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Database: UniProt
Entry: F5HPC6_BORGR
LinkDB: F5HPC6_BORGR
Original site: F5HPC6_BORGR 
ID   F5HPC6_BORGR            Unreviewed;       201 AA.
AC   F5HPC6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 31.
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:BAK23830.1};
OS   Borreliella garinii (Borrelia garinii).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borreliella.
OX   NCBI_TaxID=29519 {ECO:0000313|EMBL:BAK23830.1};
RN   [1] {ECO:0000313|EMBL:BAK23830.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=J-15 {ECO:0000313|EMBL:BAK23830.1};
RX   PubMed=21411595; DOI=10.1128/JCM.02544-10;
RA   Takano A., Nakao M., Masuzawa T., Takada N., Yano Y., Ishiguro F.,
RA   Fujita H., Ito T., Ma X., Oikawa Y., Kawamori F., Kumagai K., Mikami T.,
RA   Hanaoka N., Ando S., Honda N., Taylor K., Tsubota T., Konnai S.,
RA   Watanabe H., Ohnishi M., Kawabata H.;
RT   "Multilocus Sequence Typing Implicates Rodents as the Main Reservoir Host
RT   of Human-Pathogenic Borrelia garinii in Japan.";
RL   J. Clin. Microbiol. 49:2035-2039(2011).
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}.
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DR   EMBL; AB556298; BAK23830.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5HPC6; -.
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   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; IPR027417; P-loop_NTPase.
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.
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..102
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          141..199
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAK23830.1"
FT   NON_TER         201
FT                   /evidence="ECO:0000313|EMBL:BAK23830.1"
SQ   SEQUENCE   201 AA;  21987 MW;  3FCA53FFE003F972 CRC64;
     GSGNIAFIHL TYVPSPAGIN EQKSKPTQQS VKTLNKAGIF PDLIIARSSQ VLTDQIRKKV
     AMFCNVESTS IIDNIDVSTI YEIPISFYKQ GVHEILSSKL NIKVDPKIEE LSKLVGIIKS
     NFFVPKKIIN IAICGKYAEL DDSYASIRES LVHVGANLDL LIKSTLIDSN DLNESYLKEF
     DGIIVPGGFG GKGYEGKIIA I
//
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