ID   PYRG_XANOM              Reviewed;         554 AA.
AC   Q2P1K5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   01-APR-2015, entry version 65.
DE   RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=UTP--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_01227};
GN   Name=pyrG {ECO:0000255|HAMAP-Rule:MF_01227};
GN   OrderedLocusNames=XOO2817;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests
RT   contribution of large numbers of effector genes and insertion
RT   sequences to its race diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen.
CC       {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate +
CC       CTP + L-glutamate. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC       is the substrate. Inhibited by CTP. {ECO:0000255|HAMAP-
CC       Rule:MF_01227}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_01227}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01227}.
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DR   EMBL; AP008229; BAE69572.1; -; Genomic_DNA.
DR   RefSeq; YP_451846.1; NC_007705.1.
DR   ProteinModelPortal; Q2P1K5; -.
DR   SMR; Q2P1K5; 2-541.
DR   STRING; 342109.XOO_2817; -.
DR   EnsemblBacteria; BAE69572; BAE69572; BAE69572.
DR   KEGG; xom:XOO_2817; -.
DR   PATRIC; 24115548; VBIXanOry49434_3188.
DR   eggNOG; COG0504; -.
DR   HOGENOM; HOG000156188; -.
DR   KO; K01937; -.
DR   OMA; YERFLNR; -.
DR   OrthoDB; EOG6RC3NR; -.
DR   BioCyc; XORY342109:GIX9-2861-MONOMER; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000001957; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_01227; PyrG; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11550; PTHR11550; 1.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 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    554       CTP synthase.
FT                                /FTId=PRO_0000266266.
FT   DOMAIN      292    545       Glutamine amidotransferase type-1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   REGION        1    252       Aminator domain.
FT   ACT_SITE    380    380       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   ACT_SITE    518    518       {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    520    520       {ECO:0000255|HAMAP-Rule:MF_01227}.
SQ   SEQUENCE   554 AA;  61559 MW;  23615CCFCE279B1B CRC64;
     MTPLIFVTGG VVSSLGKGIA AASLASILEA RGLKVTMMKL DPYINVDPGT MSPFQHGEVY
     VTDDGAETDL DLGHYERYVR TRLSRKNSVT TGRIYENVIR KERRGDYLGA TVQVIPHITD
     EIRRCIDEAT AGFDVALIEI GGTVGDIESL PFLEAIRQVR TERGAEKAMF MHLTLVPYIA
     AAGELKTKPT QHSVKELRSI GIQPDVLLCR SEQAVPDSER RKIALFTNVS ERAVISCPDI
     DVLYGMPLEL LRQGLDELVI VQFKLRDKVA AADLSEWAAV VDAVKHPLDE VTIAVVGKYV
     DHQDAYKSVA EALRHGGLRQ RTKVNLKWLE AQDLERSDMA ALQDIDGILV PGGFGDRGFE
     GKVQTSKFAR EHKVPYFGIC YGMQAAVVDY ARHVADLDAA NSTENDRQSP HPVIGLITEW
     RTATGEVEKR DEKSDLGGTM RLGLQEQRLK PGTLARELYG KDVVAERHRH RYEFNNRYRT
     QLEDAGLVIS GKSMDDTLVE VVELPRDTHP WFLACQAHPE FLSTPRDGHP LFIGFVRAAR
     EKKAGGKLLK EARA
//