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Database: UniProt
Entry: A0A085GMP8_9GAMM
LinkDB: A0A085GMP8_9GAMM
Original site: A0A085GMP8_9GAMM 
ID   A0A085GMP8_9GAMM        Unreviewed;       423 AA.
AC   A0A085GMP8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE            EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN   ORFNames=GEAM_0520 {ECO:0000313|EMBL:KFC84993.1};
OS   Ewingella americana ATCC 33852.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Ewingella.
OX   NCBI_TaxID=910964 {ECO:0000313|EMBL:KFC84993.1, ECO:0000313|Proteomes:UP000028640};
RN   [1] {ECO:0000313|EMBL:KFC84993.1, ECO:0000313|Proteomes:UP000028640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33852 {ECO:0000313|EMBL:KFC84993.1,
RC   ECO:0000313|Proteomes:UP000028640};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:KFC84993.1}.
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DR   EMBL; JMPJ01000022; KFC84993.1; -; Genomic_DNA.
DR   RefSeq; WP_034787878.1; NZ_JMPJ01000022.1.
DR   AlphaFoldDB; A0A085GMP8; -.
DR   STRING; 910964.GEAM_0520; -.
DR   GeneID; 78378864; -.
DR   eggNOG; COG0504; Bacteria.
DR   OrthoDB; 9813383at2; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000028640; 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:KFC84993.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028640}.
FT   DOMAIN          184..387
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
SQ   SEQUENCE   423 AA;  46317 MW;  5A05452CC76C0D48 CRC64;
     MTITFIAHST PEPALYGAMA AILAELRALP LCHLPVTHDA KRFANARQHV TAQGQQLTSG
     LVWLERLTGR SPGAEMDLDS LITRALREDI VIPSIQPLDR ELALRAAENG IVVESLQVVK
     QQEKFHLEDV DTGKMRSNGW ARDIFGRWAF GSVLQPVMRG AQKLRIAVVG DMNEHAESYP
     ALLAALADAA DALALNIEVV GVSPTLSGSQ LDSVLFDVDG VLLPGLLPSL GEYPQNGLLA
     IATWALDHRL PVLGINQGMH HMVAALGQKT LGRERVVMHG PATLNALQTC LPVPQDSPRC
     MGNQQIYSQS GSRVAQIFGR ESTQRYNQRW SLNPELVDEL HGAGLEVSAT GEKGRGIAAV
     ELRDHPFFVG IQSHPELQSR RERASSLLMA FLQEIRQNIR QRDISHATLS KSVRLKQSYF
     SMG
//
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