位置:首页 > 蛋白库 > PDXT_STRGG
PDXT_STRGG
ID   PDXT_STRGG              Reviewed;         197 AA.
AC   B1W3G0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000255|HAMAP-Rule:MF_01615};
DE            EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01615};
DE   AltName: Full=Pdx2 {ECO:0000255|HAMAP-Rule:MF_01615};
DE   AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_01615};
DE            EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01615};
GN   Name=pdxT {ECO:0000255|HAMAP-Rule:MF_01615}; OrderedLocusNames=SGR_6013;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- FUNCTION: Catalyzes the hydrolysis of glutamine to glutamate and
CC       ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The
CC       resulting ammonia molecule is channeled to the active site of PdxS.
CC       {ECO:0000255|HAMAP-Rule:MF_01615}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate +
CC         L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-
CC         phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:59776,
CC         ChEBI:CHEBI:597326; EC=4.3.3.6; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01615};
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; EC=3.5.1.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01615};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01615}.
CC   -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of heterodimers.
CC       Only shows activity in the heterodimer. {ECO:0000255|HAMAP-
CC       Rule:MF_01615}.
CC   -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC       {ECO:0000255|HAMAP-Rule:MF_01615}.
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; AP009493; BAG22842.1; -; Genomic_DNA.
DR   RefSeq; WP_012381670.1; NC_010572.1.
DR   AlphaFoldDB; B1W3G0; -.
DR   SMR; B1W3G0; -.
DR   STRING; 455632.SGR_6013; -.
DR   MEROPS; C26.A32; -.
DR   EnsemblBacteria; BAG22842; BAG22842; SGR_6013.
DR   GeneID; 6209910; -.
DR   KEGG; sgr:SGR_6013; -.
DR   PATRIC; fig|455632.4.peg.6164; -.
DR   eggNOG; COG0311; Bacteria.
DR   HOGENOM; CLU_069674_2_0_11; -.
DR   OMA; VFIRAPI; -.
DR   OrthoDB; 1628378at2; -.
DR   UniPathway; UPA00245; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006543; P:glutamine catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01749; GATase1_PB; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_01615; PdxT; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002161; PdxT/SNO.
DR   InterPro; IPR021196; PdxT/SNO_CS.
DR   PANTHER; PTHR31559; PTHR31559; 1.
DR   Pfam; PF01174; SNO; 1.
DR   PIRSF; PIRSF005639; Glut_amidoT_SNO; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR03800; PLP_synth_Pdx2; 1.
DR   PROSITE; PS01236; PDXT_SNO_1; 1.
DR   PROSITE; PS51130; PDXT_SNO_2; 1.
PE   3: Inferred from homology;
KW   Glutamine amidotransferase; Hydrolase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..197
FT                   /note="Pyridoxal 5'-phosphate synthase subunit PdxT"
FT                   /id="PRO_1000185900"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT   ACT_SITE        176
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT   ACT_SITE        178
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT   BINDING         50..52
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT   BINDING         111
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT   BINDING         140..141
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
SQ   SEQUENCE   197 AA;  21026 MW;  F53FBD9E1B1B35D6 CRC64;
     MSDTPVIGVL ALQGDVREHL IALASADALA RPVRRPEELA EVDGLVIPGG ESTTMSKLAV
     LFGMMEPLRE RVRAGMPVYG TCAGMILLAE KILDPRSGQE TVGGIDMIVR RNAFGRQNES
     FEAAVEVGGV EGGPVDGVFI RAPWVESVGA RTEVIAEHGG HIVAVRQENA LATSFHPELT
     GDHRVHALFV DMVRAVN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024