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Entry: K0KIU4_WICCF
LinkDB: K0KIU4_WICCF
Original site: K0KIU4_WICCF 
ID   K0KIU4_WICCF            Unreviewed;       574 AA.
AC   K0KIU4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=CTP1 {ECO:0000313|EMBL:CCH42082.1};
GN   ORFNames=BN7_1621 {ECO:0000313|EMBL:CCH42082.1};
OS   Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS   3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH42082.1, ECO:0000313|Proteomes:UP000009328};
RN   [1] {ECO:0000313|EMBL:CCH42082.1, ECO:0000313|Proteomes:UP000009328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC   Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX   PubMed=23193139; DOI=10.1128/EC.00258-12;
RA   Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA   Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA   Tauch A., Kohler T., Brinkrolf K.;
RT   "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL   Eukaryot. Cell 11:1582-1583(2012).
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:CCH42082.1}.
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DR   EMBL; CAIF01000034; CCH42082.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0KIU4; -.
DR   STRING; 1206466.K0KIU4; -.
DR   eggNOG; KOG2387; Eukaryota.
DR   HOGENOM; CLU_011675_5_0_1; -.
DR   InParanoid; K0KIU4; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000009328; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009328}.
FT   DOMAIN          2..270
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          315..550
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        404
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        533
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        535
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   574 AA;  63903 MW;  908830D4DDD33D04 CRC64;
     MKYVVVSGGV ISGIGKGVLA SSTGLLLKTL GLRVTSIKID PYMNIDAGTM SPLEHGEVFV
     LNDGGEADLD LGNYERYLNI TLTRDHNITT GKVYQQVIER ERKGDYLGKT VQVVPHLTNA
     IQDWIERVAK VPVDDTGLEP EVCIIELGGT VGDIESAPFV EALRQFQFRV GHENFALIHV
     SLVPVIHGEQ KTKPTQAAIK DLRSLGLSPD VIACRCSEKL EKPVIDKISM FCHVGPNQVL
     GVHDLNSTYH VPLLLIDQKM TKYLTQRLSL DSLNVKPEAK AKGEDLLNRW KVLTTKYDRS
     FETVKIALVG KYTHLKDSYI SVIKSLEHSS MRVSRRLEIV WVEASDLELE SNDTDKVKYH
     KAWHSLCCAD GILVPGGFGS RGTEGMMQAA KWARENKIPF LGVCLGFQVA TIEFVRNVVG
     ITNSNSQEFV PELSDEEATV VYMPEIDKDK LGGTMRLGLR ETVFQTEDSV LKKLYGGVDE
     ILERHRHRYE INPKLISKIE SKGLKFVGKD LAGERMEIFE LENHPYYVAA QYHPEYLSKV
     LDPSKPFLGL VAAASGVLDK VLNGEIKPIS QGDF
//
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