ID E2FU53_9THEO Unreviewed; 182 AA.
AC E2FU53;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:ADN19493.1};
OS Thermoanaerobacter uzonensis.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=447593 {ECO:0000313|EMBL:ADN19493.1};
RN [1] {ECO:0000313|EMBL:ADN19493.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JW/IW_Z606_76 {ECO:0000313|EMBL:ADN19493.1};
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; HM191176; ADN19493.1; -; Genomic_DNA.
DR AlphaFoldDB; E2FU53; -.
DR MEROPS; C26.964; -.
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 CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR033828; GATase1_CTP_Synthase.
DR PANTHER; PTHR11550; CTP SYNTHASE; 1.
DR PANTHER; PTHR11550:SF0; CTP SYNTHASE-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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 2..181
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADN19493.1"
FT NON_TER 182
FT /evidence="ECO:0000313|EMBL:ADN19493.1"
SQ SEQUENCE 182 AA; 20474 MW; 2449FD05B58D0B82 CRC64;
LKHAGVYHRA AVNIRWVNAE HVNDETVEKL LKGADGILVP GGFGDRGIEG KIRAIQYARE
NKIPYLGLCL GMQCAVIEFA RNVAGLKGAN STEFDPDTSH PVIDLMPEQK DIDEKGGTMR
LGVYPCKVIE GTKAYEAYKD ELIYERHRHR YEFNNQYREL LTSKGLVLSG LSPDERLVEM
IE
//