PDXT_MYCPA
ID PDXT_MYCPA Reviewed; 173 AA.
AC Q73WF2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000250|UniProtKB:P37528};
DE EC=4.3.3.6 {ECO:0000250|UniProtKB:P37528};
DE AltName: Full=Pdx2 {ECO:0000250|UniProtKB:P37528};
DE AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000250|UniProtKB:P37528};
DE EC=3.5.1.2 {ECO:0000250|UniProtKB:P37528};
GN Name=pdxT {ECO:0000250|UniProtKB:P37528}; OrderedLocusNames=MAP_2708c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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:0000250|UniProtKB:P37528}.
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;
CC Evidence={ECO:0000250|UniProtKB:P37528};
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:0000250|UniProtKB:P37528};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC {ECO:0000250|UniProtKB:P37528}.
CC -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of heterodimers.
CC Only shows activity in the heterodimer. {ECO:0000250|UniProtKB:P37528}.
CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family. {ECO:0000305}.
CC -!- CAUTION: Glu-170 and Asp-172 are present instead of the conserved His
CC and Glu which are expected to be active site residues. {ECO:0000305}.
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DR EMBL; AE016958; AAS05025.1; -; Genomic_DNA.
DR RefSeq; WP_003875362.1; NC_002944.2.
DR AlphaFoldDB; Q73WF2; -.
DR SMR; Q73WF2; -.
DR STRING; 262316.MAP_2708c; -.
DR EnsemblBacteria; AAS05025; AAS05025; MAP_2708c.
DR KEGG; mpa:MAP_2708c; -.
DR eggNOG; COG0311; Bacteria.
DR HOGENOM; CLU_069674_2_0_11; -.
DR OMA; VFIRAPI; -.
DR UniPathway; UPA00245; -.
DR Proteomes; UP000000580; Chromosome.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01749; GATase1_PB; 1.
DR Gene3D; 3.40.50.880; -; 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;
KW Reference proteome.
FT CHAIN 1..173
FT /note="Pyridoxal 5'-phosphate synthase subunit PdxT"
FT /id="PRO_0000135648"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT BINDING 49..51
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT BINDING 113
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT BINDING 141..142
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P37528"
SQ SEQUENCE 173 AA; 18013 MW; F8E223AE281B0187 CRC64;
MSAPRIGVLA LQGDTREHLA ALREAGAESM PVRRRGELEA VDGLVIPGGE STTMSHLLKD
LDLLEPLRGL LADGLPAYGA CAGMILLASE ILDAGAGGRE ALPLRAIDMT VRRNAFGRQV
DSFEGDIAFA GLDGPVRAVF IRAPWVERAG DGVEVLARAA GHVVAVAGIE PDA
