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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_THET8              Reviewed;         550 AA.
Q5SIA8;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
07-JUN-2017, entry version 92.
RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227};
EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227, ECO:0000269|PubMed:15296735};
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, ECO:0000303|PubMed:15296735};
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=TTHA1466;
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579).
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
Thermus.
NCBI_TaxID=300852;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HB8 / ATCC 27634 / DSM 579;
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y.,
Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
"Complete genome sequence of Thermus thermophilus HB8.";
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[2]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF APOENZYME AND IN COMPLEX
WITH L-GLUTAMINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND SUBUNIT.
STRAIN=HB8 / ATCC 27634 / DSM 579;
PubMed=15296735; DOI=10.1016/j.str.2004.05.013;
Goto M., Omi R., Nakagawa N., Miyahara I., Hirotsu K.;
"Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine
binding sites.";
Structure 12:1413-1423(2004).
-!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
either L-glutamine or ammonia as the source of nitrogen
(PubMed:15296735). Regulates intracellular CTP levels through
interactions with the four ribonucleotide triphosphates (By
similarity). {ECO:0000255|HAMAP-Rule:MF_01227,
ECO:0000269|PubMed:15296735}.
-!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate +
CTP + L-glutamate. {ECO:0000255|HAMAP-Rule:MF_01227,
ECO:0000269|PubMed:15296735}.
-!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
is the substrate (PubMed:15296735). 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 (By similarity). {ECO:0000255|HAMAP-
Rule:MF_01227, ECO:0000269|PubMed:15296735}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.24 mM for L-glutamine (at unsaturating levels of ATP and
UTP (0.5 mM)) {ECO:0000269|PubMed:15296735};
KM=0.22 mM for L-glutamine (in the presence of GTP)
{ECO:0000269|PubMed:15296735};
KM=0.37 mM for UTP {ECO:0000269|PubMed:15296735};
Note=kcat is 7.4 sec(-1) toward L-glutamine at unsaturating
levels of ATP and UTP (0.5 mM) and 40 sec(-1) in the presence of
GTP. kcat is 260 sec(-1) toward UTP.
{ECO:0000269|PubMed:15296735};
-!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP-
Rule:MF_01227}.
-!- SUBUNIT: Homotetramer in the presence of UTP and ATP. Is in a
protein concentration-dependent equilibrium between monomer,
dimer, and tetramer in the absence of UTP and ATP.
{ECO:0000269|PubMed:15296735}.
-!- 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; AP008226; BAD71289.1; -; Genomic_DNA.
RefSeq; WP_011228700.1; NC_006461.1.
RefSeq; YP_144732.1; NC_006461.1.
PDB; 1VCM; X-ray; 2.35 A; A=1-550.
PDB; 1VCN; X-ray; 2.25 A; A=1-550.
PDB; 1VCO; X-ray; 2.15 A; A=1-550.
PDBsum; 1VCM; -.
PDBsum; 1VCN; -.
PDBsum; 1VCO; -.
ProteinModelPortal; Q5SIA8; -.
SMR; Q5SIA8; -.
STRING; 300852.TTHA1466; -.
MEROPS; C26.964; -.
EnsemblBacteria; BAD71289; BAD71289; BAD71289.
GeneID; 3169502; -.
KEGG; ttj:TTHA1466; -.
PATRIC; fig|300852.9.peg.1440; -.
eggNOG; ENOG4105C8D; Bacteria.
eggNOG; COG0504; LUCA.
HOGENOM; HOG000077515; -.
KO; K01937; -.
OMA; EFNNAYR; -.
PhylomeDB; Q5SIA8; -.
BRENDA; 6.3.4.2; 7852.
UniPathway; UPA00159; UER00277.
EvolutionaryTrace; Q5SIA8; -.
Proteomes; UP000000532; 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.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome;
Glutamine amidotransferase; Ligase; Magnesium; Metal-binding;
Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome.
CHAIN 1 550 CTP synthase.
/FTId=PRO_0000266251.
DOMAIN 302 549 Glutamine amidotransferase type-1.
{ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 24 29 ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 158 160 Allosteric inhibitor CTP.
{ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 198 203 Allosteric inhibitor CTP; alternate.
{ECO:0000255|HAMAP-Rule:MF_01227}.
NP_BIND 198 203 UTP; alternate. {ECO:0000255|HAMAP-
Rule:MF_01227}.
REGION 1 277 Amidoligase domain. {ECO:0000255|HAMAP-
Rule:MF_01227}.
REGION 392 395 L-glutamine binding.
{ECO:0000244|PDB:1VCO,
ECO:0000269|PubMed:15296735}.
ACT_SITE 391 391 Nucleophile; for glutamine hydrolysis.
{ECO:0000255|HAMAP-Rule:MF_01227,
ECO:0000305|PubMed:15296735}.
ACT_SITE 522 522 {ECO:0000255|HAMAP-Rule:MF_01227,
ECO:0000305|PubMed:15296735}.
ACT_SITE 524 524 {ECO:0000255|HAMAP-Rule:MF_01227,
ECO:0000305|PubMed:15296735}.
METAL 81 81 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01227}.
METAL 151 151 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01227}.
BINDING 23 23 Allosteric inhibitor CTP; alternate.
{ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 23 23 UTP; alternate. {ECO:0000255|HAMAP-
Rule:MF_01227}.
BINDING 64 64 L-glutamine. {ECO:0000244|PDB:1VCO,
ECO:0000269|PubMed:15296735}.
BINDING 81 81 ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 234 234 Allosteric inhibitor CTP; alternate.
{ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 234 234 UTP; alternate. {ECO:0000255|HAMAP-
Rule:MF_01227}.
BINDING 252 252 ATP; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01227}.
BINDING 364 364 L-glutamine; via carbonyl oxygen.
{ECO:0000244|PDB:1VCO,
ECO:0000269|PubMed:15296735}.
BINDING 415 415 L-glutamine. {ECO:0000244|PDB:1VCO,
ECO:0000269|PubMed:15296735}.
BINDING 472 472 L-glutamine; via amide nitrogen.
{ECO:0000244|PDB:1VCO,
ECO:0000269|PubMed:15296735}.
STRAND 13 19 {ECO:0000244|PDB:1VCO}.
STRAND 21 23 {ECO:0000244|PDB:1VCO}.
HELIX 27 39 {ECO:0000244|PDB:1VCO}.
TURN 40 42 {ECO:0000244|PDB:1VCO}.
STRAND 45 51 {ECO:0000244|PDB:1VCO}.
HELIX 58 60 {ECO:0000244|PDB:1VCO}.
HELIX 81 89 {ECO:0000244|PDB:1VCO}.
HELIX 95 97 {ECO:0000244|PDB:1VCO}.
STRAND 98 100 {ECO:0000244|PDB:1VCO}.
HELIX 101 113 {ECO:0000244|PDB:1VCO}.
TURN 114 119 {ECO:0000244|PDB:1VCO}.
TURN 124 126 {ECO:0000244|PDB:1VCO}.
HELIX 127 142 {ECO:0000244|PDB:1VCO}.
STRAND 146 152 {ECO:0000244|PDB:1VCO}.
HELIX 159 161 {ECO:0000244|PDB:1VCN}.
HELIX 162 169 {ECO:0000244|PDB:1VCO}.
HELIX 171 175 {ECO:0000244|PDB:1VCO}.
STRAND 179 187 {ECO:0000244|PDB:1VCO}.
TURN 192 195 {ECO:0000244|PDB:1VCO}.
HELIX 200 211 {ECO:0000244|PDB:1VCO}.
STRAND 217 225 {ECO:0000244|PDB:1VCO}.
HELIX 229 239 {ECO:0000244|PDB:1VCO}.
HELIX 243 245 {ECO:0000244|PDB:1VCO}.
STRAND 246 250 {ECO:0000244|PDB:1VCO}.
HELIX 257 265 {ECO:0000244|PDB:1VCO}.
HELIX 267 274 {ECO:0000244|PDB:1VCO}.
HELIX 285 295 {ECO:0000244|PDB:1VCO}.
STRAND 298 308 {ECO:0000244|PDB:1VCO}.
HELIX 314 316 {ECO:0000244|PDB:1VCN}.
HELIX 317 329 {ECO:0000244|PDB:1VCO}.
STRAND 332 340 {ECO:0000244|PDB:1VCO}.
HELIX 341 343 {ECO:0000244|PDB:1VCO}.
HELIX 349 352 {ECO:0000244|PDB:1VCO}.
TURN 353 355 {ECO:0000244|PDB:1VCO}.
STRAND 359 361 {ECO:0000244|PDB:1VCO}.
HELIX 370 382 {ECO:0000244|PDB:1VCO}.
STRAND 387 390 {ECO:0000244|PDB:1VCO}.
HELIX 392 404 {ECO:0000244|PDB:1VCO}.
TURN 414 416 {ECO:0000244|PDB:1VCO}.
STRAND 423 428 {ECO:0000244|PDB:1VCO}.
HELIX 430 432 {ECO:0000244|PDB:1VCO}.
STRAND 442 450 {ECO:0000244|PDB:1VCO}.
HELIX 455 460 {ECO:0000244|PDB:1VCO}.
STRAND 463 475 {ECO:0000244|PDB:1VCO}.
HELIX 477 486 {ECO:0000244|PDB:1VCO}.
STRAND 488 493 {ECO:0000244|PDB:1VCO}.
STRAND 497 501 {ECO:0000244|PDB:1VCM}.
STRAND 505 510 {ECO:0000244|PDB:1VCO}.
STRAND 513 521 {ECO:0000244|PDB:1VCO}.
HELIX 523 526 {ECO:0000244|PDB:1VCO}.
STRAND 529 531 {ECO:0000244|PDB:1VCM}.
HELIX 534 546 {ECO:0000244|PDB:1VCO}.
SEQUENCE 550 AA; 61003 MW; F3D20D9FC50DFDF8 CRC64;
MNGSADAGPR PRKYVFITGG VVSSLGKGIL TSSLGALLRA RGYRVTAIKI DPYVNVDAGT
MRPYEHGEVF VTADGAETDL DIGHYERFLD MDLSRGNNLT TGQVYLSVIQ KERRGEYLSQ
TVQVIPHITD EIKERIRKVA EEQKAEIVVV EVGGTVGDIE SLPFLEAIRQ FRFDEGEGNT
LYLHLTLVPY LETSEEFKTK PTQHSVATLR GVGIQPDILV LRSARPVPEE VRRKVALFTN
VRPGHVFSSP TVEHLYEVPL LLEEQGLGRA VERALGLEAV IPNLSFWQEA VRVLKHPERT
VKIAIAGKYV KMPDAYLSLL EALRHAGIKN RARVEVKWVD AESLEAADLD EAFRDVSGIL
VPGGFGVRGI EGKVRAAQYA RERKIPYLGI CLGLQIAVIE FARNVAGLKG ANSTEFDPHT
PHPVIDLMPE QLEVEGLGGT MRLGDWPMRI KPGTLLHRLY GKEEVLERHR HRYEVNPLYV
DGLERAGLVV SATTPGMRGR GAGLVEAIEL KDHPFFLGLQ SHPEFKSRPM RPSPPFVGFV
EAALAYQERA


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