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   16-SEP-2015, entry version 68.
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=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.
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; CP000542; ABM58396.1; -; Genomic_DNA.
DR   RefSeq; WP_011810395.1; NC_008786.1.
DR   ProteinModelPortal; A1WL89; -.
DR   STRING; 391735.Veis_2653; -.
DR   EnsemblBacteria; ABM58396; ABM58396; Veis_2653.
DR   KEGG; vei:Veis_2653; -.
DR   PATRIC; 24019029; VBIVerEis120356_2903.
DR   eggNOG; COG0504; -.
DR   HOGENOM; HOG000077515; -.
DR   KO; K01937; -.
DR   OMA; YERFLNR; -.
DR   OrthoDB; EOG6RC3NR; -.
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: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; 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   REGION        1    257       Aminator domain.
FT   ACT_SITE    384    384       Nucleophile. {ECO:0000255|HAMAP-
FT                                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}.
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
//