ID   A0A081LE79_9BACI        Unreviewed;       535 AA.
AC   A0A081LE79;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   08-JUN-2016, entry version 11.
DE   RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037303};
DE            EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037401};
DE   AltName: Full=CTP synthetase {ECO:0000256|HAMAP-Rule:MF_01227};
DE   AltName: Full=UTP--ammonia ligase {ECO:0000256|HAMAP-Rule:MF_01227};
GN   Name=pyrG {ECO:0000256|HAMAP-Rule:MF_01227};
GN   ORFNames=BA70_10510 {ECO:0000313|EMBL:KEP27555.1};
OS   Bacillus sp. DW5-4.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1178540 {ECO:0000313|EMBL:KEP27555.1, ECO:0000313|Proteomes:UP000028091};
RN   [1] {ECO:0000313|EMBL:KEP27555.1, ECO:0000313|Proteomes:UP000028091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW5-4 {ECO:0000313|EMBL:KEP27555.1,
RC   ECO:0000313|Proteomes:UP000028091};
RA   Lai Q., Liu Y., Shao Z.;
RT   "Genome Sequence of Bacillus sp. DW5-4.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037305}.
CC   -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate +
CC       CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227,
CC       ECO:0000256|SAAS:SAAS00037321}.
CC   -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC       is the substrate. Inhibited by CTP. {ECO:0000256|HAMAP-
CC       Rule:MF_01227}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; CTP from UDP: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01227,
CC       ECO:0000256|SAAS:SAAS00037318}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00548960}.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC       {ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KEP27555.1}.
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DR   EMBL; JOTP01000003; KEP27555.1; -; Genomic_DNA.
DR   RefSeq; WP_034318251.1; NZ_JOTP01000003.1.
DR   EnsemblBacteria; KEP27555; KEP27555; BA70_10510.
DR   Proteomes; UP000028091; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00434461};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028091};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00434680};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00434363};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00434657};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00434336}.
FT   DOMAIN      292    534       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   REGION        1    254       Aminator domain. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   ACT_SITE    381    381       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   ACT_SITE    507    507       {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    509    509       {ECO:0000256|HAMAP-Rule:MF_01227}.
SQ   SEQUENCE   535 AA;  59715 MW;  5C1F20E946D25BA1 CRC64;
     MTKYIFVTGG VVSSLGKGIT AASLGRLLKN RGMDVTIQKF DPYINVDPGT MSPYQHGEVF
     VTDDGAETDL DLGHYERFID INLNKYSNVT TGKIYSTVLK KERRGDYLGG TVQVIPHITN
     EIKDRVYRAG KETGADVVIT EIGGTVGDIE SLPFLEAIRQ MKSDIGRENV MYIHCTLVPY
     IRAAGELKTK PTQHSVKELR SLGIQPNVIV VRTEMPMTQD MKDKIALFCD IDTKAVIECQ
     DADTLYSIPL DLQKQGLDKL VCEHMKLECQ DADMTEWTAL VDKVQNLSKQ VTIGLVGKYV
     ELQDAYISVV ESLRHAGYAF DADVQIKWIN AEEVTAENIA DFAQDVDGMI VPGGFGDRGV
     EGKIIATQYA RENKVPFFGI CLGMQVASIE YARNVLGLEG AHSAEIDPET AFPIIDLLPE
     QKDVDDLGGT LRLGLYPCKL NEDSKAFAAY NDEVVYERHR HRYEFNNEYR QQMEAAGFVF
     SGTSPDGRLV EIIELKDHPW FLASQFHPEF ISRPTRPQPL FRDFVGASLQ ASESK
//