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Database: UniProt
Entry: A4HYQ5_LEIIN
LinkDB: A4HYQ5_LEIIN
Original site: A4HYQ5_LEIIN 
ID   A4HYQ5_LEIIN            Unreviewed;       600 AA.
AC   A4HYQ5; A0A2K4YSU8; A0A381MGK4;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 94.
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=LINJ_20_0630 {ECO:0000313|EMBL:CAM67443.1};
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM67443.1, ECO:0000313|Proteomes:UP000008153};
RN   [1] {ECO:0000313|EMBL:CAM67443.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM67443.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM67443.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM67443.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
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}.
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DR   EMBL; FR796452; CAM67443.1; -; Genomic_DNA.
DR   RefSeq; XP_001465196.1; XM_001465159.1.
DR   AlphaFoldDB; A4HYQ5; -.
DR   SMR; A4HYQ5; -.
DR   STRING; 5671.A4HYQ5; -.
DR   GeneID; 5068611; -.
DR   KEGG; lif:LINJ_20_0630; -.
DR   VEuPathDB; TriTrypDB:LINF_200011000; -.
DR   eggNOG; KOG2387; Eukaryota.
DR   InParanoid; A4HYQ5; -.
DR   OMA; FKPGTEW; -.
DR   OrthoDB; 166427at2759; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000008153; Chromosome 20.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008153}.
FT   DOMAIN          30..298
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          342..569
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        422
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        552
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        554
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   600 AA;  66412 MW;  5C22F1A4E71E0CCB CRC64;
     MEERKTASGS AYYLPSPLLL SQNQGEERVK FVVVSGGVCS SLGKGVTTSA IGALLHASGY
     RVCSIKIDPY INIDAGLMSP YEHGEVYVLE DGGEADLDLG NYERWMSVHL TRDHNITTGK
     VYQKLLTKER AGGFLGKTVQ LVPHFTNEVV NHIFKICQTP MSGSNKRPEI CMIELGGTVG
     DMESQPFVEA LRRLRYSILP EDFCLLHTTY LPVFGGTQKT KPTQHSCRAL LSLGLQPDFL
     VCRSEQPLAA DVKAKLSDQC GVQSKDIIGA PDVNCLYQIP VKFVDQGLID RLLHKLRLRP
     NMPPTDAPTY QTFKKFSDIL QNPNNQKVRI AFVGKYVTGG SDAYFSVLQC FEHCQLALGI
     NVEVFYLESE QLEGENAEEA KAALLECDGI FVPGGFGVRG IDGKVNAVRL AREHNIPYFG
     VCLGMQVALI EFARSQLGWE DANSEEFDAS STRQVVRIMD ADRERMGANM HLGAREVHIV
     EPHSRMSTIY SGAKVVLERH RHRYEVHGKY LNDLRKQGLV ISAVSDPDAG ENLRVEAIEN
     PSLKFFLAVQ FHPEFVSTPL DPSPPYLAFF AAAAGKEVNW PAECTARRLP ASAQLSQACR
//
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