ID   A0A081LE79_9BACI        Unreviewed;       535 AA.
AC   A0A081LE79;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   20-JUN-2018, entry version 23.
DE   RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227};
DE            EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine triphosphate synthetase {ECO:0000256|HAMAP-Rule:MF_01227};
DE            Short=CTP synthetase {ECO:0000256|HAMAP-Rule:MF_01227};
DE            Short=CTPS {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 zhangzhouensis.
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. Regulates
CC       intracellular CTP levels through interactions with the four
CC       ribonucleotide triphosphates. {ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate +
CC       CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227,
CC       ECO:0000256|SAAS:SAAS00710710}.
CC   -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC       is the substrate; GTP has no effect on the reaction when ammonia
CC       is the substrate. The allosteric effector GTP functions by
CC       stabilizing the protein conformation that binds the tetrahedral
CC       intermediate(s) formed during glutamine hydrolysis. Inhibited by
CC       the product CTP, via allosteric rather than competitive
CC       inhibition. {ECO:0000256|HAMAP-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:SAAS00710815}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227,
CC       ECO:0000256|SAAS:SAAS00710816}.
CC   -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for
CC       distinguishing between UTP and CTP. The overlapping regions of the
CC       product feedback inhibitory and substrate sites recognize a common
CC       feature in both compounds, the triphosphate moiety. To
CC       differentiate isosteric substrate and product pyrimidine rings, an
CC       additional pocket far from the expected kinase/ligase catalytic
CC       site, specifically recognizes the cytosine and ribose portions of
CC       the product inhibitor. {ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00710794}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {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   UniPathway; UPA00159; UER00277.
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-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01746; GATase1_CTP_Synthase; 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; IPR033828; GATase1_CTP_Synthase.
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:SAAS00710699};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028091};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|PROSITE-ProRule:PRU00605, ECO:0000256|SAAS:SAAS00710676};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00710762};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00710689};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00710675};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00710810};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00710748}.
FT   DOMAIN      292    534       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   NP_BIND      14     19       ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   NP_BIND     148    150       Allosteric inhibitor CTP.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   NP_BIND     188    193       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   NP_BIND     188    193       UTP; alternate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   REGION        1    267       Amidoligase domain. {ECO:0000256|HAMAP-
FT                                Rule:MF_01227}.
FT   REGION      382    385       L-glutamine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01227}.
FT   ACT_SITE    381    381       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00605}.
FT   ACT_SITE    381    381       Nucleophile; for glutamine hydrolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    507    507       {ECO:0000256|HAMAP-Rule:MF_01227,
FT                                ECO:0000256|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    509    509       {ECO:0000256|HAMAP-Rule:MF_01227,
FT                                ECO:0000256|PROSITE-ProRule:PRU00605}.
FT   METAL        71     71       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   METAL       141    141       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   BINDING      13     13       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   BINDING      13     13       UTP; alternate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   BINDING      54     54       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   BINDING      71     71       ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   BINDING     224    224       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   BINDING     224    224       UTP; alternate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   BINDING     242    242       ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   BINDING     354    354       L-glutamine; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   BINDING     405    405       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   BINDING     462    462       L-glutamine; via amide nitrogen.
FT                                {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
//