PDXT_METJA
ID PDXT_METJA Reviewed; 186 AA.
AC Q59055;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
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}; OrderedLocusNames=MJ1661;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
RA Manzoku M., Ebihara A., Yokoyama S., Kuramitsu S.;
RT "Crystal structure of uncharacterized conserved protein from
RT Methanocaldococcus jannaschii.";
RL Submitted (APR-2007) to the PDB data bank.
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}.
CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC {ECO:0000255|HAMAP-Rule:MF_01615}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L77117; AAB99679.1; -; Genomic_DNA.
DR PIR; C64507; C64507.
DR RefSeq; WP_010871185.1; NC_000909.1.
DR PDB; 2YWJ; X-ray; 1.90 A; A=1-186.
DR PDBsum; 2YWJ; -.
DR AlphaFoldDB; Q59055; -.
DR SMR; Q59055; -.
DR STRING; 243232.MJ_1661; -.
DR PRIDE; Q59055; -.
DR EnsemblBacteria; AAB99679; AAB99679; MJ_1661.
DR GeneID; 1452570; -.
DR KEGG; mja:MJ_1661; -.
DR eggNOG; arCOG00034; Archaea.
DR HOGENOM; CLU_069674_2_0_2; -.
DR InParanoid; Q59055; -.
DR OMA; VFIRAPI; -.
DR OrthoDB; 78046at2157; -.
DR PhylomeDB; Q59055; -.
DR UniPathway; UPA00245; -.
DR EvolutionaryTrace; Q59055; -.
DR Proteomes; UP000000805; 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..186
FT /note="Pyridoxal 5'-phosphate synthase subunit PdxT"
FT /id="PRO_0000135680"
FT ACT_SITE 75
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT ACT_SITE 167
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 101
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 128..129
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:2YWJ"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2YWJ"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:2YWJ"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:2YWJ"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:2YWJ"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2YWJ"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:2YWJ"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:2YWJ"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2YWJ"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:2YWJ"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:2YWJ"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:2YWJ"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2YWJ"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:2YWJ"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:2YWJ"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:2YWJ"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2YWJ"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2YWJ"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:2YWJ"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:2YWJ"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2YWJ"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:2YWJ"
SQ SEQUENCE 186 AA; 20597 MW; FB1EB98EF5E982AA CRC64;
MIIGVLAIQG DVEEHEEAIK KAGYEAKKVK RVEDLEGIDA LIIPGGESTA IGKLMKKYGL
LEKIKNSNLP ILGTCAGMVL LSKGTGINQI LLELMDITVK RNAYGRQVDS FEKEIEFKDL
GKVYGVFIRA PVVDKILSDD VEVIARDGDK IVGVKQGKYM ALSFHPELSE DGYKVYKYFV
ENCVKK
