ID   PYRG_SPHAL              Reviewed;         543 AA.
AC   Q1GTY6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   29-APR-2008, entry version 20.
DE   CTP synthase (EC 6.3.4.2) (UTP--ammonia ligase) (CTP synthetase).
GN   Name=pyrG; OrderedLocusNames=Sala_1170;
OS   Sphingopyxis alaskensis (Sphingomonas alaskensis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=117207;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C.,
RA   Chertkov O., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Cavicchioli R., Robb F., Ertan H., Schut F.,
RA   Ting L.M., Richardson P.;
RT   "Complete sequence of chromosome of Sphingopyxis alaskensis RB2256.";
RL   Submitted (APR-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 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UTP + NH(3) = ADP + phosphate + CTP.
CC   -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC       is the substrate. Inhibited by CTP (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; CTP from UDP: step 2/2.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000356; ABF52886.1; -; Genomic_DNA.
DR   RefSeq; YP_616219.1; -.
DR   GeneID; 4080876; -.
DR   GenomeReviews; CP000356_GR; Sala_1170.
DR   KEGG; sal:Sala_1170; -.
DR   NMPDR; fig|317655.9.peg.1104; -.
DR   BioCyc; SALA317655:SALA_1170-MON; -.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:HAMAP.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01227; -; 1.
DR   InterPro; IPR000991; GATase_1.
DR   InterPro; IPR012998; GATase_1_AS.
DR   InterPro; IPR004468; PyrG_synth.
DR   PANTHER; PTHR11550; PyrG_synth; 1.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   TIGRFAMs; TIGR00337; PyrG; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glutamine amidotransferase; Ligase;
KW   Pyrimidine biosynthesis.
FT   CHAIN         1    543       CTP synthase.
FT                                /FTId=PRO_0000266223.
FT   DOMAIN      291    542       Glutamine amidotransferase type-1.
FT   REGION        1    252       Aminator domain.
FT   ACT_SITE    381    381       Nucleophile (By similarity).
FT   ACT_SITE    515    515       By similarity.
FT   ACT_SITE    517    517       By similarity.
SQ   SEQUENCE   543 AA;  59457 MW;  B33AAC32224CA804 CRC64;
     MARFIFITGG VVSSLGKGLM AASLAALLQA RGYRVRIRKF DPYLNVDPGT MSPYQHGEVY
     VTDDGAETDL DLGHYERFTG VAARQSDNVT SGRIYQGIIA KERRGDYLGA TVQVVPHVTD
     AIKDFARAET DDLDFVLCEI GGTVGDIESL PFIEAIRQLK NEVGRDNAIS VHVTLVPYIA
     AAGELKTKPT QHSVRELASL GVQPDILLCR CEKPLPDSER AKIALFCNVR KEAVIPALDA
     DSIYSVPVQY HGEGLDSEVL RAFGILDAPA PDLTAWYDIM DRKQHPEGEV TIGVVGKYVS
     LPDAYKSLNE ALVHGGMAHR VKVNIRWLDA EMFERDEDLV ANLEPLHGIL VPGGFGERGS
     EGKIASVRFA RERNVPFFGI CLGMQMACIE AARNTSGIAN ASSTEFGPTD EPVVGLITEW
     MSAEGLQKRG ANTDLGGTMR LGAYDAKLSP NSHVASVYGT NEISERHRHR YEVNGAYRER
     LEKGGLVFSG MSPDGMLPEI VERPDHPWFI GVQFHPELKS KPFDPHPLFA GFIEAAVKQS
     RLV
//