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ECOLI:PDXA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) pdxA
Protein Name(s) 4-hydroxythreonine-4-phosphate dehydrogenase

4-(phosphohydroxy)-L-threonine dehydrogenase

External Links
UniProt P19624
EMBL M68521
U00096
AP009048
PIR JV0026
RefSeq NP_414594.1
YP_488358.1
PDB 1PS6
1PS7
1PTM
PDBsum 1PS6
1PS7
1PTM
ProteinModelPortal P19624
SMR P19624
DIP DIP-10448N
IntAct P19624
STRING 511145.b0052
PaxDb P19624
PRIDE P19624
EnsemblBacteria AAC73163
BAB96619
GeneID 12932019
944919
KEGG ecj:Y75_p0052
eco:b0052
PATRIC 32115203
EchoBASE EB0685
EcoGene EG10691
eggNOG COG1995
HOGENOM HOG000221592
InParanoid P19624
KO K00097
OMA DTLFQDK
OrthoDB EOG6GN6ZC
PhylomeDB P19624
BioCyc EcoCyc:PDXA-MONOMER
ECOL316407:JW0051-MONOMER
MetaCyc:PDXA-MONOMER
UniPathway UPA00244
EvolutionaryTrace P19624
PRO PR:P19624
Proteomes UP000000318
UP000000625
Genevestigator P19624
GO GO:0005737
GO:0050570
GO:0050897
GO:0042802
GO:0000287
GO:0051287
GO:0008270
GO:0042823
GO:0008615
Gene3D 3.40.718.10
HAMAP MF_00536
InterPro IPR024084
IPR005255
Pfam PF04166
TIGRFAMs TIGR00557

Annotations

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

enables

GO:0042802

identical protein binding

PMID:24627523[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P19624

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24561554[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P19624

F

Seeded From UniProt

complete

enables

GO:0051287

NAD binding

PMID:12896974[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0050570

4-hydroxythreonine-4-phosphate dehydrogenase activity

PMID:15026039[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0042823

pyridoxal phosphate biosynthetic process

PMID:1537800[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008615

pyridoxine biosynthetic process

PMID:1537800[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:15026039[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:12896974[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:15026039[4]

ECO:0000314

direct assay evidence used in manual assertion

F

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:IPR037510

P

Seeded From UniProt

complete

enables

GO:0050570

4-hydroxythreonine-4-phosphate dehydrogenase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR037510

F

Seeded From UniProt

complete

enables

GO:0051287

NAD binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005255

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005255

P

Seeded From UniProt

complete

enables

GO:0050570

4-hydroxythreonine-4-phosphate dehydrogenase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.1.1.262

F

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:UR000094090

P

Seeded From UniProt

complete

involved_in

GO:0008615

pyridoxine biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094090

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094090

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094090

C

Seeded From UniProt

complete

enables

GO:0050570

4-hydroxythreonine-4-phosphate dehydrogenase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094090

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094090

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094090

F

Seeded From UniProt

complete

enables

GO:0050897

cobalt ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094090

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0008615

pyridoxine biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0664

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

Notes

References

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

  1. Häuser, R et al. (2014) A second-generation protein-protein interaction network of Helicobacter pylori. Mol. Cell Proteomics 13 1318-29 PubMed GONUTS page
  2. Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
  3. 3.0 3.1 Sivaraman, J et al. (2003) Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway. J. Biol. Chem. 278 43682-90 PubMed GONUTS page
  4. 4.0 4.1 4.2 Banks, J & Cane, DE (2004) Biosynthesis of vitamin B6: direct identification of the product of the PdxA-catalyzed oxidation of 4-hydroxy-l-threonine-4-phosphate using electrospray ionization mass spectrometry. Bioorg. Med. Chem. Lett. 14 1633-6 PubMed GONUTS page
  5. 5.0 5.1 Lam, HM et al. (1992) Suppression of insertions in the complex pdxJ operon of Escherichia coli K-12 by lon and other mutations. J. Bacteriol. 174 1554-67 PubMed GONUTS page