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BACSU:PDXT
Contents
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 |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000774355 |
C |
Seeded From UniProt |
complete | ||
involved_in |
GO:0042823 |
pyridoxal phosphate biosynthetic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000774355 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0042819 |
vitamin B6 biosynthetic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000774355 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0008614 |
pyridoxine metabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000774355 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000774355 |
C |
Seeded From UniProt |
complete | ||
contributes_to |
GO:0004359 |
glutaminase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000774355 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004359 |
glutaminase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0042819 |
vitamin B6 biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0042823 |
pyridoxal phosphate biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004359 |
glutaminase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0036381 |
pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0036381 |
pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000079265 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0004359 |
glutaminase activity |
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 |
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 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000079265 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006541 |
glutamine metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016829 |
lyase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0042823 |
pyridoxal phosphate biosynthetic process |
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.
- ↑ 1.0 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
- ↑ 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
- ↑ 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
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