(data stored in ACNUC7421 zone)

SWISSPROT: D6XV07_BACIE

ID   D6XV07_BACIE            Unreviewed;       197 AA.
AC   D6XV07;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
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=Bsel_0014 {ECO:0000313|EMBL:ADH97565.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97565.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97565.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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; CP001791; ADH97565.1; -; Genomic_DNA.
DR   RefSeq; WP_013170995.1; NC_014219.1.
DR   STRING; 439292.Bsel_0014; -.
DR   MEROPS; C26.A32; -.
DR   EnsemblBacteria; ADH97565; ADH97565; Bsel_0014.
DR   KEGG; bse:Bsel_0014; -.
DR   eggNOG; ENOG4108UHX; Bacteria.
DR   eggNOG; COG0311; LUCA.
DR   HOGENOM; HOG000039949; -.
DR   KO; K08681; -.
DR   OMA; VFIRAPI; -.
DR   OrthoDB; 1628378at2; -.
DR   BioCyc; BSEL439292:G1GLR-17-MONOMER; -.
DR   UniPathway; UPA00245; -.
DR   Proteomes; UP000000271; 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; D6XV07.
DR   SWISS-2DPAGE; D6XV07.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01615,
KW   ECO:0000313|EMBL:ADH97565.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transferase {ECO:0000313|EMBL:ADH97565.1}.
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   197 AA;  21632 MW;  5657C2F0CD9030EA CRC64;
     MIKIGVLALQ GAVREHVKAL QAPDVDVITI KRKEQLAGID GLVFPGGEST TMRRLINQYG
     FYEPLKAFAA KGKPIFGTCA GAILMASEIA NQDDPHLAVM DMTVERNAFG RQKESFEVML
     NMKDVAPDIE AVFIRAPIIQ SVGPDVDVLA EYDGQIVAAR QGPFLACSFH PELTDDDRMH
     QYFVTLVRDA VQTVNNV
//

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