(data stored in SCRATCH zone)

SWISSPROT: D1CDF2_THET1

ID   D1CDF2_THET1            Unreviewed;       196 AA.
AC   D1CDF2;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000256|HAMAP-Rule:MF_01615};
DE            EC=4.3.3.6 {ECO:0000256|HAMAP-Rule:MF_01615};
DE   AltName: Full=Pdx2 {ECO:0000256|HAMAP-Rule:MF_01615};
DE   AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000256|HAMAP-Rule:MF_01615};
DE            EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01615};
GN   Name=pdxT {ECO:0000256|HAMAP-Rule:MF_01615};
GN   OrderedLocusNames=Tter_0035 {ECO:0000313|EMBL:ACZ40958.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40958.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40958.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01615};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-
CC         phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate
CC         + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:31507,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58273, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:597326; EC=4.3.3.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01615};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01615}.
CC   -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of
CC       heterodimers. Only shows activity in the heterodimer.
CC       {ECO:0000256|HAMAP-Rule:MF_01615}.
CC   -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC       {ECO:0000256|HAMAP-Rule:MF_01615}.
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DR   EMBL; CP001825; ACZ40958.1; -; Genomic_DNA.
DR   RefSeq; WP_012873993.1; NC_013525.1.
DR   STRING; 525904.Tter_0035; -.
DR   MEROPS; C26.A32; -.
DR   EnsemblBacteria; ACZ40958; ACZ40958; Tter_0035.
DR   KEGG; ttr:Tter_0035; -.
DR   eggNOG; ENOG4108UHX; Bacteria.
DR   eggNOG; COG0311; LUCA.
DR   HOGENOM; HOG000039949; -.
DR   KO; K08681; -.
DR   OMA; VFIRAPI; -.
DR   OrthoDB; 1628378at2; -.
DR   BioCyc; TTER525904:G1GGS-35-MONOMER; -.
DR   UniPathway; UPA00245; -.
DR   Proteomes; UP000000323; Chromosome 1.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006543; P:glutamine catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; D1CDF2.
DR   SWISS-2DPAGE; D1CDF2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01615,
KW   ECO:0000313|EMBL:ACZ40958.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01615};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01615};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01615};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transferase {ECO:0000313|EMBL:ACZ40958.1}.
FT   REGION       46     48       L-glutamine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01615}.
FT   REGION      133    134       L-glutamine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01615}.
FT   ACT_SITE     78     78       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01615}.
FT   ACT_SITE    170    170       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_01615}.
FT   ACT_SITE    172    172       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_01615}.
FT   BINDING     104    104       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01615}.
SQ   SEQUENCE   196 AA;  21526 MW;  12E0951F89A038CB CRC64;
     MKIGVLALQG DFREHEQMLH RIGIVPVEVR KPEHLYGLDG IIIPGGESTT IGKLAVNYGL
     MEPLKDFAAQ GKPVWGTCAG MIFLSKDVGM EQPLLGLLDV KVRRNAFGRQ LDSFEADIEM
     PEVSERPVHA VFIRAPIVES VGPGVQVLGK LQDGTIVAVR QGNILATSFH PELTQDPTMH
     LYFISMAKED LVTNRS
//

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