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   16-JUN-2009, entry version 19.
DE   RecName: Full=Bifunctional pantoate ligase/cytidylate kinase;
DE   Includes:
DE     RecName: Full=Pantothenate synthetase;
DE              Short=PS;
DE              EC=6.3.2.1;
DE     AltName: Full=Pantoate--beta-alanine ligase;
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=sync_0483;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F.,
RA   Badger J.H., Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J.,
RA   Durkin A.S., Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y.,
RA   Halpin R., Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to
RT   a coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
CC   -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine
CC       in an ATP-dependent reaction via a pantoyl-adenylate intermediate
CC       (By similarity).
CC   -!- FUNCTION: Displays a CMP kinase activity (By similarity).
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; CP000435; ABI45138.1; -; Genomic_DNA.
DR   RefSeq; YP_729710.1; -.
DR   GeneID; 4260685; -.
DR   GenomeReviews; CP000435_GR; sync_0483.
DR   KEGG; syg:sync_0483; -.
DR   TIGR; sync_0483; -.
DR   HOGENOM; Q0ICW2; -.
DR   OMA; Q0ICW2; 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; 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    494       Bifunctional pantoate ligase/cytidylate
FT                                kinase.
FT                                /FTId=PRO_0000333300.
FT   NP_BIND       7     14       ATP (By similarity).
FT   NP_BIND     130    133       ATP (By similarity).
FT   NP_BIND     167    170       ATP (By similarity).
FT   REGION        1    258       Pantoate--beta-alanine ligase.
FT   REGION      259    494       Cytidylate kinase.
FT   ACT_SITE     14     14       Proton donor (By similarity).
FT   BINDING      41     41       Beta-alanine (By similarity).
FT   BINDING      41     41       Pantoate (By similarity).
FT   BINDING     136    136       Pantoate (By similarity).
FT   BINDING     159    159       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
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
//