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Database: UniProt
Entry: E2FTS7_9THEO
LinkDB: E2FTS7_9THEO
Original site: E2FTS7_9THEO 
ID   E2FTS7_9THEO            Unreviewed;       434 AA.
AC   E2FTS7;
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:ADN19367.1};
OS   Thermoanaerobacter uzonensis.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=447593 {ECO:0000313|EMBL:ADN19367.1};
RN   [1] {ECO:0000313|EMBL:ADN19367.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JW/IW_Z606_72 {ECO:0000313|EMBL:ADN19367.1}, and JW/IW_Z606_73
RC   {ECO:0000313|EMBL:ADN19368.1};
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; HM191050; ADN19367.1; -; Genomic_DNA.
DR   EMBL; HM191051; ADN19368.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2FTS7; -.
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   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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};
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..210
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          245..429
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADN19367.1"
FT   NON_TER         434
FT                   /evidence="ECO:0000313|EMBL:ADN19367.1"
SQ   SEQUENCE   434 AA;  49208 MW;  60B7F23AC88FED34 CRC64;
     EVFVTEDGAE TDLDLGHYER FIDINLTKNS NVTAGKVYWT VITKERKGDY LGATVQVIPH
     ITNEIKERVY RVAKEKNVDV VITEIGGTVG DIESLPFLEA IRQVAIEQGR ENVMFIHVTL
     VPHLGKTGEL KTKPTQHSVK ELRSIGIQPD MIVCRTELPL TQDLKEKIAL FCNVSVEAVI
     ENRDVESIYQ VPLELERQKV DEYVLKRLNL PIEESDLKEW REYVEREKNP TRQVEVALVG
     KYVDLHDAYI SVVEALKHAG VYHRAAVNIR WVNAEHVNDE TVEKLLKGAD GILVPGGFGD
     RGIEGKIRAI QYARENKIPY LGLCLGMQCA VIEFARNVAG LKGANSTEFD PDTSHPVIDL
     MPEQKDIDEK GGTMRLGVYP CKVIEGTKAY EAYKDELIYE RHRHRYEFNN QYRELLTSKG
     LVLSGLSPDE RLVE
//
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