PYG1A_XENLA
ID PYG1A_XENLA Reviewed; 591 AA.
AC Q5XHA8; Q642R7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=CTP synthase 1-A {ECO:0000305};
DE EC=6.3.4.2 {ECO:0000250|UniProtKB:P17812};
DE AltName: Full=CTP synthetase 1-A;
DE AltName: Full=UTP--ammonia ligase 1-A;
GN Name=ctps1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This enzyme is involved in the de novo synthesis of CTP, a
CC precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent
CC amination of UTP to CTP with either L-glutamine or ammonia as a source
CC of nitrogen. {ECO:0000250|UniProtKB:P17812}.
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:0000250|UniProtKB:P17812};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2. {ECO:0000250|UniProtKB:P17812}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5XHA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XHA8-2; Sequence=VSP_019890, VSP_019891, VSP_019892;
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR EMBL; BC081096; AAH81096.1; -; mRNA.
DR EMBL; BC084164; AAH84164.1; -; mRNA.
DR RefSeq; NP_001088219.1; NM_001094750.1. [Q5XHA8-1]
DR AlphaFoldDB; Q5XHA8; -.
DR SMR; Q5XHA8; -.
DR BioGRID; 105127; 1.
DR DNASU; 495047; -.
DR GeneID; 495047; -.
DR KEGG; xla:495047; -.
DR CTD; 495047; -.
DR Xenbase; XB-GENE-6254536; ctps1.S.
DR OrthoDB; 810128at2759; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 495047; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; ISS:UniProtKB.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006241; P:CTP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 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 PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Glutamine amidotransferase; Ligase;
KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..591
FT /note="CTP synthase 1-A"
FT /id="PRO_0000247030"
FT DOMAIN 300..554
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 399
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 526
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 528
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT VAR_SEQ 56..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019890"
FT VAR_SEQ 397..417
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019891"
FT VAR_SEQ 565..591
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019892"
FT CONFLICT 365
FT /note="E -> D (in Ref. 1; AAH81096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 66872 MW; 9A1140CA053223E7 CRC64;
MKYILVTGGV ISGIGKGVIA SSIGTILKSS NLHVTSIKID PYINIDAGTF SPYEHGEVFV
LDDGGEVDLD LGNYERFLDI RLTKDNNLTT GKIYQSVINK ERKGDYLGKT VQVVPHITDA
IQEWVMRQAL IPVDEDGIEP EVCVIELGGT VGDIESMPFV EAFRQFQFKV RRENFCNIHV
SLVPQPSATG EQKTKPTQNS VRELRGLGLS PDLVVCRCST PLDTSVKEKI SMFCHVEPQQ
VICVHDVSSI YRVPLLLEEQ GVVDYFRQRL DLPIGRQPRR LLMKWKEMAD RYERLLESCS
IALVGKYTKF SDSYASVIKA LEHSALAINH RLEIKYIDSA DLEQETLQEE PVRYHEAWQK
LCSSEGILVP GGFGVRGTEG KIQAIAWARK QKKPFLGVCL GMQLAVVEFA RDVLGWTDAN
STEFNPKTSH PVVIDMPEHN PGQMGGTMRL GKRRTIFHSQ NSIMKKLYGG HEYVEERHRH
RYEVNPELRR ELEVRGLKFV GQDTEGERME IVELEDHPYF VGVQYHPEFL SRPIKPSPPY
FGLLLASVGR LSQYIERGCR LSPRDTYSDR SENSSPDAEI AELKLPMIDH D