ID E8SDZ8_STAPH Unreviewed; 537 AA.
AC E8SDZ8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 01-MAY-2013, entry version 17.
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=SPSINT_1793;
OS Staphylococcus pseudintermedius (strain HKU10-03).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=937773;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HKU10-03;
RA Tse H., Tsoi H.W., Leung S.P., Urquhart I.J., Lau S.K.P., Woo P.C.Y.,
RA Yuen K.Y.;
RT "Complete genome sequence of Staphylococcus pseudintermedius.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKU10-03;
RX PubMed=21278300; DOI=10.1128/JB.00023-11;
RA Tse H., Tsoi H.W., Leung S.P., Urquhart I.J., Lau S.K., Woo P.C.,
RA Yuen K.Y.;
RT "Complete genome sequence of the veterinary pathogen Staphylococcus
RT pseudintermedius strain HKU10-03, isolated in a case of canine
RT pyoderma.";
RL J. Bacteriol. 193:1783-1784(2011).
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; CP002439; ADV06321.1; -; Genomic_DNA.
DR RefSeq; YP_004149957.1; NC_014925.1.
DR EnsemblBacteria; ADV06321; ADV06321; SPSINT_1793.
DR GeneID; 10136600; -.
DR KEGG; ssd:SPSINT_1793; -.
DR PATRIC; 45366872; VBIStaPse177932_1792.
DR HOGENOM; HOG000077515; -.
DR KO; K01937; -.
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 DOMAIN 293 535 Glutamine amidotransferase type-1 (By
FT similarity).
FT REGION 1 254 Aminator domain (By similarity).
FT ACT_SITE 382 382 Nucleophile (By similarity).
FT ACT_SITE 508 508 By similarity.
FT ACT_SITE 510 510 By similarity.
SQ SEQUENCE 537 AA; 60245 MW; 4FFB8E80AA7590B1 CRC64;
MTKFIFVTGG VVSSLGKGIT AASLGRLLKD RGLKVTIQKF DPYLNVDPGT MSPYQHGEVF
VTDDGAETDL DLGHYERFID INLNQYSNVT AGKVYSHVLQ KERRGDYLGG TVQVIPHITN
EIKSRLLLAG ESTNADVVIT EIGGTTGDIE SLPFIEAIRQ IKSDLGRDNV MYVHCTLLPY
IKAAGEMKTK PTQHSVKELR GLGIQPDLIV VRTEYEMTQD LKDKIALFCD IDKESVIECR
DAESLYEIPL QLSHQNMDDI VIERLGLQVD RDTQLDEWNH LLRVVNNLEG KVTIGLVGKY
VSLQDAYLSV AESLKHAGYQ FMKDIEIRWI DSSEVNDDNA AEYLSDVDGI LVPGGFGFRA
SEGKISAIKY AREQQIPFFG ICLGMQLATV EYARHVVGLE GAHSAELDPN TPYPVIDLLP
EQKDIEDLGG TLRLGLYPCT IQEGTLAEKI YGKTEVEERH RHRYEFNNEY REQLEAAGMI
FSGTSPDGRL VEMVELKEHP FFIACQFHPE FLSRPNRPQP IFKSFIEAAL LQQNKTK
//
