ID F2S9E0_TRIT1 Unreviewed; 550 AA.
AC F2S9E0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=TESG_07510 {ECO:0000313|EMBL:EGE00190.1};
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933;
RN [1] {ECO:0000313|EMBL:EGE00190.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818 {ECO:0000313|EMBL:EGE00190.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Henn M., Martinez D., Young S.K., Zeng Q., Gargeya S., Haas B.,
RA Alvarado L., Berlin A., Chapman S., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Larson L., Mehta T., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., White T.C.,
RA Abdel-Rahman S., Graser Y., Gurr S.J., Kohler G., Martinez-Rossi N.,
RA Oliver B.C., Rossi A., Shelest E., Summerbell R., Lander E., Nusbaum C.,
RA Birren B.;
RT "Annotation of Trichophyton tonsurans strain CBS 112818.";
RL Submitted (JUL-2009) 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.
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}.
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DR EMBL; GG698533; EGE00190.1; -; Genomic_DNA.
DR AlphaFoldDB; F2S9E0; -.
DR HOGENOM; CLU_011675_5_0_1; -.
DR OrthoDB; 166427at2759; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000009172; 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; 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 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}.
FT DOMAIN 2..238
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 284..514
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 503
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 550 AA; 61149 MW; AC09E21BCD5236D3 CRC64;
MHVTSIKIDP YMNVDAGTMA PTEHGEVFVL NDGGEADLDL GNYERYLNVT LSRDNNITTG
KMYKHVIEKE RRGDYLGRTV QIVPHLTDAI QDWIERVART PADDSNEEPD VCVIELGGTL
GDIESAPFVE AMRQLRRRAG KNNFLQIHVS LVPAIHGELK TKPTQQAIRD ARSAGLSPDL
IACRCERALD KATTDKIAMF CQVEPEQVIG VHDVASTYHV PLLLEQQGFL GQLRDILKID
ELTIPQASID KGQNTWKQWK ALTTSQEHAY STVNIALVGK YVSLHDSYLS VIKSLEHSAM
ACHRKLKITW IDASNLEKSA AEANPEAFHK AWHDMCTADG ILVPGGFGTR GTEGMVAAAH
WARTKGKPYL GICLGMQIAV IEYARNVCGI PKASSIEFDD RTPDPLIVFM PEIDQVNLGG
TMRLGSRPTI FQQDSEWSKL RMLYGLSRAS IDERHRHRYE VNPEYIDTLQ KAGLHFIGKD
DKGERMEIIE LKDHPWFVGV QFHPEYLSRV LAPSKPFLGL VATAAGVFDE IMKSQACGKD
LASGVANIAI
//
