(data stored in ACNUC7421 zone)

SWISSPROT: PDXT_BACSU

ID   PDXT_BACSU              Reviewed;         196 AA.
AC   P37528;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 132.
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, ECO:0000269|PubMed:16030023};
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, ECO:0000269|PubMed:16030023};
GN   Name=pdxT {ECO:0000255|HAMAP-Rule:MF_01615}; Synonyms=yaaE;
GN   OrderedLocusNames=BSU00120;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 74-87, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, IDENTIFICATION OF REACTION PRODUCT, AND IDENTIFICATION OF
RP   ACTIVE SITE CYS.
RC   STRAIN=168;
RX   PubMed=16030023; DOI=10.1074/jbc.m501356200;
RA   Raschle T., Amrhein N., Fitzpatrick T.B.;
RT   "On the two components of pyridoxal 5'-phosphate synthase from Bacillus
RT   subtilis.";
RL   J. Biol. Chem. 280:32291-32300(2005).
RN   [4]
RP   CHARACTERIZATION.
RC   STRAIN=168 / SMY;
RX   PubMed=14762015; DOI=10.1128/jb.186.4.1191-1196.2004;
RA   Belitsky B.R.;
RT   "Physical and enzymological interaction of Bacillus subtilis proteins
RT   required for de novo pyridoxal 5'-phosphate biosynthesis.";
RL   J. Bacteriol. 186:1191-1196(2004).
RN   [5]
RP   COMPLEX FORMATION OF PDXS AND PDXT.
RX   PubMed=17408246; DOI=10.1021/bi602602x;
RA   Neuwirth M., Flicker K., Strohmeier M., Tews I., Macheroux P.;
RT   "Thermodynamic characterization of the protein-protein interaction in the
RT   heteromeric Bacillus subtilis pyridoxalphosphate synthase.";
RL   Biochemistry 46:5131-5139(2007).
RN   [6]
RP   MUTAGENESIS OF GLN-10; GLU-15; GLU-48; ARG-106 AND ARG-135.
RX   PubMed=19152323; DOI=10.1021/bi801887r;
RA   Wallner S., Neuwirth M., Flicker K., Tews I., Macheroux P.;
RT   "Dissection of contributions from invariant amino acids to complex
RT   formation and catalysis in the heteromeric pyridoxal 5-phosphate synthase
RT   complex from Bacillus subtilis.";
RL   Biochemistry 48:1928-1935(2009).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=14585832; DOI=10.1074/jbc.m310311200;
RA   Bauer J.A., Bennett E.M., Begley T.P., Ealick S.E.;
RT   "Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase
RT   implicated in pyridoxal-5'-phosphate biosynthesis.";
RL   J. Biol. Chem. 279:2704-2711(2004).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF APOENZYME AND MUTANT ASN-170 IN
RP   COMPLEX WITH SUBUNIT PDXS AND GLUTAMINE, SUBUNIT, AND MUTAGENESIS OF
RP   HIS-170.
RC   STRAIN=168 / CU1065;
RX   PubMed=17159152; DOI=10.1073/pnas.0604950103;
RA   Strohmeier M., Raschle T., Mazurkiewicz J., Rippe K., Sinning I.,
RA   Fitzpatrick T.B., Tews I.;
RT   "Structure of a bacterial pyridoxal 5'-phosphate synthase complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:19284-19289(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, ECO:0000269|PubMed:16030023}.
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, ECO:0000269|PubMed:16030023};
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         ECO:0000269|PubMed:16030023};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.99 mM for L-glutamine {ECO:0000269|PubMed:16030023};
CC         Note=kcat is 7.60 min(-1) for glutaminase activity.
CC         {ECO:0000269|PubMed:16030023};
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:17159152}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-7051766, EBI-7051766;
CC       P37527:pdxS; NbExp=5; IntAct=EBI-7051766, EBI-7828661;
CC   -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC       {ECO:0000255|HAMAP-Rule:MF_01615}.
DR   EMBL; D26185; BAA05248.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11788.1; -; Genomic_DNA.
DR   PIR; S66042; S66042.
DR   RefSeq; NP_387893.1; NC_000964.3.
DR   RefSeq; WP_003226797.1; NZ_JNCM01000024.1.
DR   PDB; 1R9G; X-ray; 2.50 A; A/B=1-196.
DR   PDB; 2NV0; X-ray; 1.73 A; A/B=1-196.
DR   PDB; 2NV2; X-ray; 2.12 A; B/D/F/H/J/L/N/P/R/T/V/X=1-196.
DR   PDBsum; 1R9G; -.
DR   PDBsum; 2NV0; -.
DR   PDBsum; 2NV2; -.
DR   SMR; P37528; -.
DR   DIP; DIP-57719N; -.
DR   IntAct; P37528; 2.
DR   MINT; P37528; -.
DR   STRING; 224308.BSU00120; -.
DR   PaxDb; P37528; -.
DR   PRIDE; P37528; -.
DR   EnsemblBacteria; CAB11788; CAB11788; BSU00120.
DR   GeneID; 939971; -.
DR   KEGG; bsu:BSU00120; -.
DR   PATRIC; fig|224308.179.peg.12; -.
DR   eggNOG; ENOG4108UHX; Bacteria.
DR   eggNOG; COG0311; LUCA.
DR   HOGENOM; HOG000039949; -.
DR   InParanoid; P37528; -.
DR   KO; K08681; -.
DR   OMA; PVYGTCA; -.
DR   PhylomeDB; P37528; -.
DR   BioCyc; BSUB:BSU00120-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-15503; -.
DR   BRENDA; 4.3.3.6; 658.
DR   UniPathway; UPA00245; -.
DR   EvolutionaryTrace; P37528; -.
DR   Proteomes; UP000001570; 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:0042802; F:identical protein binding; IPI:IntAct.
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   GO; GO:0042819; P:vitamin B6 biosynthetic 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;
DR   PRODOM; P37528.
DR   SWISS-2DPAGE; P37528.
KW   3D-structure; Direct protein sequencing; Glutamine amidotransferase;
KW   Hydrolase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..196
FT                   /note="Pyridoxal 5'-phosphate synthase subunit PdxT"
FT                   /id="PRO_0000135632"
FT   REGION          47..49
FT                   /note="L-glutamine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615,
FT                   ECO:0000269|PubMed:17159152"
FT   REGION          134..135
FT                   /note="L-glutamine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615,
FT                   ECO:0000269|PubMed:17159152"
FT   ACT_SITE        79
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615, ECO:0000305"
FT   ACT_SITE        170
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615, ECO:0000305"
FT   ACT_SITE        172
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615, ECO:0000305"
FT   BINDING         106
FT                   /note="L-glutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01615,
FT                   ECO:0000269|PubMed:17159152"
FT   MUTAGEN         10
FT                   /note="Q->A: 3-fold reduction in glutaminase activity."
FT                   /evidence="ECO:0000269|PubMed:19152323"
FT   MUTAGEN         10
FT                   /note="Q->E: Almost no activity."
FT                   /evidence="ECO:0000269|PubMed:19152323"
FT   MUTAGEN         10
FT                   /note="Q->N: 10-fold reduction in glutaminase activity."
FT                   /evidence="ECO:0000269|PubMed:19152323"
FT   MUTAGEN         15
FT                   /note="E->A: Almost no effect on glutaminase activity."
FT                   /evidence="ECO:0000269|PubMed:19152323"
FT   MUTAGEN         48
FT                   /note="E->A: No activity, disturbing interaction with
FT                   PdxS."
FT                   /evidence="ECO:0000269|PubMed:19152323"
FT   MUTAGEN         106
FT                   /note="R->A: No activity, disturbing interaction with
FT                   PdxS."
FT                   /evidence="ECO:0000269|PubMed:19152323"
FT   MUTAGEN         135
FT                   /note="R->A: No activity, disturbing interaction with
FT                   PdxS."
FT                   /evidence="ECO:0000269|PubMed:19152323"
FT   MUTAGEN         170
FT                   /note="H->N: No activity."
FT                   /evidence="ECO:0000269|PubMed:17159152"
FT   STRAND          3..7
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          9..11
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   HELIX           14..22
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          26..30
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   HELIX           33..38
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          40..44
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   HELIX           49..58
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   HELIX           62..70
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          75..78
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   HELIX           80..85
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          86..89
FT                   /evidence="ECO:0000244|PDB:2NV2"
FT   STRAND          102..105
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   TURN            106..109
FT                   /evidence="ECO:0000244|PDB:2NV2"
FT   TURN            111..113
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          114..120
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          129..135
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          138..142
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          147..152
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          155..161
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          164..169
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   STRAND          173..175
FT                   /evidence="ECO:0000244|PDB:2NV0"
FT   HELIX           178..193
FT                   /evidence="ECO:0000244|PDB:2NV0"
SQ   SEQUENCE   196 AA;  21447 MW;  91111DEF75257882 CRC64;
     MLTIGVLGLQ GAVREHIHAI EACGAAGLVV KRPEQLNEVD GLILPGGEST TMRRLIDTYQ
     FMEPLREFAA QGKPMFGTCA GLIILAKEIA GSDNPHLGLL NVVVERNSFG RQVDSFEADL
     TIKGLDEPFT GVFIRAPHIL EAGENVEVLS EHNGRIVAAK QGQFLGCSFH PELTEDHRVT
     QLFVEMVEEY KQKALV
//

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