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 01-MAY-2013, entry version 48.
DE RecName: Full=CTP synthase;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase;
DE AltName: Full=UTP--ammonia ligase;
GN Name=pyrG; 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 (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + UTP + NH(3) = ADP + phosphate + CTP.
CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC is the substrate. Inhibited by CTP (By similarity).
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC pathway; CTP from UDP: step 2/2.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SIMILARITY: Belongs to the CTP synthase family.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR EMBL; CP000671; ABQ98679.1; -; Genomic_DNA.
DR RefSeq; YP_001291062.1; NC_009566.1.
DR ProteinModelPortal; A5UD28; -.
DR SMR; A5UD28; 1-542.
DR STRING; 374930.CGSHiEE_06690; -.
DR EnsemblBacteria; ABQ98679; ABQ98679; CGSHiEE_06690.
DR GeneID; 5225847; -.
DR KEGG; hip:CGSHiEE_06690; -.
DR PATRIC; 20278829; VBIHaeInf81350_1349.
DR eggNOG; COG0504; -.
DR HOGENOM; HOG000077515; -.
DR KO; K01937; -.
DR OMA; TNEIKDR; -.
DR ProtClustDB; PRK05380; -.
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:HAMAP.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:HAMAP.
DR HAMAP; MF_01227; PyrG; 1; -.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR017926; GATASE_1.
DR PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase;
KW Nucleotide-binding; Pyrimidine biosynthesis.
FT CHAIN 1 545 CTP synthase.
FT /FTId=PRO_1000139467.
FT DOMAIN 291 542 Glutamine amidotransferase type-1.
FT REGION 1 253 Aminator domain.
FT ACT_SITE 379 379 Nucleophile (By similarity).
FT ACT_SITE 515 515 By similarity.
FT ACT_SITE 517 517 By similarity.
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
//
