ID   PANCY_TRIEI             Reviewed;         528 AA.
AC   Q110U9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Tery_2799;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriales; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000393; ABG51975.1; -; Genomic_DNA.
DR   RefSeq; YP_722448.1; -.
DR   GeneID; 4245333; -.
DR   GenomeReviews; CP000393_GR; Tery_2799.
DR   KEGG; ter:Tery_2799; -.
DR   HOGENOM; Q110U9; -.
DR   OMA; Q110U9; LGEKDWQ.
DR   BioCyc; TERY203124:TERY_2799-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; 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    528       Bifunctional pantoate ligase/cytidylate
FT                                kinase.
FT                                /FTId=PRO_0000333303.
FT   NP_BIND      34     41       ATP (By similarity).
FT   NP_BIND     160    163       ATP (By similarity).
FT   NP_BIND     197    200       ATP (By similarity).
FT   REGION        1    293       Pantoate--beta-alanine ligase.
FT   REGION      294    528       Cytidylate kinase.
FT   ACT_SITE     41     41       Proton donor (By similarity).
FT   BINDING      65     65       Beta-alanine (By similarity).
FT   BINDING      65     65       Pantoate (By similarity).
FT   BINDING     166    166       Pantoate (By similarity).
FT   BINDING     189    189       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
SQ   SEQUENCE   528 AA;  58427 MW;  EC536758F6078812 CRC64;
     MRLFTTIAGL NCYLNLLRNE QKKSPDTIGL VPTMGALHKG HLSLIKRARE ENTITVVSIF
     INPLQFAPRE DFKEYPRQLE IDKEFCEKEG VDVIFAPTPE TMGMKNALST DAQDSTTTVV
     SPSHMTSIMC GVSRPNFFQG VATIVTKLLN IVKPNNAYFG QKDAQQLAII KQLVKDLSLP
     VNIVYCPIIR EASGLAISSR NQYLTPEQKE QASMLYASLC YGRKIFLENQ DTPNILETVE
     NAVKEKLASQ PVLKLEYLEI VDPETLKPLE NIQNIGLLAI AAYIGSCRLI DNILLRNRKP
     IIAIDGPAGA GKSTVTKLVG QSLGLLYLDT GAMYRAVTWM VLQSGVPVTD QAQVAELVSQ
     CQISFNSPEN NHVVINGQDV TVAIRSREVT NNVSIVAAQP TVRYFMVKQQ QQFGAKGGIV
     AEGRDIGSHV FPNAELKIFL TASLKERSRR RLVELKQKGQ TNISLEEVEK EIICRDQKDT
     NRKISPLRKS SDAVEISTDG LSIGEVTQKI VDIFKTTCYG KSSVNNII
//