PDXT_THEMA
ID PDXT_THEMA Reviewed; 188 AA.
AC Q9WYU3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000255|HAMAP-Rule:MF_01615};
DE EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01615};
DE AltName: Full=Pdx2 {ECO:0000255|HAMAP-Rule:MF_01615};
DE AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_01615};
DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01615};
GN Name=pdxT {ECO:0000255|HAMAP-Rule:MF_01615};
GN Synonyms=yaaE {ECO:0000303|PubMed:17144654}; OrderedLocusNames=TM_0472;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH SUBUNIT PDXS,
RP SUBUNIT, AND REACTION MECHANISM.
RX PubMed=17144654; DOI=10.1021/bi061464y;
RA Zein F., Zhang Y., Kang Y.N., Burns K., Begley T.P., Ealick S.E.;
RT "Structural insights into the mechanism of the PLP synthase holoenzyme from
RT Thermotoga maritima.";
RL Biochemistry 45:14609-14620(2006).
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:0000255|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:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01615};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01615}.
CC -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of heterodimers.
CC Only shows activity in the heterodimer. {ECO:0000255|HAMAP-
CC Rule:MF_01615, ECO:0000269|PubMed:17144654}.
CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC {ECO:0000255|HAMAP-Rule:MF_01615}.
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DR EMBL; AE000512; AAD35557.1; -; Genomic_DNA.
DR PIR; H72371; H72371.
DR RefSeq; NP_228282.1; NC_000853.1.
DR RefSeq; WP_004081494.1; NZ_CP011107.1.
DR PDB; 2ISS; X-ray; 2.90 A; D/E/F=1-188.
DR PDBsum; 2ISS; -.
DR AlphaFoldDB; Q9WYU3; -.
DR SMR; Q9WYU3; -.
DR STRING; 243274.THEMA_02330; -.
DR EnsemblBacteria; AAD35557; AAD35557; TM_0472.
DR KEGG; tma:TM0472; -.
DR eggNOG; COG0311; Bacteria.
DR InParanoid; Q9WYU3; -.
DR OMA; VFIRAPI; -.
DR OrthoDB; 1628378at2; -.
DR UniPathway; UPA00245; -.
DR EvolutionaryTrace; Q9WYU3; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1903600; C:glutaminase complex; IBA:GO_Central.
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:0006543; P:glutamine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0008614; P:pyridoxine metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Glutamine amidotransferase; Hydrolase; Lyase;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..188
FT /note="Pyridoxal 5'-phosphate synthase subunit PdxT"
FT /id="PRO_0000135669"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 46..48
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 105
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 134..135
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2ISS"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:2ISS"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2ISS"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:2ISS"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2ISS"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2ISS"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:2ISS"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2ISS"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:2ISS"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2ISS"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2ISS"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:2ISS"
SQ SEQUENCE 188 AA; 21178 MW; AAE2FA50E81F8348 CRC64;
MKIGVLGVQG DVREHVEALH KLGVETLIVK LPEQLDMVDG LILPGGESTT MIRILKEMDM
DEKLVERINN GLPVFATCAG VILLAKRIKN YSQEKLGVLD ITVERNAYGR QVESFETFVE
IPAVGKDPFR AIFIRAPRIV ETGKNVEILA TYDYDPVLVK EGNILACTFH PELTDDLRLH
RYFLEMVK
