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Database: UniProt
Entry: A0A1L8ZBC7_BORBI
LinkDB: A0A1L8ZBC7_BORBI
Original site: A0A1L8ZBC7_BORBI 
ID   A0A1L8ZBC7_BORBI        Unreviewed;       168 AA.
AC   A0A1L8ZBC7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
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:OJH15070.1};
GN   ORFNames=ER70_04860 {ECO:0000313|EMBL:OJH15070.1};
OS   Borrelia bissettiae (Borreliella bissettiae).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borreliella.
OX   NCBI_TaxID=64897 {ECO:0000313|EMBL:OJH15070.1, ECO:0000313|Proteomes:UP000183624};
RN   [1] {ECO:0000313|EMBL:OJH15070.1, ECO:0000313|Proteomes:UP000183624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO275 {ECO:0000313|EMBL:OJH15070.1,
RC   ECO:0000313|Proteomes:UP000183624};
RX   PubMed=26419825; DOI=10.1099/mic.0.000192;
RA   Leydet B.F.Jr., Liang F.T.;
RT   "Similarities in murine infection and immune response to Borrelia bissettii
RT   and Borrelia burgdorferi sensu stricto.";
RL   Microbiology 161:2352-2360(2015).
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}.
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:OJH15070.1}.
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DR   EMBL; JNBW01000245; OJH15070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L8ZBC7; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000183624; 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-KW.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017926; GATASE.
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, ECO:0000313|EMBL:OJH15070.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT   DOMAIN          4..167
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OJH15070.1"
FT   NON_TER         168
FT                   /evidence="ECO:0000313|EMBL:OJH15070.1"
SQ   SEQUENCE   168 AA;  18835 MW;  C6CFC089D3202EE2 CRC64;
     AELDDSYASI RESLVHVAAN LDLLIKSTII DSNDLNENRL KEFDGIIVPG GFGGKGYEGK
     IMAIKYAREN NIPFLGICLG LQLAVIEFAR NVCGIFDADT EENLAKDKPL KSPVIHLLPE
     QKEIKDKGAT MRLGGYPVIL KKNTIAFKLY GQDRIIERFR HRYEVNND
//
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