ID F6ELL1_HOYSD Unreviewed; 206 AA.
AC F6ELL1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=AS9A_1812 {ECO:0000313|EMBL:AEF40261.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF40261.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF40261.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
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: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-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:0000256|HAMAP-
CC Rule:MF_01615};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01615}.
CC -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of heterodimers.
CC Only shows activity in the heterodimer. {ECO:0000256|HAMAP-
CC Rule:MF_01615}.
CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC {ECO:0000256|ARBA:ARBA00008345, ECO:0000256|HAMAP-Rule:MF_01615}.
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DR EMBL; CP002786; AEF40261.1; -; Genomic_DNA.
DR AlphaFoldDB; F6ELL1; -.
DR STRING; 443218.AS9A_1812; -.
DR MEROPS; C26.A32; -.
DR KEGG; asd:AS9A_1812; -.
DR eggNOG; COG0311; Bacteria.
DR HOGENOM; CLU_069674_2_0_11; -.
DR UniPathway; UPA00245; -.
DR Proteomes; UP000009235; 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 NCBIfam; TIGR03800; PLP_synth_Pdx2; 1.
DR PANTHER; PTHR31559; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO; 1.
DR PANTHER; PTHR31559:SF0; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED; 1.
DR Pfam; PF01174; SNO; 1.
DR PIRSF; PIRSF005639; Glut_amidoT_SNO; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS01236; PDXT_SNO_1; 1.
DR PROSITE; PS51130; PDXT_SNO_2; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01615,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
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:UP000009235};
KW Transferase {ECO:0000313|EMBL:AEF40261.1}.
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT ECO:0000256|PIRSR:PIRSR005639-1"
FT ACT_SITE 181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 181
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT ECO:0000256|PIRSR:PIRSR005639-1"
FT ACT_SITE 183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT ECO:0000256|PIRSR:PIRSR005639-1"
FT BINDING 50..52
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT ECO:0000256|PIRSR:PIRSR005639-2"
FT BINDING 111
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT ECO:0000256|PIRSR:PIRSR005639-2"
FT BINDING 140..141
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT ECO:0000256|PIRSR:PIRSR005639-2"
SQ SEQUENCE 206 AA; 22169 MW; 7A9FE7F45625FF8C CRC64;
MMSTPLIGVL ALQGDFREHI AAVEACGARA IGLRRREEID AIDGLVIPGG ESTTMSRLLT
AFELLDPLRS RLKEGLPALG SCAGMIMLAS EILDTRPDAQ HLDALDITVR RNAFGRQVDS
FEEDLHIDGI EGGPVRAVFI RAPWVERVGA SVEVLARVEA GPAQGRIVAV RENAVIATSF
HPEVTGDLRI HDLFVQTVRG STLNSG
//
