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Database: UniProt
Entry: Q73WF2
LinkDB: Q73WF2
Original site: Q73WF2 
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   22-JUL-2015, entry version 70.
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   Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10).
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.,
RA   Banerji N., 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
CC       PdxS. {ECO:0000250|UniProtKB:P37528}.
CC   -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate + D-glyceraldehyde 3-
CC       phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3
CC       H(2)O + phosphate. {ECO:0000250|UniProtKB:P37528}.
CC   -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3).
CC       {ECO:0000250|UniProtKB:P37528}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
CC       biosynthesis. {ECO:0000250|UniProtKB:P37528}.
CC   -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of
CC       heterodimers. Only shows activity in the heterodimer.
CC       {ECO:0000250|UniProtKB:P37528}.
CC   -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Glu-170 and Asp-172 are present instead of the conserved
CC       His and Glu which are expected to be active site residues.
CC       {ECO:0000305}.
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DR   EMBL; AE016958; AAS05025.1; -; Genomic_DNA.
DR   RefSeq; WP_003875362.1; NC_002944.2.
DR   ProteinModelPortal; Q73WF2; -.
DR   STRING; 262316.MAP2708c; -.
DR   EnsemblBacteria; AAS05025; AAS05025; MAP_2708c.
DR   GeneID; 2720021; -.
DR   KEGG; mpa:MAP2708c; -.
DR   PATRIC; 17998124; VBIMycAvi108102_2876.
DR   eggNOG; COG0311; -.
DR   KO; K08681; -.
DR   OMA; STTIARH; -.
DR   OrthoDB; EOG66F0BW; -.
DR   BioCyc; MAVI262316:GCQR-2744-MONOMER; -.
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   GO; GO:0042819; P:vitamin B6 biosynthetic process; IEA:InterPro.
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   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   Complete proteome; Glutamine amidotransferase; Hydrolase; Lyase;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    173       Pyridoxal 5'-phosphate synthase subunit
FT                                PdxT.
FT                                /FTId=PRO_0000135648.
FT   REGION       49     51       L-glutamine binding.
FT                                {ECO:0000250|UniProtKB:P37528}.
FT   REGION      141    142       L-glutamine binding.
FT                                {ECO:0000250|UniProtKB:P37528}.
FT   ACT_SITE     81     81       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P37528}.
FT   BINDING     113    113       L-glutamine.
FT                                {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
//
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