ID E1F224_GIAIA Unreviewed; 619 AA.
AC E1F224;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=GLP15_578 {ECO:0000313|EMBL:EFO63518.1};
OS Giardia intestinalis (strain P15) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=658858 {ECO:0000313|EMBL:EFO63518.1, ECO:0000313|Proteomes:UP000008974};
RN [1] {ECO:0000313|EMBL:EFO63518.1, ECO:0000313|Proteomes:UP000008974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P15 {ECO:0000313|EMBL:EFO63518.1,
RC ECO:0000313|Proteomes:UP000008974};
RX PubMed=20929575; DOI=10.1186/1471-2164-11-543;
RA Jerlstrom-Hultqvist J., Franzen O., Ankarklev J., Xu F., Nohynkova E.,
RA Andersson J.O., Svard S.G., Andersson B.;
RT "Genome analysis and comparative genomics of a Giardia intestinalis
RT assemblage E isolate.";
RL BMC Genomics 11:543-543(2010).
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:EFO63518.1}.
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DR EMBL; ACVC01000129; EFO63518.1; -; Genomic_DNA.
DR AlphaFoldDB; E1F224; -.
DR STRING; 658858.E1F224; -.
DR EnsemblProtists; EFO63518; EFO63518; GLP15_578.
DR VEuPathDB; GiardiaDB:GLP15_578; -.
DR OMA; HAAMYCH; -.
DR OrthoDB; 3641227at2759; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000008974; 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 5..275
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 344..610
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 382..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 455
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 591
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 593
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 619 AA; 67911 MW; 4DF37BB13811DFCC CRC64;
MQTYYIFVTG GVISGIGKGL FAASLGMLIK SYGYDVVMQK CDPYINVDPG LMSPYQHGEV
FVTDDGAETD LDLGHYERFL DTNLTRLSSV TTGSIYSTVI QREREGGYNG MTVQVVPQIV
DEIKARMRCF ELIPTVPGES SEPQRKHSAS LSSTQKRFVI IEIGGTVGDM ESTAFLEAMR
QLIDDVGRCN ACSFHVSYIP VLSNGKELKT KPTQHSVRTL LSVGIKPDFL VCRTDTHLPK
ETIAKLAHSC GLSKEHVIEN YTVQSIYQLP LLIKHVPALV FNLFNVVPIR ATAEKEAKAS
LDRWSEIVER FTHPATLTSD TLAGKESDEK PHIRIGLVGK YVELRDAYIS VYEAIHHAAA
HSNCYVDILS IVSDTCEGVD RASSSTSAPT AQSAEPTKSE EKSHTETHNL VPTAVTLENV
DAIIIPGGFG SRGVSGKLEA IKYCRQNNKP ILGICLGMQC MAIEFANNVL KLKDATSTEF
DPETTNPVIA TIISEDVKAA NPLAATLIRG SGGSMRLGAC NCTLINGTLA QRCYQCKSVR
ERHRHRYEFN GRYKTLFEEA GVVFSGLSTE SSLVEIMEIP SLDFFLGVQF HPELLSRPLK
PHPLFVGLIN AALTKKRGV
//
