位置:首页 > 蛋白库 > PYRG_RHILW
PYRG_RHILW
ID   PYRG_RHILW              Reviewed;         542 AA.
AC   B5ZPZ7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 91.
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}; OrderedLocusNames=Rleg2_1832;
OS   Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2304;
RX   PubMed=21304679; DOI=10.4056/sigs.44642;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA   Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT   WSM2304, an effective microsymbiont of the South American clover Trifolium
RT   polymorphum.";
RL   Stand. Genomic Sci. 2:66-76(2010).
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:
CC       Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-
CC         glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01227};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01227};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + NH4(+) + UTP = ADP + CTP + 2 H(+) + phosphate;
CC         Xref=Rhea:RHEA:16597, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01227};
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP, when glutamine is
CC       the substrate; GTP has no effect on the reaction when ammonia is the
CC       substrate. The allosteric effector GTP functions by stabilizing the
CC       protein conformation that binds the tetrahedral intermediate(s) formed
CC       during glutamine hydrolysis. Inhibited by the product CTP, via
CC       allosteric rather than competitive inhibition. {ECO:0000255|HAMAP-
CC       Rule:MF_01227}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for distinguishing
CC       between UTP and CTP. The overlapping regions of the product feedback
CC       inhibitory and substrate sites recognize a common feature in both
CC       compounds, the triphosphate moiety. To differentiate isosteric
CC       substrate and product pyrimidine rings, an additional pocket far from
CC       the expected kinase/ligase catalytic site, specifically recognizes the
CC       cytosine and ribose portions of the product inhibitor.
CC       {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01227}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001191; ACI55117.1; -; Genomic_DNA.
DR   RefSeq; WP_012557733.1; NC_011369.1.
DR   AlphaFoldDB; B5ZPZ7; -.
DR   SMR; B5ZPZ7; -.
DR   STRING; 395492.Rleg2_1832; -.
DR   EnsemblBacteria; ACI55117; ACI55117; Rleg2_1832.
DR   KEGG; rlt:Rleg2_1832; -.
DR   eggNOG; COG0504; Bacteria.
DR   HOGENOM; CLU_011675_5_0_5; -.
DR   OMA; EFNNAYR; -.
DR   OrthoDB; 783657at2; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000008330; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004359; F:glutaminase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd03113; CTPS_N; 1.
DR   CDD; cd01746; GATase1_CTP_Synthase; 1.
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; IPR033828; GATase1_CTP_Synthase.
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; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis.
FT   CHAIN           1..542
FT                   /note="CTP synthase"
FT                   /id="PRO_1000139545"
FT   DOMAIN          291..541
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   REGION          1..265
FT                   /note="Amidoligase domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   ACT_SITE        380
FT                   /note="Nucleophile; for glutamine hydrolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   ACT_SITE        514
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   ACT_SITE        516
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         13
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         13
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         14..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         146..148
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         186..191
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         186..191
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         222
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         222
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         353
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         381..384
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         404
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         469
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
SQ   SEQUENCE   542 AA;  59852 MW;  625254359A1D9F5B CRC64;
     MARYVFITGG VVSSLGKGIA AAALGALLQA RGYRVRLRKL DPYLNVDPGT MSPTQHGEVF
     VTDDGAETDL DLGHYERFTG RSATKTDNIT TGRIYKNIID KERRGDYLGA TVQVIPHVTN
     EIKDFVIEGN DDYDFVICEI GGTVGDIEAM PFMEAIRQLG NDLPRGTAVY VHLTLMPYIP
     AAGELKTKPT QHSVKELQAL GIHPDILLVR ADREIPEAER RKLSLFCNVR PSAVIQALDV
     ANIYDVPIAY HKEGLDDEVL AAFGIEPAPK PRLDPWEEVC NRIRTPEGEV TIAIVGKYTG
     LKDAYKSLIE ALHHGGIANR VKVKLEWIES EVFEKEDPAP YLEKVHGILV PGGFGERGSE
     GKIHAARFAR ERKVPYFGIC FGMQMAVIEA ARNLADVSGA SSTEFGPTKE PVVGLMTEWV
     KGNELQKRTA AGDLGGTMRL GAYKAALKKG TKISDIYGST DISERHRHRY EVNVDYKDRL
     ESCGLVFSGM SPDGVLPETI EYPDHPWFIG VQYHPELKSR PLDPHPLFAS FIEAATEQSR
     LV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024