ID S9TK56_9TRYP Unreviewed; 373 AA.
AC S9TK56;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=STCU_09884 {ECO:0000313|EMBL:EPY18542.1};
OS Strigomonas culicis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY18542.1, ECO:0000313|Proteomes:UP000015354};
RN [1] {ECO:0000313|EMBL:EPY18542.1, ECO:0000313|Proteomes:UP000015354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23560078;
RA Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA de Souza W., Schenkman S., de Vasconcelos A.T.;
RT "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT Family.";
RL PLoS ONE 8:E60209-E60209(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPY18542.1}.
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DR EMBL; ATMH01009884; EPY18542.1; -; Genomic_DNA.
DR AlphaFoldDB; S9TK56; -.
DR EnsemblProtists; EPY18542; EPY18542; STCU_09884.
DR OrthoDB; 3641227at2759; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000015354; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
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:UP000015354}.
FT DOMAIN 1..93
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 132..362
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 208
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 343
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 373 AA; 41745 MW; E7052198BDA45AC5 CRC64;
MHLTLVPSVS SSSELKTKPT QHSVQKLREI GIFPDVILCR ASRRISSEER SKISMFSNVP
MESVISVWNV DSIYKIPSIL QEQGVDDIVC KTMCFNPSPA DLSVWKKLVE RIENPSCDVD
IGIIGKYIDF TESYKSLIEA LAHAGIHTNS RVNIKYINSE DIENKGIDLI KNLDGIIVPG
GFGNRGIEGK IMAINYAREN KIPFLGICLG MQLAVVEFAR NVAGLRNANS TEFDIDTKYP
VIALINEWKD ISGQIERRSV DSDKGGTLRK GAQNISVKNN TRTNGIYGAS LYERHRHRYE
VNNNYLKCLN DAGLIIGAST SSENLTEVIE LNDHPWFIGV QFHPEFTSTP RNGHPLFIDY
VKAIINRKFS KSV
//
