ID E0SGI5_DICD3 Unreviewed; 259 AA.
AC E0SGI5;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN OrderedLocusNames=Dda3937_01579 {ECO:0000313|EMBL:ADM96471.1};
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADM96471.1, ECO:0000313|Proteomes:UP000006859};
RN [1] {ECO:0000313|EMBL:ADM96471.1, ECO:0000313|Proteomes:UP000006859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937 {ECO:0000313|EMBL:ADM96471.1,
RC ECO:0000313|Proteomes:UP000006859};
RX PubMed=21217001; DOI=10.1128/JB.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR EMBL; CP002038; ADM96471.1; -; Genomic_DNA.
DR AlphaFoldDB; E0SGI5; -.
DR STRING; 198628.Dda3937_01579; -.
DR KEGG; ddd:Dda3937_01579; -.
DR eggNOG; COG0504; Bacteria.
DR HOGENOM; CLU_081279_0_0_6; -.
DR OMA; PFLGTCG; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000006859; Chromosome.
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 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:ADM96471.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000006859}.
FT DOMAIN 58..238
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
SQ SEQUENCE 259 AA; 28662 MW; CD615C3EF3B210AA CRC64;
MPPLTIKPTT STLPPICRSL LFYQPENVMK QIVRIALIGD YTPTVTAHQA IPPALDLAAR
QLDLTTQYQW IDSELLSPAS QLDAFDAVWC VPASPYRHDD NILQAIRFAR ETHIPFLGTC
GGCQYALLEY ARHVLSWHDA NNAEVTQEGR AVISPLQCEM VEKQGDIRLS PDSRIGRAYG
RDAIAEGYRC RYGINEAFRD AFTTAGVRVS GVDDNGDIRA VELTDHPFFV GTLFQPERAA
LKQIAPPLAI ALLEAASVR
//