ID   PYRG_ANAPZ              Reviewed;         541 AA.
AC   Q2GLS9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=APH_0038;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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; CP000235; ABD43636.1; -; Genomic_DNA.
DR   RefSeq; YP_504672.1; -.
DR   GeneID; 3930011; -.
DR   GenomeReviews; CP000235_GR; APH_0038.
DR   KEGG; aph:APH_0038; -.
DR   NMPDR; fig|212042.5.peg.33; -.
DR   TIGR; APH_0038; -.
DR   HOGENOM; Q2GLS9; -.
DR   OMA; Q2GLS9; EFNNAYR.
DR   BioCyc; APHA212042:APH_0038-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    541       CTP synthase.
FT                                /FTId=PRO_0000266055.
FT   DOMAIN      296    537       Glutamine amidotransferase type-1.
FT   REGION        1    258       Aminator domain.
FT   ACT_SITE    382    382       Nucleophile (By similarity).
FT   ACT_SITE    510    510       By similarity.
FT   ACT_SITE    512    512       By similarity.
SQ   SEQUENCE   541 AA;  59454 MW;  CBB6A8950CB6809E CRC64;
     MVGKLNPTRF IFVTGGVVSS LGKGLAAASI GALLQARGFS VRLRKLDPYL NVDPGTMSPA
     QHGEVFVTSD GGETDLDLGH YERFTGVMKT RADNVTAGKI YHELIVKERR GDYLGQTVQV
     IPHVIDLIIS CILHNDAGAD FVICEIGGTV GDIESQPFLE AIRQVSYRLS KNLTIFVHLT
     LVPYIGAVGE LKTKPTQHSV KELSSLGIQP DIVLYRSRAQ LPQYQCAKIA NFCNVAEDNI
     IAALDVSNIY MLPVMYHEHR LDTQILKHFD VDSPEPDLTQ WENVLRMSET ASDRIVIAIV
     GKYVTSLDAY TSLEEALRHA GLHSGIRVEI KWVDARLPAS EIDLTDADAI LIPGGFGDNG
     IGTKICAIEY ARVNNIPMLG ICLGMQLAVI EFALNVAGIE DANSTEFKSD CKNPVVCELP
     GLQVGDEYKM GGSMRLGSYT CNLAPGSRIM SIYDSSTVVE RRRHRYGINP EYRDVLSKCG
     LAFTGAAEDR DLPEVLELPD HPWFIGVQFH PEFQSTPFKS HPLFLSFVTS TLQVKKASSR
     S
//