ID   PANCY_ANAVT             Reviewed;         534 AA.
AC   Q3MEJ8;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-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=Ava_0964;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000117; ABA20588.1; -; Genomic_DNA.
DR   RefSeq; YP_321483.1; -.
DR   GeneID; 3680227; -.
DR   GenomeReviews; CP000117_GR; Ava_0964.
DR   KEGG; ava:Ava_0964; -.
DR   NMPDR; fig|240292.3.peg.170; -.
DR   HOGENOM; Q3MEJ8; -.
DR   OMA; Q3MEJ8; LGEKDWQ.
DR   BioCyc; AVAR240292:AVA_0964-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    534       Bifunctional pantoate ligase/cytidylate
FT                                kinase.
FT                                /FTId=PRO_0000239786.
FT   NP_BIND     315    323       ATP (By similarity).
FT   REGION        1    302       Pantoate--beta-alanine ligase.
FT   REGION      303    534       Cytidylate kinase.
SQ   SEQUENCE   534 AA;  59145 MW;  60E70FEF5A9B4CA6 CRC64;
     MRLLTTVAAL RCYLNKRRWE SQLTASEEQI LDSMTSWYQT AIGLVPTMGS LHQGHLSLIE
     RARHENSTVI VSIFINPLQF GPNEDYGRYP RTLEQDRQLC EQAGVDAIFA PSPEELGIPQ
     KNIQESQVTQ VIPPSVMISG LCGHSRLGHF QGVATIVTKL LNLVQPDRAY FGQKDGQQLA
     VIKRLVADLN LPVEIVACPT VREASGLACS SRNQYLTAPE KQQAAVLYRG LLQAEAAFKA
     GVRYSSRLRE VVRQELAKVS SVLVEYIELV EPTTLMPLDK IQEEGMLAIA ARLGSTRLID
     NTILRDRQPI IAIDGPAGAG KSTVARQVAT KLGLVYLDTG AMYRAVTWLV LQQGIAIDDD
     CAIAELANNC KIELTPSQDL QSPVRVWIND TDVTQDIRTI EVTSQVSAIA AQAAVREALV
     KQQQRWGKRG GLVAEGRDIG THVFPDAEVK IFLTASVGER ARRRQQDFQK QGQPEVSLEQ
     LEKDIAERDW KDSTRKVSPL QKAADAVELQ TDGLSISDVA SQIVDYYQQR LSQW
//