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CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)

 PYRG_EHRCJ              Reviewed;         538 AA.
Q3YSZ0;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 1.
10-OCT-2018, entry version 90.
RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227};
EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227};
AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01227};
AltName: Full=Cytidine triphosphate synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
Short=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
Short=CTPS {ECO:0000255|HAMAP-Rule:MF_01227};
AltName: Full=UTP--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_01227};
Name=pyrG {ECO:0000255|HAMAP-Rule:MF_01227};
OrderedLocusNames=Ecaj_0114;
Ehrlichia canis (strain Jake).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Anaplasmataceae; Ehrlichia.
NCBI_TaxID=269484;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Jake;
PubMed=16707693; DOI=10.1128/JB.01837-05;
Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P.,
Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C.,
Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W.,
Kyrpides N.C.;
"The genome of the obligately intracellular bacterium Ehrlichia canis
reveals themes of complex membrane structure and immune evasion
strategies.";
J. Bacteriol. 188:4015-4023(2006).
-!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
either L-glutamine or ammonia as the source of nitrogen. Regulates
intracellular CTP levels through interactions with the four
ribonucleotide triphosphates. {ECO:0000255|HAMAP-Rule:MF_01227}.
-!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate +
CTP + L-glutamate. {ECO:0000255|HAMAP-Rule:MF_01227}.
-!- ACTIVITY REGULATION: Allosterically activated by GTP, when
glutamine is the substrate; GTP has no effect on the reaction when
ammonia is the substrate. The allosteric effector GTP functions by
stabilizing the protein conformation that binds the tetrahedral
intermediate(s) formed during glutamine hydrolysis. Inhibited by
the product CTP, via allosteric rather than competitive
inhibition. {ECO:0000255|HAMAP-Rule:MF_01227}.
-!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP-
Rule:MF_01227}.
-!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01227}.
-!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for
distinguishing between UTP and CTP. The overlapping regions of the
product feedback inhibitory and substrate sites recognize a common
feature in both compounds, the triphosphate moiety. To
differentiate isosteric substrate and product pyrimidine rings, an
additional pocket far from the expected kinase/ligase catalytic
site, specifically recognizes the cytosine and ribose portions of
the product inhibitor. {ECO:0000255|HAMAP-Rule:MF_01227}.
-!- SIMILARITY: Belongs to the CTP synthase family.
{ECO:0000255|HAMAP-Rule:MF_01227}.
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EMBL; CP000107; AAZ68165.1; -; Genomic_DNA.
RefSeq; WP_011304243.1; NC_007354.1.
ProteinModelPortal; Q3YSZ0; -.
SMR; Q3YSZ0; -.
STRING; 269484.Ecaj_0114; -.
MEROPS; C26.964; -.
EnsemblBacteria; AAZ68165; AAZ68165; Ecaj_0114.
KEGG; ecn:Ecaj_0114; -.
eggNOG; ENOG4105C8D; Bacteria.
eggNOG; COG0504; LUCA.
HOGENOM; HOG000077515; -.
KO; K01937; -.
OMA; EFNNAYR; -.
OrthoDB; POG091H02IX; -.
BioCyc; ECAN269484:ECAJ_RS00610-MONOMER; -.
UniPathway; UPA00159; UER00277.
Proteomes; UP000000435; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
CDD; cd01746; GATase1_CTP_Synthase; 1.
Gene3D; 3.40.50.880; -; 1.
HAMAP; MF_01227; PyrG; 1.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR004468; CTP_synthase.
InterPro; IPR017456; CTP_synthase_N.
InterPro; IPR017926; GATASE.
InterPro; IPR033828; GATase1_CTP_Synthase.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11550; PTHR11550; 1.
Pfam; PF06418; CTP_synth_N; 1.
Pfam; PF00117; GATase; 1.
SUPFAM; SSF52317; SSF52317; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00337; PyrG; 1.
PROSITE; PS51273; GATASE_TYPE_1; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase;
Magnesium; Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis;
Reference proteome.
CHAIN 1 538 CTP synthase.
/FTId=PRO_0000266111.
DOMAIN 295 537 Glutamine amidotransferase type-1.
{ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 19 24 ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 151 153 Allosteric inhibitor CTP.
{ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 191 196 Allosteric inhibitor CTP; alternate.
{ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 191 196 UTP; alternate. {ECO:0000255|HAMAP-
Rule:MF_01227}.
REGION 1 270 Amidoligase domain. {ECO:0000255|HAMAP-
Rule:MF_01227}.
REGION 384 387 L-glutamine binding. {ECO:0000255|HAMAP-
Rule:MF_01227}.
ACT_SITE 383 383 Nucleophile; for glutamine hydrolysis.
{ECO:0000255|HAMAP-Rule:MF_01227}.
ACT_SITE 510 510 {ECO:0000255|HAMAP-Rule:MF_01227}.
ACT_SITE 512 512 {ECO:0000255|HAMAP-Rule:MF_01227}.
METAL 76 76 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01227}.
METAL 144 144 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01227}.
BINDING 18 18 Allosteric inhibitor CTP; alternate.
{ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 18 18 UTP; alternate. {ECO:0000255|HAMAP-
Rule:MF_01227}.
BINDING 76 76 ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 227 227 Allosteric inhibitor CTP; alternate.
{ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 227 227 UTP; alternate. {ECO:0000255|HAMAP-
Rule:MF_01227}.
BINDING 356 356 L-glutamine; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 407 407 L-glutamine. {ECO:0000255|HAMAP-
Rule:MF_01227}.
BINDING 463 463 L-glutamine; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01227}.
SEQUENCE 538 AA; 60221 MW; 71E12065EA4A1413 CRC64;
MSNQTSSRFI FVTGGVVSSL GKGLAAASIG ALLQARGFKI CLRKLDPYLN IDPGTMSPIQ
HGEVFVTDDG AETDLDLGHY ERFTGVKTTK NDNITTGKVY HNLLKKERRG DYLGQTVQII
PHVTDLINSF ILHNTEGLDF VICEIGGTVG DIESQPFLES IRQIGYKLSK NNTIFVHLTL
VPYIDAAMEL KTKPTQHSVK ELSAVGIQPD IILYRSKIPL SKEQRDKIAN LCNVSPTNII
PALDVKNIYE LPISYHNYNL DTQILKHFNV NSPDPNLSKW ENILNISHTL TKTVTVAIIG
KYIKLLDAYK SLIEALEHAS IHNRVKLSIR WIDSRSLDSN GINAFDNVDS ILIPGGFGDD
GVKGKITAIT HARLNKIPFL GICMGMQLAI VEFANNVAHL EDANSTEFNL YCKNPVIHQL
PELQQNFLGG SMKLGSCPCY LDANSKIFSI YQQSVINERR RHRYTFNLQY KDLLEQHGLT
FTGKANNTDD SLIEVIELNN HPWFIGVQFH PEFKSSPFHS HPLFISFIKA SLSYQEAK


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