GenomeNet

Database: UniProt
Entry: A5UD28
LinkDB: A5UD28
Original site: A5UD28 
ID   PYRG_HAEIE              Reviewed;         545 AA.
AC   A5UD28;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   06-JUL-2016, entry version 69.
DE   RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine triphosphate synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            Short=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            Short=CTPS {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=UTP--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_01227};
GN   Name=pyrG {ECO:0000255|HAMAP-Rule:MF_01227};
GN   OrderedLocusNames=CGSHiEE_06690;
OS   Haemophilus influenzae (strain PittEE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittEE;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R.,
RA   Post J.C., Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12
RT   clinical nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen. Regulates
CC       intracellular CTP levels through interactions with the four
CC       ribonucleotide triphosphates. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate +
CC       CTP + L-glutamate. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC       is the substrate; GTP has no effect on the reaction when ammonia
CC       is the substrate. The allosteric effector GTP functions by
CC       stabilizing the protein conformation that binds the tetrahedral
CC       intermediate(s) formed during glutamine hydrolysis. Inhibited by
CC       the product CTP, via allosteric rather than competitive
CC       inhibition. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_01227}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for
CC       distinguishing between UTP and CTP. The overlapping regions of the
CC       product feedback inhibitory and substrate sites recognize a common
CC       feature in both compounds, the triphosphate moiety. To
CC       differentiate isosteric substrate and product pyrimidine rings, an
CC       additional pocket far from the expected kinase/ligase catalytic
CC       site, specifically recognizes the cytosine and ribose portions of
CC       the product inhibitor. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01227}.
DR   EMBL; CP000671; ABQ98679.1; -; Genomic_DNA.
DR   RefSeq; WP_012054511.1; NC_009566.1.
DR   ProteinModelPortal; A5UD28; -.
DR   SMR; A5UD28; 1-542.
DR   MEROPS; C26.964; -.
DR   EnsemblBacteria; ABQ98679; ABQ98679; CGSHiEE_06690.
DR   KEGG; hip:CGSHiEE_06690; -.
DR   PATRIC; 20278829; VBIHaeInf81350_1349.
DR   HOGENOM; HOG000077515; -.
DR   KO; K01937; -.
DR   OMA; MRLGEYE; -.
DR   OrthoDB; EOG6RC3NR; -.
DR   BioCyc; HINF374930:GJDD-1243-MONOMER; -.
DR   UniPathway; UPA00159; UER00277.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_01227; PyrG; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11550; PTHR11550; 1.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00337; PyrG; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutamine amidotransferase; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis.
FT   CHAIN         1    545       CTP synthase.
FT                                /FTId=PRO_1000139467.
FT   DOMAIN      291    542       Glutamine amidotransferase type-1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND      15     20       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     147    149       Allosteric inhibitor CTP.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     187    192       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     187    192       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   NP_BIND     239    241       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   REGION        1    266       Amidoligase domain. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   REGION      380    383       L-glutamine binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   ACT_SITE    379    379       Nucleophile; for glutamine hydrolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    515    515       {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    517    517       {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   METAL        72     72       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   METAL       140    140       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING      14     14       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING      14     14       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING      72     72       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     223    223       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     223    223       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING     352    352       L-glutamine; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     403    403       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING     470    470       L-glutamine; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
SQ   SEQUENCE   545 AA;  60212 MW;  938EB38676B1C635 CRC64;
     MATNYIFVTG GVVSSLGKGI AAASLAAILE ARGLNVTIMK LDPYINVDPG TMSPTQHGEV
     FVTQDGAETD LDLGHYERFI RTKMTKRNNF TTGKIYSEVL RKERRGDYLG ATIQVIPHIT
     NEIKDRVIAG AQGHDVVIVE VGGTVGDIES LPFLEALRQL AVQVGREHTL FMHLTLVPYI
     PTAGEVKTKP TQHSVKELLS IGIQPDVLIC RSDRMIPPNE RAKIALFCNV AERAVISLKD
     VNSIYQIPAL LKSQGLDDFV CERFRLTCPE ADLTEWEQVL YKQANPVGEV TIGMVGKYTE
     LPDAYKSVNE ALKHAGLTNR LSVSIKYIDS QDVETKGVEV LKGVDGILVP GGFGYRGVEG
     KIRTAQYARE NKIPYLGICL GMQIALIEYA RNVAGLTKAN SSEFDKDCEQ PVVALITEWQ
     DAEGNTEVRT DESDLGGTMR LGAQQCHLVS GSRARELYGK ETIEERHRHR YEVNNTLLPQ
     IEKAGLKVTG LSADKKLVEI IEVPNHPWFV ACQFHPEFTS TPRDGHPLFA GFVKAAYENH
     KKSVK
//
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