ID   PYRG_VEREI              Reviewed;         554 AA.
AC   A1WL89;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   07-SEP-2016, entry version 72.
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=Cytidine 5'-triphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine triphosphate synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            Short=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            Short=CTPS {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=Veis_2653;
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-
RT   2.";
RL   Submitted (DEC-2006) 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: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; 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:0000255|HAMAP-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   -!- 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: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; CP000542; ABM58396.1; -; Genomic_DNA.
DR   RefSeq; WP_011810395.1; NC_008786.1.
DR   ProteinModelPortal; A1WL89; -.
DR   SMR; A1WL89; 2-549.
DR   STRING; 391735.Veis_2653; -.
DR   EnsemblBacteria; ABM58396; ABM58396; Veis_2653.
DR   KEGG; vei:Veis_2653; -.
DR   PATRIC; 24019029; VBIVerEis120356_2903.
DR   eggNOG; ENOG4105C8D; Bacteria.
DR   eggNOG; COG0504; LUCA.
DR   HOGENOM; HOG000077515; -.
DR   KO; K01937; -.
DR   OMA; TMRLGEY; -.
DR   OrthoDB; POG091H02IX; -.
DR   BioCyc; VEIS391735:GHY5-2681-MONOMER; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000000374; 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: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-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   Magnesium; Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    554       CTP synthase.
FT                                /FTId=PRO_1000139598.
FT   DOMAIN      295    548       Glutamine amidotransferase type-1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND      14     19       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     151    153       Allosteric inhibitor CTP.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     191    196       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     191    196       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   REGION        1    270       Amidoligase domain. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   REGION      385    388       L-glutamine binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   ACT_SITE    384    384       Nucleophile; for glutamine hydrolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    521    521       {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    523    523       {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   METAL        71     71       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   METAL       144    144       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING      13     13       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING      13     13       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING      71     71       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     227    227       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     227    227       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING     357    357       L-glutamine; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     408    408       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING     474    474       L-glutamine; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
SQ   SEQUENCE   554 AA;  61306 MW;  A1CD97835912DF86 CRC64;
     MTKFVFVTGG VVSSLGKGIA SASLAAILES RGLKVTLIKL DPYINVDPGT MSPFQHGEVF
     VTDDGAETDL DLGHYERFIE TRMNRANNFT TGKIYQSVLE KERRGDYLGK TVQVIPHVTN
     EIQEFIQRGA GMGTPVAVDV AIVEIGGTVG DIESLPFLEA VRQMSLRMGA NNSTFVHLTY
     LPWIATAGEL KTKPTQHTVQ KLREIGIQAD ALLCRADRRI PGEERAKISL FTNVPEWGVI
     SMWDVDIIYK VPRMLHEQGL DGLICDKLRL NTRPTNLQRW DDLVYATEHP QGAVTVAMVG
     KYVDLSDSYK SVNEALRHAG MRNHVRVQID HVDSETIDSA DAAARLARYD AILVPGGFGQ
     RGVEGKIATA RYAREHKLPY LGICLGMQVA TIEYARHVAG LANANSTEFD PATPHPVIAL
     ITEWQDADGS IQQRDQDSNL GGTMRLGAQS SDVLAGTLAH RIYGDVVTER HRHRYEANVN
     YLEPLRKAGL VIAALTQREQ LTEIVELPQS MHPWFIGVQF HPEFKSTPWN GHPLFNSFIA
     AAKARHQARH EGPA
//