ID Q4GZ95_TRYB2 Unreviewed; 589 AA. AC Q4GZ95; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=CTP synthase {ECO:0000256|RuleBase:RU810713}; DE EC=6.3.4.2 {ECO:0000256|RuleBase:RU810713}; DE AltName: Full=UTP--ammonia ligase {ECO:0000256|RuleBase:RU810713}; GN ORFNames=TB927.1.1240 {ECO:0000313|EMBL:CAJ16071.1}; OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1). OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=185431 {ECO:0000313|EMBL:CAJ16071.1, ECO:0000313|Proteomes:UP000008524}; RN [1] {ECO:0000313|EMBL:CAJ16071.1, ECO:0000313|Proteomes:UP000008524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:CAJ16071.1, RC ECO:0000313|Proteomes:UP000008524}; RX PubMed=12907729; DOI=10.1093/nar/gkg674; RA Hall N., Berriman M., Lennard N.J., Harris B.R., Hertz-Fowler C., RA Bart-Delabesse E.N., Gerrare C.S., Atkin R.J., Barron A.J., Bowman S., RA Bray-Allen S.P., Bringaud F., Clark L.N., Corton C.H., Cronin A., RA Davies R., Doggett J., Fraser A., Gruter E., Hall S., Harper A.D., RA Kay M.P., Leech V., Mayes R., Price C., Quail M.A., Rabbinowitch E., RA Reitter C., Rutherford K., Sasse J., Sharp S., Shownkeen R., Macleod A., RA Taylor S., Tweedie A., Turner C.M.R., Tait A., Gull K., Barrell B., RA Melville S.E.; RT "The DNA sequence of chromosome I of an African trypanosome: gene content, RT chromosome organisation, recombination and polymorphism."; RL Nucleic Acids Res. 31:4864-4873(2003). RN [2] {ECO:0000313|Proteomes:UP000008524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=927/4 GUTat10.1 {ECO:0000313|Proteomes:UP000008524}; RX PubMed=16020726; DOI=10.1126/science.1112642; RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H., RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U., RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B., RA Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F., RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C., RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A., RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D., RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D., RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S., RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S., RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G., RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A., RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M., RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S., RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S., RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E., RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E., RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.; RT "The genome of the African trypanosome Trypanosoma brucei."; RL Science 309:416-422(2005). RN [3] {ECO:0007829|PDB:2W7T} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 319-589. RG Structural Genomics Consortium (SGC); RA Welin M., Moche M., Arrowsmith C.H., Berglund H., Bountra C., Collins R., RA Dahlgren L.G., Edwards A.M., Flodin S., Flores A., Graslund S., RA Hammarstrom M., Johansson A., Johansson I., Karlberg T., Kotenyova T., RA Lehtio L., Nilsson M.E., Nyman T., Persson C., Sagemark J., Schueler H., RA Siponen M.I., Thorsell A.G., Tresaugues L., Van Den Berg S., Weigelt J., RA Wikstrom M., Wisniewska M., Nordlund P.; RT "Trypanosoma Brucei Ctps - Glutaminase Domain with Bound Acivicin."; RL Submitted (DEC-2008) to the PDB data bank. CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with CC either L-glutamine or ammonia as the source of nitrogen. CC {ECO:0000256|RuleBase:RU810713}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L- CC glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2; CC Evidence={ECO:0000256|ARBA:ARBA00000314, CC ECO:0000256|RuleBase:RU810713}; CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CC CTP from UDP: step 2/2. {ECO:0000256|ARBA:ARBA00005171, CC ECO:0000256|RuleBase:RU810713}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000256|ARBA:ARBA00007533, ECO:0000256|RuleBase:RU810713}. 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; AL929603; CAJ16071.1; -; Genomic_DNA. DR RefSeq; XP_001218826.1; XM_001218825.1. DR PDB; 2W7T; X-ray; 2.10 A; A=319-589. DR PDBsum; 2W7T; -. DR AlphaFoldDB; Q4GZ95; -. DR SMR; Q4GZ95; -. DR STRING; 185431.Q4GZ95; -. DR PaxDb; 5691-CAJ16071; -. DR GeneID; 4357199; -. DR KEGG; tbr:TB927.1.1240; -. DR VEuPathDB; TriTrypDB:Tb11.v5.0356; -. DR VEuPathDB; TriTrypDB:Tb927.1.1240; -. DR eggNOG; KOG2387; Eukaryota. DR InParanoid; Q4GZ95; -. DR OMA; HAAMYCH; -. DR OrthoDB; 166427at2759; -. DR UniPathway; UPA00159; UER00277. DR EvolutionaryTrace; Q4GZ95; -. DR Proteomes; UP000008524; Chromosome 1. DR GO; GO:0036064; C:ciliary basal body; IDA:GeneDB. DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; EXP:GeneDB. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006241; P:CTP biosynthetic process; EXP:GeneDB. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central. DR CDD; cd03113; CTPS_N; 1. DR CDD; cd01746; GATase1_CTP_Synthase; 1. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR004468; CTP_synthase. DR InterPro; IPR017456; CTP_synthase_N. DR InterPro; IPR017926; GATASE. DR InterPro; IPR033828; GATase1_CTP_Synthase. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR00337; PyrG; 1. DR PANTHER; PTHR11550; CTP SYNTHASE; 1. DR PANTHER; PTHR11550:SF0; CTP SYNTHASE-RELATED; 1. DR Pfam; PF06418; CTP_synth_N; 1. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2W7T}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU810713}; KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962, KW ECO:0000256|PROSITE-ProRule:PRU00605}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU810713}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU810713}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, KW ECO:0000256|RuleBase:RU810713}; KW Reference proteome {ECO:0000313|Proteomes:UP000008524}. FT DOMAIN 27..295 FT /note="CTP synthase N-terminal" FT /evidence="ECO:0000259|Pfam:PF06418" FT DOMAIN 339..567 FT /note="Glutamine amidotransferase" FT /evidence="ECO:0000259|Pfam:PF00117" FT ACT_SITE 419 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 549 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 551 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" SQ SEQUENCE 589 AA; 65213 MW; C3005DABAE3C386E CRC64; MEGSATAKAY MLPSPELRPV SGTGACKYIV VTGGVCSSLG KGVTTSATGA LLRAEGYQVC SIKIDPYINM DAGLMSPYEH GEVYVLDDGG EVDLDLGNYE RWMSVQLRRE HNITTGKVYQ KLINKERQGG FLGKTVQLVP HFTNDVVESI FRVSQSPVDE SGAQPEICMI ELGGTVGDME SQPFVEALRR LRCLVGPDEF CLMHTTYLPV FGGSQKTKPT QHSTRTLLSM GLQPDILICR SENRLTPDAK EKLSNLCGVR SGDIVSAPNV SCLYEVPVVF TKDGLVDRLV EKLRLVKRTP ATDVPRIDTY KTYVKILRNM SNPTVRIAFV GKYLQDAGDT YFSVLQCFEH CQIALQVRLD ILYVDSEELE GPNADEARKA LLGCDGIFVP GGFGNRGVDG KCAAAQVARM NNIPYFGVCL GMQVAVIELS RNVVGWSDAN SEEFNKESTH QVVRIMDCDR NKMGANMHLG ACDVHIVEKS SIMAKIYSKS NIVVERHRHR YEVNTAYFED LRKAGLCISA VTDPTFSSRC RVEAVENPSL RFFLAVQFHP EFISTPMDPA PTYLSFMAAA AKKDYVWPQK CSQRRLKQA //