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

 A0A0A3JB97_9BACI        Unreviewed;       533 AA.
A0A0A3JB97;
04-FEB-2015, integrated into UniProtKB/TrEMBL.
04-FEB-2015, sequence version 1.
27-SEP-2017, entry version 21.
RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227};
EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227};
AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01227};
AltName: Full=Cytidine triphosphate synthetase {ECO:0000256|HAMAP-Rule:MF_01227};
Short=CTP synthetase {ECO:0000256|HAMAP-Rule:MF_01227};
Short=CTPS {ECO:0000256|HAMAP-Rule:MF_01227};
AltName: Full=UTP--ammonia ligase {ECO:0000256|HAMAP-Rule:MF_01227};
Name=pyrG {ECO:0000256|HAMAP-Rule:MF_01227};
ORFNames=CD30_01235 {ECO:0000313|EMBL:KGR92463.1};
Lysinibacillus massiliensis 4400831 = CIP 108448 = CCUG 49529.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
Lysinibacillus.
NCBI_TaxID=1211035 {ECO:0000313|EMBL:KGR92463.1, ECO:0000313|Proteomes:UP000030595};
[1] {ECO:0000313|EMBL:KGR92463.1, ECO:0000313|Proteomes:UP000030595}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CCUG 49529 {ECO:0000313|EMBL:KGR92463.1,
ECO:0000313|Proteomes:UP000030595};
Zhang F., Wang G., Zhang L.;
"Draft genome sequence of Lysinibacillus massiliensis CCUG 49529.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
-!- 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:0000256|HAMAP-Rule:MF_01227}.
-!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate +
CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710710}.
-!- 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:0000256|HAMAP-Rule:MF_01227}.
-!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
pathway; CTP from UDP: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710815}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710816}.
-!- 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:0000256|HAMAP-Rule:MF_01227}.
-!- SIMILARITY: Belongs to the CTP synthase family.
{ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00710794}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KGR92463.1}.
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EMBL; JPVQ01000001; KGR92463.1; -; Genomic_DNA.
RefSeq; WP_036171233.1; NZ_JPVQ01000001.1.
EnsemblBacteria; KGR92463; KGR92463; CD30_01235.
UniPathway; UPA00159; UER00277.
Proteomes; UP000030595; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710699};
Complete proteome {ECO:0000313|Proteomes:UP000030595};
Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710676};
Ligase {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710762};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710689};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710675};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710699};
Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710748};
Reference proteome {ECO:0000313|Proteomes:UP000030595}.
DOMAIN 292 533 Glutamine amidotransferase type-1.
{ECO:0000259|PROSITE:PS51273}.
NP_BIND 14 19 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
NP_BIND 148 150 Allosteric inhibitor CTP.
{ECO:0000256|HAMAP-Rule:MF_01227}.
NP_BIND 188 193 Allosteric inhibitor CTP; alternate.
{ECO:0000256|HAMAP-Rule:MF_01227}.
NP_BIND 188 193 UTP; alternate. {ECO:0000256|HAMAP-
Rule:MF_01227}.
NP_BIND 240 242 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01227}.
REGION 1 267 Amidoligase domain. {ECO:0000256|HAMAP-
Rule:MF_01227}.
REGION 382 385 L-glutamine binding. {ECO:0000256|HAMAP-
Rule:MF_01227}.
ACT_SITE 381 381 Nucleophile; for glutamine hydrolysis.
{ECO:0000256|HAMAP-Rule:MF_01227}.
ACT_SITE 507 507 {ECO:0000256|HAMAP-Rule:MF_01227}.
ACT_SITE 509 509 {ECO:0000256|HAMAP-Rule:MF_01227}.
METAL 71 71 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01227}.
METAL 141 141 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01227}.
BINDING 13 13 Allosteric inhibitor CTP; alternate.
{ECO:0000256|HAMAP-Rule:MF_01227}.
BINDING 13 13 UTP; alternate. {ECO:0000256|HAMAP-
Rule:MF_01227}.
BINDING 54 54 L-glutamine. {ECO:0000256|HAMAP-
Rule:MF_01227}.
BINDING 71 71 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
BINDING 224 224 Allosteric inhibitor CTP; alternate.
{ECO:0000256|HAMAP-Rule:MF_01227}.
BINDING 224 224 UTP; alternate. {ECO:0000256|HAMAP-
Rule:MF_01227}.
BINDING 354 354 L-glutamine; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01227}.
BINDING 405 405 L-glutamine. {ECO:0000256|HAMAP-
Rule:MF_01227}.
BINDING 462 462 L-glutamine; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01227}.
SEQUENCE 533 AA; 59942 MW; 2C539622E24C4905 CRC64;
MTKYIFVTGG VVSSLGKGIV ASSLGRLLKN RGLQVTIQKF DPYLNIDPGT MSPYQHGEVF
VTDDGAEADL DLGHYERFID INLGKHSTVT SGRVYQSVLA KERRGDYNGK TVQVIPHVTN
EIKDRIQRAG RETNADIVIT EVGGTVGDIE SLPFLEAIRQ MKSDLGHNNV MYVHCTLIPY
IAAAGELKTK PTQHSVKELR SLGIQPNIIV VRTEHPVSQE MKEKLALFCD VTPRDIIESR
DANYLYEIPL NLHAQDFDDI VLEHFRIEAP EANMEEWKEL VDKVANLKHK TRIALVGKYV
ELQDAYISVV EALKHAGYVY NSDIEVDWIN AEDVTEENVH ELLNTADGIL IPGGFGDRGI
EGKISAIKYA RENDVPLLGI CLGMQLASIE FARNVLGLKG AHTTEIDKET PYPIIDFLPD
QSDDIDLGGT LRLGLYPCKL KEGSRAMEAY NDELVYERHR HRYEFNNEFR EAMEAEGLVF
SGTSPDNKLV EIIELPEKKF FVACQFHPEF VSRPQRPQPL FREFVGAAFN NKK


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