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Database: UniProt
Entry: A0A0J1CRK6_9BURK
LinkDB: A0A0J1CRK6_9BURK
Original site: A0A0J1CRK6_9BURK 
ID   A0A0J1CRK6_9BURK        Unreviewed;       231 AA.
AC   A0A0J1CRK6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE            EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN   ORFNames=EOS_27875 {ECO:0000313|EMBL:KLU22951.1};
OS   Caballeronia mineralivorans PML1(12).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU22951.1, ECO:0000313|Proteomes:UP000035963};
RN   [1] {ECO:0000313|EMBL:KLU22951.1, ECO:0000313|Proteomes:UP000035963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX   PubMed=26205858;
RA   Uroz S., Oger P.;
RT   "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT   Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT   Ability.";
RL   Genome Announc. 3:e00798-15(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:KLU22951.1}.
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DR   EMBL; AEJF01000168; KLU22951.1; -; Genomic_DNA.
DR   RefSeq; WP_047895421.1; NZ_AEJF01000168.1.
DR   AlphaFoldDB; A0A0J1CRK6; -.
DR   PATRIC; fig|908627.4.peg.6234; -.
DR   OrthoDB; 9801107at2; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000035963; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT   DOMAIN          27..227
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
SQ   SEQUENCE   231 AA;  24844 MW;  CB00BB59942B2A9C CRC64;
     MRKKVMVGLV GDYNQSVPAH RAIPLALKRA ADAKQVEVEF EWVPTGDIIS VSRISAFDGI
     WCVPASPYHS MEGALLAIRH AREAAIPFLG TCGGFQHAVI EYARNVLGWA DAEHAETAPG
     AARAVISPLE CALVETVDLV RLLPGTHIAA AYGVSETTEG YRCRYGLNPE FRTSLVSGPL
     RVAADDETGD VRAVEMDGHP FFVATLFQPE RAALREESAL LVNAFVEACG A
//
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