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ECOLI:PDXJ

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) pdxJ
Protein Name(s) Pyridoxine 5'-phosphate synthase

PNP synthase

External Links
UniProt P0A794
EMBL M76470
M74526
D64044
U36841
U00096
AP009048
PIR A42293
RefSeq NP_417059.1
YP_490792.1
PDB 1HO1
1HO4
1IXN
1IXO
1IXP
1IXQ
1M5W
PDBsum 1HO1
1HO4
1IXN
1IXO
1IXP
1IXQ
1M5W
ProteinModelPortal P0A794
SMR P0A794
DIP DIP-36215N
IntAct P0A794
MINT MINT-1227457
STRING 511145.b2564
PaxDb P0A794
PRIDE P0A794
EnsemblBacteria AAC75617
BAE76740
GeneID 12931607
947039
KEGG ecj:Y75_p2517
eco:b2564
PATRIC 32120527
EchoBASE EB0687
EcoGene EG10693
eggNOG COG0854
HOGENOM HOG000258095
InParanoid P0A794
KO K03474
OMA GMEELNI
OrthoDB EOG6M9F0H
PhylomeDB P0A794
BioCyc EcoCyc:PDXJ-MONOMER
ECOL316407:JW2548-MONOMER
MetaCyc:PDXJ-MONOMER
UniPathway UPA00244
EvolutionaryTrace P0A794
PRO PR:P0A794
Proteomes UP000000318
UP000000625
Genevestigator P0A794
GO GO:0005829
GO:0033856
GO:0008615
Gene3D 3.20.20.70
HAMAP MF_00279
InterPro IPR013785
IPR004569
Pfam PF03740
SUPFAM SSF63892
TIGRFAMs TIGR00559

Annotations

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

part_of

GO:0005829

cytosol

PMID:16858726[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0033856

pyridoxine 5'-phosphate synthase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10693
PANTHER:PTN000765245

F

Seeded From UniProt

complete

involved_in

GO:0008615

pyridoxine biosynthetic process

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10693
PANTHER:PTN000765245

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10693
PANTHER:PTN000765245

C

Seeded From UniProt

complete

involved_in

GO:0008615

pyridoxine biosynthetic process

PMID:1537799[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:10944349[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0033856

pyridoxine 5'-phosphate synthase activity

PMID:10225425[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013785

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004569
InterPro:IPR036130

C

Seeded From UniProt

complete

involved_in

GO:0008615

pyridoxine biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004569
InterPro:IPR036130

P

Seeded From UniProt

complete

enables

GO:0033856

pyridoxine 5'-phosphate synthase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004569
InterPro:IPR036130

F

Seeded From UniProt

complete

enables

GO:0033856

pyridoxine 5'-phosphate synthase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.6.99.2

F

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:UR000083111

P

Seeded From UniProt

complete

enables

GO:0016769

transferase activity, transferring nitrogenous groups

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000083111

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:UR000083111

C

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

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

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

Notes

References

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

  1. Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  2. 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. Takiff, HE et al. (1992) Locating essential Escherichia coli genes by using mini-Tn10 transposons: the pdxJ operon. J. Bacteriol. 174 1544-53 PubMed GONUTS page
  4. Garrido Franco, M et al. (2000) Crystallization and preliminary X-ray crystallographic analysis of PdxJ, the pyridoxine 5'-phosphate synthesizing enzyme. Acta Crystallogr. D Biol. Crystallogr. 56 1045-8 PubMed GONUTS page
  5. Laber, B et al. (1999) Vitamin B6 biosynthesis: formation of pyridoxine 5'-phosphate from 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by PdxA and PdxJ protein. FEBS Lett. 449 45-8 PubMed GONUTS page
  6. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page