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Database: UniProt
Entry: E2FU13_9THEO
LinkDB: E2FU13_9THEO
Original site: E2FU13_9THEO 
ID   E2FU13_9THEO            Unreviewed;       409 AA.
AC   E2FU13;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE            EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
DE   Flags: Fragment;
GN   Name=pyrG {ECO:0000313|EMBL:ADN19453.1};
OS   Thermoanaerobacter uzonensis.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=447593 {ECO:0000313|EMBL:ADN19453.1};
RN   [1] {ECO:0000313|EMBL:ADN19453.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JW/IW_A615_31 {ECO:0000313|EMBL:ADN19453.1};
RA   Wagner I.D., Varghese L., Wiegel J.;
RT   "Universally conserved protein coding gene sequence heterogeneity among
RT   Thermoanaerobacter uzonensis isolates from geothermal springs of Kamchatka,
RT   Russian Far East.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2. {ECO:0000256|ARBA:ARBA00005171}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007533}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR   EMBL; HM191136; ADN19453.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2FU13; -.
DR   UniPathway; UPA00159; UER00277.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT   DOMAIN          1..185
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          220..404
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADN19453.1"
FT   NON_TER         409
FT                   /evidence="ECO:0000313|EMBL:ADN19453.1"
SQ   SEQUENCE   409 AA;  46314 MW;  91E42FE78BC8DB0E CRC64;
     LTKNSNVTAG KVYWTVITKE RKGDYLGATV QVIPHITNEI KERVYRVAKE KNVDVVITEI
     GGTVGDIESL PFLEAIRQVA IEQGRENVMF IHVTLVPHLG KTGELKTKPT QHSVKELRSI
     GIQPDMIVCR TELPLTQDLK EKIALFCNVS VEAVIENRDV ESIYQVPLEL ERQKVDEYVL
     KRLNLPIEES DLKEWREYVE REKNPTRQVE VALVGKYVDL HDAYISVVEA LKHGGVYHRA
     AVNIRWVNAE HVNDETVEKL LKGADGILVP GGFGDRGIEG KIRAIQYARE NKIPYLGLCL
     GMQCAVIEFA RNVAGLKGAN STEFDPDTSH PVIDLMPEQK DIDEKGGTMR LGVYPCKVIE
     GTKAYEAYKD ELIYERHRHR YEFNNQYREL LTSKGLVLSG LSPDERLVE
//
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