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BACSU:PDXT

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Species (Taxon ID) Bacillus subtilis (strain 168). (224308)
Gene Name(s) pdxT (ECO:0000255 with HAMAP-Rule:MF_01615) (synonyms: yaaE)
Protein Name(s) Pyridoxal 5'-phosphate synthase subunit PdxT (ECO:0000255 with HAMAP-Rule:MF_01615)

Pdx2 (ECO:0000255 with HAMAP-Rule:MF_01615) Pyridoxal 5'-phosphate synthase glutaminase subunit (ECO:0000255 with HAMAP-Rule:MF_01615)

External Links
UniProt P37528
EMBL D26185
AL009126
PIR S66042
RefSeq NP_387893.1
WP_003226797.1
PDB 1R9G
2NV0
2NV2
PDBsum 1R9G
2NV0
2NV2
ProteinModelPortal P37528
SMR P37528
DIP DIP-57719N
IntAct P37528
MINT P37528
STRING 224308.Bsubs1_010100000060
PaxDb P37528
PRIDE P37528
EnsemblBacteria CAB11788
GeneID 939971
KEGG bsu:BSU00120
PATRIC fig|224308.179.peg.12
eggNOG ENOG4108UHX
COG0311
HOGENOM HOG000039949
InParanoid P37528
KO K08681
OMA VFIRAPI
PhylomeDB P37528
BioCyc BSUB:BSU00120-MONOMER
MetaCyc:MONOMER-15503
BRENDA 4.3.3.6
UniPathway UPA00245
EvolutionaryTrace P37528
Proteomes UP000001570
GO GO:0005829
GO:1903600
GO:0004359
GO:0042802
GO:0036381
GO:0006541
GO:0042823
GO:0008614
CDD cd01749
Gene3D 3.40.50.880
HAMAP MF_01615
InterPro IPR029062
IPR002161
IPR021196
PANTHER PTHR31559
Pfam PF01174
PIRSF PIRSF005639
SUPFAM SSF52317
TIGRFAMs TIGR03800
PROSITE PS01236
PS51130

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:1903600

glutaminase complex

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000774355
SGD:S000004701

C

Seeded From UniProt

complete

involved_in

GO:0042823

pyridoxal phosphate biosynthetic process

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000774355
UniProtKB:P9WII7

P

Seeded From UniProt

complete

involved_in

GO:0042819

vitamin B6 biosynthetic process

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000774355
TAIR:locus:2175083
UniProtKB:Q8IIK4

P

Seeded From UniProt

complete

involved_in

GO:0008614

pyridoxine metabolic process

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000774355
SGD:S000001834

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000774355
TAIR:locus:2175083

C

Seeded From UniProt

complete

contributes_to

GO:0004359

glutaminase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000774355
SGD:S000004701
TAIR:locus:2175083
UniProtKB:Q8IIK4

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19523954[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P37528

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:17159152[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P37528

F

Seeded From UniProt

complete

enables

GO:0004359

glutaminase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002161

F

Seeded From UniProt

complete

involved_in

GO:0042819

vitamin B6 biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002161

P

Seeded From UniProt

complete

involved_in

GO:0042823

pyridoxal phosphate biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002161

P

Seeded From UniProt

complete

enables

GO:0004359

glutaminase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.5.1.2

F

Seeded From UniProt

complete

enables

GO:0036381

pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.3.3.6

F

Seeded From UniProt

complete

enables

GO:0036381

pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079265

F

Seeded From UniProt

complete

enables

GO:0004359

glutaminase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079265

F

Seeded From UniProt

complete

involved_in

GO:0006543

glutamine catabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079265

P

Seeded From UniProt

complete

involved_in

GO:0042823

pyridoxal phosphate biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079265

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0006541

glutamine metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0315

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

involved_in

GO:0042823

pyridoxal phosphate biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00245

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. Neuwirth, M et al. (2009) X-ray crystal structure of Saccharomyces cerevisiae Pdx1 provides insights into the oligomeric nature of PLP synthases. FEBS Lett. 583 2179-86 PubMed GONUTS page
  3. Strohmeier, M et al. (2006) Structure of a bacterial pyridoxal 5'-phosphate synthase complex. Proc. Natl. Acad. Sci. U.S.A. 103 19284-9 PubMed GONUTS page