PMM1590.
DR KEGG; pmm:PMM1590; -.
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; UP000001026; 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_0000239792"
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; 58295 MW; 315DC94E014CBDF8 CRC64;
MNKIIIRKTE DLKEWRRNLK CDINFIPTMG NLHDGHQKLI STAQSSNCNT NLLSIFVNPL
QFDSKEDLKS YPKTVDKDIE IAFSNGADAI FIPNVTDIYP KKNKSISYLK ASKELSSALC
GLTRVGHFDG VCTVVYRLLK LIQPKNLFLG EKDWQQLLII KNLIEEKKFN IKIIPVPTQR
DSDGVPFSSR NKHLSKSERK SLKLFSNELE NAKIIFKKDK RIDLKQLTNK LKSKNISIEY
LEHLHPYSLK KVQSNDNISI LAGAIKCGKT RLIDHVFLMK RKPIIAIDGP AGSGKSTITK
LIAKELNLLY LDTGAMYRAI SWLFKKEKID YAKESELKKI LNNISIIFKS NSISQQDVFI
NNFCVTEEIR SQEISSIVSK ISSIKKVREF LVYEQRKIGQ SGGLVAEGRD IGTTVFPNAE
LKIFLTASID ERAKRRKSEL DLRGTEEIDF NQLRELIRKR DFEDSTRKIS PLKKANDAIE
LLTDGYSINE VVEKIVNIYN LNIPKEIQLE
