(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHG7_GEOS0

ID   A0A0F6BHG7_GEOS0        Unreviewed;       192 AA.
AC   A0A0F6BHG7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 20.
DE   RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000256|HAMAP-Rule:MF_01615};
DE            EC=4.3.3.6 {ECO:0000256|HAMAP-Rule:MF_01615};
DE   AltName: Full=Pdx2 {ECO:0000256|HAMAP-Rule:MF_01615};
DE   AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000256|HAMAP-Rule:MF_01615};
DE            EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01615};
GN   Name=pdxT {ECO:0000256|HAMAP-Rule:MF_01615};
GN   OrderedLocusNames=GY4MC1_0012 {ECO:0000313|EMBL:ADP72868.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72868.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72868.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72868.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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
CC       PdxS. {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01615};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-
CC         phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate
CC         + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:31507,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58273, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:597326; EC=4.3.3.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01615};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01615}.
CC   -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of
CC       heterodimers. Only shows activity in the heterodimer.
CC       {ECO:0000256|HAMAP-Rule:MF_01615}.
CC   -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC       {ECO:0000256|HAMAP-Rule:MF_01615}.
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DR   EMBL; CP002293; ADP72868.1; -; Genomic_DNA.
DR   RefSeq; WP_003247363.1; NC_014650.1.
DR   EnsemblBacteria; ADP72868; ADP72868; GY4MC1_0012.
DR   GeneID; 29237372; -.
DR   KEGG; gmc:GY4MC1_0012; -.
DR   KO; K08681; -.
DR   OMA; VFIRAPI; -.
DR   OrthoDB; 1628378at2; -.
DR   BioCyc; GSP581103:G1GOQ-17-MONOMER; -.
DR   UniPathway; UPA00245; -.
DR   Proteomes; UP000002034; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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;
DR   PRODOM; A0A0F6BHG7.
DR   SWISS-2DPAGE; A0A0F6BHG7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01615,
KW   ECO:0000313|EMBL:ADP72868.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01615};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01615};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01615};
KW   Transferase {ECO:0000313|EMBL:ADP72868.1}.
FT   REGION       47     49       L-glutamine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01615}.
FT   REGION      134    135       L-glutamine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01615}.
FT   ACT_SITE     79     79       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01615}.
FT   ACT_SITE    170    170       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_01615}.
FT   ACT_SITE    172    172       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_01615}.
FT   BINDING     106    106       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01615}.
SQ   SEQUENCE   192 AA;  21129 MW;  4A0F85B44AD74E6B CRC64;
     MMKIGVLGLQ GAVQEHVRSI EACGAEAVVV KKIEQLEEID GLILPGGEST TMRRLMDKYG
     FIEPLKQFAA AGKPMFGTCA GLILLAKRIV GYDEPHLGLM DVTVERNSFG RQRESFEAEL
     SVAGVADDFT GVFIRAPHIV EVGEDVEILA KYEGRIVAAR QGQFLGCSFH PELTDDHRMT
     QYFLNMVKEA KA
//

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