ID A0A1G2CXS9_9BACT Unreviewed; 554 AA.
AC A0A1G2CXS9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN ORFNames=A2845_01475 {ECO:0000313|EMBL:OGZ06067.1};
OS Candidatus Lloydbacteria bacterium RIFCSPHIGHO2_01_FULL_49_22.
OC Bacteria; Candidatus Lloydbacteria.
OX NCBI_TaxID=1798658 {ECO:0000313|EMBL:OGZ06067.1, ECO:0000313|Proteomes:UP000177122};
RN [1] {ECO:0000313|EMBL:OGZ06067.1, ECO:0000313|Proteomes:UP000177122}
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:OGZ06067.1}.
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DR EMBL; MHLI01000005; OGZ06067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2CXS9; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000177122; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..269
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 310..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 554 AA; 60944 MW; A52BBFB6FE555016 CRC64;
MAKAHKYIFV AGGVMSGVGK GVATSSIALL LQARGFKISP IKIDPYLNVD AGTMNPTEHG
EVFVLKSGLE TDQDMGSYER FLGRDLNTEN YMTGGLIYKT VIDRERALGY GGRCVEPVPH
IPEEVIRRIK DAGEKDKSDI TIVEIGGTLG EYQSVMFIEA ARTLKMANPD DVLFVLVTYL
PVPGKLGEMK TKPTQYAVRT MNSYGVQPDI IIARGEVPVD MKRKEKIASS SGMRVEQVIS
APDVDSVYDV PLNFEADNIA TIVMKLLKLK SKKPVDLAPW KGFVRKTKNT KGEVRIGMVG
KYFATGDFVL ADSYLSVIEA LKYAAFHAGK RPVIDWIAAT DFEGTNAAKN CAKLAQYDGI
VVPGGFGARG IEGKLNVIKY VRTHKIPYFG LCYGMQLMVA EYARNVLGLK GAITTEIDPK
TKYPVVAVMP DQQVKLDAGD YGGSMRLGSY PAYLKEGTVA RGAYKAEMVH ERHRHRYEVN
PEYVAAIEKA GLVFSGISPD EKLMEIAELP KLKHPFFLGT QFHPEFTARP LTSHPLFDAF
IKACVSSRAT SKKK
//
