ID   PYRG_AYWBP              Reviewed;         536 AA.
AC   Q2NK04;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=CTP synthase;
DE            EC=6.3.4.2;
DE   AltName: Full=UTP--ammonia ligase;
DE   AltName: Full=CTP synthetase;
GN   Name=pyrG; OrderedLocusNames=AYWB_122;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A.,
RA   Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W.,
RA   Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to
RT   diverse environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(2006).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UTP + NH(3) = ADP + phosphate + CTP.
CC   -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC       is the substrate. Inhibited by CTP (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; CTP from UDP: step 2/2.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR   EMBL; CP000061; ABC65239.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_456318.1; -.
DR   GeneID; 3865884; -.
DR   GenomeReviews; CP000061_GR; AYWB_122.
DR   KEGG; ayw:AYWB_122; -.
DR   HOGENOM; Q2NK04; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:HAMAP.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01227; -; 1.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
DR   PANTHER; PTHR11550; PyrG_synth; 1.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   TIGRFAMs; TIGR00337; PyrG; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase;
KW   Nucleotide-binding; Pyrimidine biosynthesis.
FT   CHAIN         1    536       CTP synthase.
FT                                /FTId=PRO_0000266056.
FT   DOMAIN      306    536       Glutamine amidotransferase type-1.
FT   REGION        1    260       Aminator domain.
FT   ACT_SITE    388    388       Nucleophile (By similarity).
FT   ACT_SITE    512    512       By similarity.
FT   ACT_SITE    514    514       By similarity.
SQ   SEQUENCE   536 AA;  60798 MW;  F2C6E114400F2ADE CRC64;
     MNNKDLKTKF IFITGGVVSS LGKGITAASI GQILKNRGLK VSIQKLDPYI NVDPGTMSPY
     QHGEVFVTDD GAETDLDLGH YERFLDENMS KKSNVTAGQI YQSVINKERE GKYLGKTVQV
     IPHITEEIKQ KLTDAALFHK SDVVIVEIGG TVGDIESSPF LEAIRQVRFD FGYRNVLYLH
     TTLVPYLKKT KEIKTKPTQH SFKELRALGI QPQILVLRSE VPINQETKNK ISALCDINSQ
     AIFEALDVDI LYQMILNLNH QGIDDFILQH FKLTNFPTAD LQAWQQLITR IQNLEKKVVI
     ALVGKYIVLH DAYLSIVEAL KHASYQYNCK LEIKWIDAEK VTSDNISSFF EDCDGILVPY
     GFGNRAIEGK ILAINYARTN NIPFFGICLG MQLAVIEYAR NVLHLQDANS LEVDEKTPHP
     VITKKIVDIN LGGTLRLGSY SCHLKANTKS KAIYNQEIIY ERHRHRFEMN PHYVSLFEKN
     NDFVVSGINP EQNLCEIVEL KSHPWFIAVQ FHPEFLSRPL KPHPLFKGFV EASLLN
//