ID   PYRG_ANAMM              Reviewed;         560 AA.
AC   Q5PBX6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
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=AM018;
OS   Anaplasma marginale (strain St. Maries).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=234826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA   Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA   Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT   "Complete genome sequencing of Anaplasma marginale reveals that the
RT   surface is skewed to two superfamilies of outer membrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
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; CP000030; AAV86203.1; -; Genomic_DNA.
DR   RefSeq; YP_153458.1; -.
DR   GeneID; 3171313; -.
DR   GenomeReviews; CP000030_GR; AM018.
DR   KEGG; ama:AM018; -.
DR   HOGENOM; Q5PBX6; -.
DR   OMA; Q5PBX6; EFNNAYR.
DR   BioCyc; AMAR234826:AM018-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    560       CTP synthase.
FT                                /FTId=PRO_0000266054.
FT   DOMAIN      297    539       Glutamine amidotransferase type-1.
FT   REGION        1    259       Aminator domain.
FT   ACT_SITE    383    383       Nucleophile (By similarity).
FT   ACT_SITE    512    512       By similarity.
FT   ACT_SITE    514    514       By similarity.
SQ   SEQUENCE   560 AA;  61146 MW;  D64F80BDE27F74D2 CRC64;
     MSIRDGCSAR FIFVTGGVVS SLGKGLAAAS IGALLQARGF RVRLRKLDPY LNVDPGTMSP
     AQHGEVFVTD DGGETDLDLG NYERFTGVNT TKEDNITAGR IYQQLLAKER RGDYLGHTVQ
     VIPHVTDLII SFILSNDDGA DFIICEIGGT VGDIESQPFL ESIRQVSYRL SKNFTIFVHL
     TLVPCVGSAG ELKTKPTQHS VKELSSLGIQ PDIILYRSAE PLPQYQSAKI ANFCNVSADN
     VIPALDVESM YKLPVMYHAH KLDTQILSHF GMGAPEPDLT KWANVLTMVN NARNVVTIAI
     IGKYTKFLDA YTSLTEALDH AGMHSGIKIQ VKWVDSRLPV RESDLHDVDG VLIPGGFGDD
     GVDGKVLAIG YARANGIPML GICMGMQLAA IEFALNVAKL EDANSTEFNQ ACKNPIVVEL
     PWLQKGEGEY LLGGSMRLGS CTYRLSADSR VASVYGSTVI NERCRHRYCI NPQYKNVLEE
     HGLSFTGMSD SHGLVEVLEL QSHPWFIGVQ FHPEFKSSPF APHPLFTSFV QNVLQIKQRG
     FMHKSVSAAA ILVPGSSVVS
//