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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_HYPNA              Reviewed;         544 AA.
Q0C195;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 1.
07-JUN-2017, entry version 78.
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=HNE_1794;
Hyphomonas neptunium (strain ATCC 15444).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Hyphomonadaceae; Hyphomonas.
NCBI_TaxID=228405;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15444;
PubMed=16980487; DOI=10.1128/JB.00111-06;
Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T.,
Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E.,
Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A.,
Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C.,
Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D.,
Davidsen T.M., Yang Q., Zafar N., Ward N.L.;
"Comparative genomic evidence for a close relationship between the
dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
crescentus.";
J. Bacteriol. 188:6841-6850(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}.
-!- ENZYME 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; CP000158; ABI78786.1; -; Genomic_DNA.
RefSeq; WP_011646798.1; NC_008358.1.
ProteinModelPortal; Q0C195; -.
SMR; Q0C195; -.
STRING; 228405.HNE_1794; -.
MEROPS; C26.964; -.
EnsemblBacteria; ABI78786; ABI78786; HNE_1794.
KEGG; hne:HNE_1794; -.
eggNOG; ENOG4105C8D; Bacteria.
eggNOG; COG0504; LUCA.
HOGENOM; HOG000077515; -.
KO; K01937; -.
OMA; EFNNAYR; -.
OrthoDB; POG091H02IX; -.
UniPathway; UPA00159; UER00277.
Proteomes; UP000001959; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-EC.
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 1 544 CTP synthase.
/FTId=PRO_0000266135.
DOMAIN 292 543 Glutamine amidotransferase type-1.
{ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 14 19 ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 147 149 Allosteric inhibitor CTP.
{ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 187 192 Allosteric inhibitor CTP; alternate.
{ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 187 192 UTP; alternate. {ECO:0000255|HAMAP-
Rule:MF_01227}.
NP_BIND 239 241 ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
REGION 1 266 Amidoligase domain. {ECO:0000255|HAMAP-
Rule:MF_01227}.
REGION 383 386 L-glutamine binding. {ECO:0000255|HAMAP-
Rule:MF_01227}.
ACT_SITE 382 382 Nucleophile; for glutamine hydrolysis.
{ECO:0000255|HAMAP-Rule:MF_01227}.
ACT_SITE 516 516 {ECO:0000255|HAMAP-Rule:MF_01227}.
ACT_SITE 518 518 {ECO:0000255|HAMAP-Rule:MF_01227}.
METAL 71 71 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01227}.
METAL 140 140 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01227}.
BINDING 13 13 Allosteric inhibitor CTP; alternate.
{ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 13 13 UTP; alternate. {ECO:0000255|HAMAP-
Rule:MF_01227}.
BINDING 71 71 ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 223 223 Allosteric inhibitor CTP; alternate.
{ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 223 223 UTP; alternate. {ECO:0000255|HAMAP-
Rule:MF_01227}.
BINDING 355 355 L-glutamine; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 406 406 L-glutamine. {ECO:0000255|HAMAP-
Rule:MF_01227}.
BINDING 471 471 L-glutamine; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01227}.
SEQUENCE 544 AA; 59756 MW; A97FDF596EA842B5 CRC64;
MIRYIFITGG VVSSLGKGIA SASLGALLQS RGYRVRLRKL DPYLNVDPGT MSPRQHGEVY
VTDDGAETDL DLGHYERFTG VSARQSDNIT TGRIYQRIIE KERRGDYLGA TIQVIPHVTN
DIKEFVLSDP GEGVDFVLCE IGGTVGDIEG LPFFEAIRQL GQELGPQRAC FIHLTLLPYI
PAAGEMKTKP TQHSVKELRS IGIQPQILLC RCDRPIPVNE KGKIASFCNV RLASVIEARD
VGHIYDVPMA YHAEGLDSEV LSHFGITDAP PPDLSSWQRI AQTIKNPDGQ VTIGLVGKYT
DVPDAYKSVS EALGHGGLAN KVKVDIRFVD SEKFDDPDAA LEDLDGVHGI LLPGGFGERG
AHGKMRVARY ARERNMPCFG ICYGMQLSVV EAARNLAGIK NASTSEFGPT KEPVVGLMEE
WTKGNEKVTR DASTDLGGTM RLGAYPARLK EGSMVAQVYG SLEISERHRH RYEVNASYIE
RLEKAGMIFS GMSPDGRLPE IVELEGHPWF IGVQFHPELK SRPFEPHPLF ASFIAAAVKQ
SRLV


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