ID A0A1Y1YLU4_9FUNG Unreviewed; 594 AA.
AC A0A1Y1YLU4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=K493DRAFT_213978 {ECO:0000313|EMBL:ORX98564.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORX98564.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORX98564.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORX98564.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
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:ORX98564.1}.
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DR EMBL; MCFE01000111; ORX98564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1YLU4; -.
DR STRING; 1314790.A0A1Y1YLU4; -.
DR InParanoid; A0A1Y1YLU4; -.
DR OrthoDB; 166427at2759; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000193498; 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 HAMAP; MF_01227; PyrG; 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:UP000193498}.
FT DOMAIN 3..273
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 318..552
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 407
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 536
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 538
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 594 AA; 65869 MW; EFC504599D816758 CRC64;
MVKYILVSGG VISGIGKGII ASSTGLLLKT LGLRVTAIKI DPYLNIDAGT LSPLDHGEVF
VLDDGGEVDL DLGNYERFLD VTLSRENNIT TGKVYRNVIE KERKGDYLGK TVQVVPHITD
AIQDWVETVS KNPVDDSGEE PDVCIIELGG TVGDIESAPF VEAMRQFQFR VGHENFALIH
VSLIPVVGSV GEQKTKPTQA SIRDLRGLGL NPDFIACRSS KPLDEGIRDK ISMFCHVNPE
CVLAVRDVSS IYHVPLLLQQ QGALEAFRKR LNLDSISISP SMVREGHELW SKWRQVALRH
DRPQDEVTIA LVGKYTFLHD SYCSVVKALE HASLSSNLKL NIKWVEGTDL EPEAQHKDPI
KYHDSWQAVC SADGILIPGG FGIRGTEGKM LAIKWAREHN VPFLGICLGL QLAATEFARN
VLGLENAHSA EFVEDTPHPI AIYMPEISKT HLGGTMRLGV RPTIFQDGSE NSKIRRLYKG
AKTVEERHRH RYEINPAYID ALEAKGLKFI GRDEKGERMI ILEKEDHPYF VAAQFHPEYI
TRPLKPSPPF VGLVLAAAGK LDQYLESNNF AQYDSDSDSD GLSVNKILGD AEKH
//
