ID   PYRG_AZOBR     STANDARD;      PRT;   544 AA.
AC   P28595;
DT   01-DEC-1992 (Rel. 24, Created)
DT   01-DEC-1992 (Rel. 24, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   CTP synthase (EC 6.3.4.2) (UTP--ammonia ligase) (CTP synthetase).
GN   Name=pyrG;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sp7 / ATCC 29145;
RX   MEDLINE=94186025; PubMed=8138139; DOI=10.1016/0378-1097(94)90026-4;
RA   Zimmer W., Hundeshagen B.;
RT   "Identification and sequencing of pyrG, the CTP synthetase gene of
RT   Azospirillum brasilense Sp7.";
RL   FEMS Microbiol. Lett. 115:273-278(1994).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen.
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.
CC   -!- PATHWAY: Pyrimidine biosynthesis; conversion of UMP to CTP; third
CC       (last) step.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC   -!- SIMILARITY: Contains 1 type-1 glutamine amidotransferase domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; X67216; CAA47656.1; -.
DR   PIR; I39496; S25101.
DR   HAMAP; MF_01227; -; 1.
DR   InterPro; IPR000991; GATase_1.
DR   InterPro; IPR004468; PyrG_synth.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   TIGRFAMs; TIGR00337; PyrG; 1.
DR   PROSITE; PS00442; GATASE_TYPE_I; 1.
KW   Glutamine amidotransferase; Ligase; Pyrimidine biosynthesis.
FT   DOMAIN        1    300       Aminator domain.
FT   DOMAIN      301    544       Glutamine amidotransferase.
FT   ACT_SITE    380    380       GATase (By similarity).
FT   ACT_SITE    516    516       GATase (By similarity).
FT   ACT_SITE    518    518       GATase (By similarity).
SQ   SEQUENCE   544 AA;  59908 MW;  13AA1A8B8EB6C5DB CRC64;
     MTRYIFITGG VVSSLGKGLA SAALGALLQA RGYKVRLAKL DPYLNVDPGT MSPYQHGEVY
     VTDDGAETDL DLGHYERFTG VAARRGDNIT TGRIYSNVIA KERRGDYLGA TVQVIPHVTD
     QIKDFIGAET TDEDFILCEI GGTVGDIEST PFLEAIRQFG NEVGPENALF IHLTLLPYIP
     TAGELKTKPT QHSVKELLGM GIQANILLCR ADRPIPENER KKIALFCNIR PERVIAALDV
     DSIYQVPVSY HEEGFDTQVL AYFGLPTEGK PDLSRWTSIV ERVRKPQGEV TIAVVGKYTS
     LLDSYKSLAE ALTHGGIANN VKVKLDWIDS EIFEDESAVQ RLENVHGILV PGGFGSRGTE
     GKIRAAQFAR ERKVPYFGIC FGMQMAVIES ARNMAGIVDA GSTELGKPGN PVVGLLGLMT
     EWMRGNSLEK RTEGTDVGGT MRLGTYPAKL VPGSKVAEVY GTTDITERHR HRYEVNVYYK
     DRLEKVGLLF SGLSPTQLPE IVEIPDHPWF IGVQFHPELK SKPFDPHPLF TSFIKAAIEQ
     SRLV
//