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Database: UniProt
Entry: B1H2S0_XENTR
LinkDB: B1H2S0_XENTR
Original site: B1H2S0_XENTR 
ID   B1H2S0_XENTR            Unreviewed;       578 AA.
AC   B1H2S0;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 85.
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   Name=ctps2 {ECO:0000313|RefSeq:NP_001120396.1,
GN   ECO:0000313|Xenbase:XB-GENE-991292};
GN   Synonyms=LOC100145472 {ECO:0000313|EMBL:AAI61106.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI61106.1};
RN   [1] {ECO:0000313|RefSeq:NP_001120396.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAI61106.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testes {ECO:0000313|EMBL:AAI61106.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001120396.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen. Constitutes
CC       the rate-limiting enzyme in the synthesis of cytosine nucleotides.
CC       {ECO:0000256|ARBA:ARBA00037348}.
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; BC161106; AAI61106.1; -; mRNA.
DR   RefSeq; NP_001120396.1; NM_001126924.1.
DR   MEROPS; C26.964; -.
DR   GeneID; 100145472; -.
DR   KEGG; xtr:100145472; -.
DR   CTD; 56474; -.
DR   Xenbase; XB-GENE-991292; ctps2.
DR   OrthoDB; 166427at2759; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000008143; Chromosome 2.
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:SF2; CTP SYNTHASE 2; 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   2: Evidence at transcript level;
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:UP000008143}.
FT   DOMAIN          2..272
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          310..542
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        399
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        526
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        528
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   578 AA;  65183 MW;  B5BD538F4DF52151 CRC64;
     MKYILVTGGV ISGVGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV
     LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQQVINR ERRGDYLGKT VQVVPHITDA
     IQEWVLNQAK VPVDSDQKEP QICVIELGGT IGDIEGMPFI EAFRQFQFKA KRENFCNIHV
     SLVPQPSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSAK PIEMAVKQKI SMFCHVEPEQ
     VIFVHDVSST YRVPILLQEQ GIIKYFKQRL SIPIDDQPST LLFKWKRMAD RYERLLKTCS
     IALVGKYTKL SDCYTSVFKA LEHSALAINH KLNLMYIDSA DLEPSMKAED PVKYHKAWEE
     LCKAEGILVP GGFGLRGTEG KIQAITWARE RKIPFLGICL GMQLAVVEFA RNILKMTDAN
     STEFDPNTNN PVVIDMPEHH PGDMGGTMRL GRRKTVFKTS DSVIKKLYDN YEFVEERHRH
     RYEVNPELVH QFEEKGLKFV GQDNEGQRME IIELEGHPYF VGVQFHPEFC SRPMKPSPPY
     LGFMLAASGK FNSYVQNGCK LSPRNSYSEH SDESSSDS
//
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