ID A0A1Y1WGL1_9FUNG Unreviewed; 586 AA.
AC A0A1Y1WGL1;
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=DL89DRAFT_220386 {ECO:0000313|EMBL:ORX72649.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX72649.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX72649.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX72649.1,
RC ECO:0000313|Proteomes:UP000193922};
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:ORX72649.1}.
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DR EMBL; MCFD01000002; ORX72649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1WGL1; -.
DR STRING; 61395.A0A1Y1WGL1; -.
DR OrthoDB; 166427at2759; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000193922; 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:UP000193922}.
FT DOMAIN 6..276
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 321..558
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 410
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 542
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 544
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 586 AA; 64878 MW; 9F9DE47E86F27B6C CRC64;
MAKQTKYIIV SGGVISGIGK GIIASSTGLL LKTLGLTVTS IKIDPYLNID AGTLSPLDHG
EVFVLDDGGE VDLDLGNYER YLSVQLSRDN NITTGKIYRE VIEKERRGDY LGKTVQVVPH
ITNAIQDWVE RVGRVPTSQN GRIPDVCIVE LGGTVGDIES APFIEAMRQF QFRVGHDNFC
LIHVSLVPVV GAVGEQKTKP TQASVRDLRG LGLSPDILAC RSATPFEEGI REKLSMFCQV
RPEQVFSVHD CESLYHVPIL LRKQGIIDVL TERLKLNKLS ISGELQGEGD ALWAQWREFA
RRRARDLEVT TIAVVGKYTY LTDSYISVVK ALEHASLNVN RKIEISWVEA SDLEESSAQK
DPLKYHEAWQ RLCAADGILV PGGFGERGVE GKVLAAKWAR EHNVPYLGIC LGLQVAVIEF
ARHVAGLPTA HSAEFRENCD TPVVVFMPEI DRTTMGGTMR LGSRPTKFQG TSFAQNSKIR
QLYGSVDEVN ERHRHRYEVN PERVDELEAK GMHFVGRDAD TGERMEILEL ESHPYFVAVQ
YHPEYLTRPL SPSPPFLGLL LAASGQLDSY LSGAGIAADV DTKLKM
//
