ID   PANCY_PROMT             Reviewed;         516 AA.
AC   Q46IM3;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Bifunctional pantoate ligase/cytidylate kinase;
DE   Includes:
DE     RecName: Full=Pantoate--beta-alanine ligase;
DE              EC=6.3.2.1;
DE     AltName: Full=Pantothenate synthetase;
DE     AltName: Full=Pantoate-activating enzyme;
DE   Includes:
DE     RecName: Full=Cytidylate kinase;
DE              Short=CK;
DE              EC=2.7.4.14;
DE     AltName: Full=Cytidine monophosphate kinase;
DE              Short=CMP kinase;
GN   Name=panC/cmk; OrderedLocusNames=PMN2A_1165;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Prochlorophytes; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L.,
RA   Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J.,
RA   Steglich C., Church G.M., 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   -!- CATALYTIC ACTIVITY: ATP + (R)-pantoate + beta-alanine = AMP +
CC       diphosphate + (R)-pantothenate.
CC   -!- CATALYTIC ACTIVITY: ATP + (d)CMP = ADP + (d)CDP.
CC   -!- PATHWAY: Cofactor biosynthesis; pantothenate biosynthesis;
CC       pantothenate from beta-alanine and pantoate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the pantothenate
CC       synthetase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the cytidylate
CC       kinase family. Type 1 subfamily.
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DR   EMBL; CP000095; AAZ58655.1; -; Genomic_DNA.
DR   RefSeq; YP_292358.1; -.
DR   GeneID; 3606556; -.
DR   GenomeReviews; CP000095_GR; PMN2A_1165.
DR   KEGG; pmn:PMN2A_1165; -.
DR   HOGENOM; Q46IM3; -.
DR   OMA; Q46IM3; LGEKDWQ.
DR   BioCyc; PMAR59920:PMN2A_1165-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004127; F:cytidylate kinase activity; IEA:HAMAP.
DR   GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:HAMAP.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:HAMAP.
DR   HAMAP; MF_01349; -; 1.
DR   InterPro; IPR003136; Cytidylate_kin.
DR   InterPro; IPR011994; Cytidylate_kin_d.
DR   InterPro; IPR003721; Pantoate_ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR21299:SF1; Pantoate_ligase; 1.
DR   Pfam; PF02224; Cytidylate_kin; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   ProDom; PD000657; Adenylate_kin; 1.
DR   TIGRFAMs; TIGR00017; cmk; 1.
DR   TIGRFAMs; TIGR00018; panC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; Ligase;
KW   Multifunctional enzyme; Nucleotide-binding; Pantothenate biosynthesis;
KW   Transferase.
FT   CHAIN         1    516       Bifunctional pantoate ligase/cytidylate
FT                                kinase.
FT                                /FTId=PRO_0000239793.
FT   NP_BIND     292    300       ATP (By similarity).
FT   REGION        1    279       Pantoate--beta-alanine ligase.
FT   REGION      280    516       Cytidylate kinase.
SQ   SEQUENCE   516 AA;  58289 MW;  3980DA9C3BFB07FA CRC64;
     MVRKIFQTNA ELKDWLSGQN SAIIFIPTMG GLHPGHQYLI QKAKEKKTNT NQIILVSIFV
     NPLQFSKGED FKKYPRNIKR DAELAFSAGA DAIWAPEYDE VFPGGADSHF KIEVPKTLHN
     QLCGAERKGH FDGVATVIIR LIKIIKPKKL ILGEKDWQQL IIIRKLFQEL SIPVKIESYS
     TQRDQSGFAY SSRNSYLSDS ERVNAQSLPN AIKEAKTEFD KGKVINLTKI ASIFKENNLK
     IEYLKIVDPF SLKETENINR LCLLAIAVKC GSTRLIDHTF LMHRKPIIAI DGPAGAGKST
     VTKAFAKKLG FIYLDTGAMY RAVTWLIISN SIDPNDQAEI KNILKDSKLE FKNSSFVEQK
     IFINNIDVTE KIRSPQVTSM VSEIAKQQFV REVLTRKQQV IGNNGGLVAE GRDIGTAVFP
     DADLKIFLTA SPTERAKRRA LDLHKRGYEF SSIEDLEKEI KERDKKDSER KIAPLKKAQD
     AIELVTDGMN IEDVLKELID IFRSKIPEEV WPTPNS
//