ID   PANCY_SYNJA             Reviewed;         540 AA.
AC   Q2JRH9;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
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=CYA_2663;
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium
OS   Yellowstone A-Prime).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
OX   NCBI_TaxID=321327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M.,
RA   Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community
RT   revealed by comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(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; CP000239; ABD00775.1; -; Genomic_DNA.
DR   RefSeq; YP_476038.1; -.
DR   GeneID; 3899594; -.
DR   GenomeReviews; CP000239_GR; CYA_2663.
DR   KEGG; cya:CYA_2663; -.
DR   TIGR; CYA_2663; -.
DR   HOGENOM; Q2JRH9; -.
DR   OMA; Q2JRH9; LGEKDWQ.
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; IPR004821; Cyt_trans_rel.
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; TIGR00125; cyt_tran_rel; 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    540       Bifunctional pantoate ligase/cytidylate
FT                                kinase.
FT                                /FTId=PRO_0000239795.
FT   NP_BIND     314    322       ATP (By similarity).
FT   REGION        1    280       Pantoate--beta-alanine ligase.
FT   REGION      281    540       Cytidylate kinase.
SQ   SEQUENCE   540 AA;  59712 MW;  A710282A55B4D3DD CRC64;
     MQWLRTVAAL REQVASWRGS TIGLVPTMGS LHEGHLSLIR RCRQECDHTV VSIFVNPLQF
     GPNEDWDRYP RDEEGDRALC EAAGVDVVFA PDPQEMGADP ATAGDRTWVM PPESLLQTLC
     APHRPGHFRG VATIVLQLLN LVQPQRAYFG QKDAQQLAII QRLVQDLQIP TTIVPCPTVR
     EADGLAYSSR NRYLSAVERQ VAASLYRALR RGYDHWQAGD PSAEGILAAA RAELERTPEL
     RVQYLELVDP QTLQPLSEVK DKGLLAIAAY VGQTRLIDNL LLSPEGVDPL PQEQQSAVPP
     SPKRGRRPLI AIDGPAGAGK SSVARAVAAQ LQLLYLDTGA MYRAITWLAL QRGIPLDDAE
     QLTQLAAQTQ LTLQSGPSAD EPTRIWADGE EVTQAIRSPE VTRWVSQVAA VPGVRQELVK
     RQRLIGRDGG AVLEGRDIGT HVFPDAELKV FLTASVGERA QRRQHQLQAQ GQVVSLEELK
     AQIEQRDRRD SERLISPLRP APDAILIDTD HLSQAEVEDK IVRLYRQLLE RSGAAHFDII
//