ID A0A1G2S5Z8_9BACT Unreviewed; 552 AA.
AC A0A1G2S5Z8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN ORFNames=A3D51_00330 {ECO:0000313|EMBL:OHA80520.1};
OS Candidatus Yonathbacteria bacterium RIFCSPHIGHO2_02_FULL_44_14.
OC Bacteria; Candidatus Yonathbacteria.
OX NCBI_TaxID=1802724 {ECO:0000313|EMBL:OHA80520.1, ECO:0000313|Proteomes:UP000179118};
RN [1] {ECO:0000313|EMBL:OHA80520.1, ECO:0000313|Proteomes:UP000179118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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: 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:OHA80520.1}.
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DR EMBL; MHUT01000018; OHA80520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2S5Z8; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000179118; Unassembled WGS sequence.
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-UniRule.
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 ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 7..270
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 312..542
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 392
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 523
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 525
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 552 AA; 61340 MW; F917D05BA6934860 CRC64;
MKKKTRKYIF VVGGVISGVG KGVTTSSIGK ILQSHGYRVT AMKIDPYVNV DAGTMNPTEH
GEVFVLKDGD ETDQDMGNYE RFLDTSLTCD NYMTTGRVYL SVIEKERALA YKGKCVQVVP
HIPYEVIDRI NHAVDKANAE IVVIEVGGTV GEYENILFLE TARMLKIKNP DDVLFAIVSY
LPTPSKIGEM KTKPTQHAVR ALNSAGIQPD FIIARSDMAL DVKRKEKLAL FCNMLPDGVI
SAPDVDSIYD IPGNFEKDRL GEKILKRLKL KSRGSNEKWK EWEAFARKAG KVKDEVRIAV
VGKYFDTGDY VLADSYLSII EALKYSAIAQ GKKARLVWLS SATFEGKNPP LTELIGFDGI
LVPGGFGSRG VEGKLNVIRF AREHKIPYFG ICYGMQLAVI EYARNVLGFK DATSREIDPK
SKHIIIDIME GQKENIEKGN LGGSMRLGAY PAVLKKGTIA RAAYGRDLIV ERHRHRFEVN
PEYVGALEEK GLVFSGKSPD GLLMEISELP ASVHPFFLGT QFHPEFEARP LSPHPIFNAF
IKATIARNKQ SK
//
