ID   PYRG_ANAVT              Reviewed;         545 AA.
AC   Q3MAV1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=CTP synthase;
DE            EC=6.3.4.2;
DE   AltName: Full=UTP--ammonia ligase;
DE   AltName: Full=CTP synthetase;
GN   Name=pyrG; OrderedLocusNames=Ava_2267;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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.
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DR   EMBL; CP000117; ABA21885.1; -; Genomic_DNA.
DR   RefSeq; YP_322780.1; -.
DR   GeneID; 3679012; -.
DR   GenomeReviews; CP000117_GR; Ava_2267.
DR   KEGG; ava:Ava_2267; -.
DR   HOGENOM; Q3MAV1; -.
DR   OMA; Q3MAV1; EFNNAYR.
DR   BioCyc; AVAR240292:AVA_2267-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:HAMAP.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01227; -; 1.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
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   ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase;
KW   Nucleotide-binding; Pyrimidine biosynthesis.
FT   CHAIN         1    545       CTP synthase.
FT                                /FTId=PRO_0000266052.
FT   DOMAIN      292    534       Glutamine amidotransferase type-1.
FT   REGION        1    254       Aminator domain.
FT   ACT_SITE    381    381       Nucleophile (By similarity).
FT   ACT_SITE    507    507       By similarity.
FT   ACT_SITE    509    509       By similarity.
SQ   SEQUENCE   545 AA;  60341 MW;  2F34AAF699AA7977 CRC64;
     MTKFIFVTGG VVSSIGKGIV AASLGRLLKS RDYSVSILKL DPYINIDPGT MSPFQHGEVF
     VTQDGAETDL DLGHYERFTD TSMSRLNSVT TGSIYQAVIM RERRGDYNGG TVQVIPHITN
     EIKERILSVA KETNPSVVIT EIGGTVGDIE SLPFLEAIRQ LRKQVGRQNV LYMHVTLMPY
     IASAGEMKTK PTQHSVKELR SIGIQPDILV CRSDRPIPRG LKQKLSEFCD VPVECVITSQ
     DARSIYEVPL ILEGEGLAEQ TLKLLQMEQR QPNLEKWQAM VQGLYSPKHT VEIAIVGKYV
     SLGDAYLSVV EALRHAAIAT QGDLQLRWIN SEDLETQAPE TYLAGVDGIV VPGGFGTRGV
     DGKIAAIKYA RDRQIPFLGL CLGMQCSVIE WARNVGGLAG ANSAEFDSTT KYPVINLLPE
     QQDVVDLGGT MRLGVYPCHI LPNTLASKLY QAEIIQERHR HRYEFNNDYR QLLLDSGYVI
     SGTSPDGRLV EIVEYPQHPF FISCQFHPEF QSRPNTPHPL FTGFVQAAIA QSHPTANFQT
     PVKVS
//