Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P19624 (PDXA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxythreonine-4-phosphate dehydrogenase

EC=1.1.1.262
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase
Gene names
Name:pdxA
Ordered Locus Names:b0052, JW0051
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). Ref.5 Ref.6

Catalytic activity

4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH. Ref.6

Cofactor

Binds 1 divalent metal cation per subunit. Can use ions such as zinc, magnesium or cobalt. Ref.5 Ref.7

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. HAMAP-Rule MF_00536

Subunit structure

Homodimer. Ref.7

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00536.

Miscellaneous

The active site is located at the dimer interface.

According to Ref.6, PdxA may catalyze both oxidation and decarboxylation reactions that directly lead to AHAP.

Sequence similarities

Belongs to the PdxA family.

Biophysicochemical properties

Kinetic parameters:

KM=85 µM for 4-(phosphohydroxy)-L-threonine (at 0.1 M Tris-HCl and pH 7.5) Ref.5

KM=113 µM for 4-(phosphohydroxy)-L-threonine (at 0.1 M phosphate buffer and pH 7.5)

Vmax=2.8 µmol/min/mg enzyme with 4-(phosphohydroxy)-L-threonine as substrate (at 0.1 M Tris-HCl and pH 7.5)

Vmax=0.66 µmol/min/mg enzyme with 4-(phosphohydroxy)-L-threonine as substrate (at 0.1 M phosphate buffer and pH 7.5)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-1112869,EBI-1112869

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3293294-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188804

Sites

Metal binding1661Divalent metal cation; shared with dimeric partner
Metal binding2111Divalent metal cation; shared with dimeric partner
Metal binding2661Divalent metal cation; shared with dimeric partner
Binding site1361Substrate
Binding site1371Substrate
Binding site2741Substrate
Binding site2831Substrate
Binding site2921Substrate

Secondary structure

........................................................ 329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19624 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 44E1FEE233C86233

FASTA32935,114
        10         20         30         40         50         60 
MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA TLLTNRAAML GLPLTLRPYS 

        70         80         90        100        110        120 
PNSPAQPQTA GTLTLLPVAL RAPVTAGQLA VENGHYVVET LARACDGCLN GEFAALITGP 

       130        140        150        160        170        180 
VHKGVINDAG IPFTGHTEFF EERSQAKKVV MMLATEELRV ALATTHLPLR DIADAITPAL 

       190        200        210        220        230        240 
LHEVIAILHH DLRTKFGIAE PRILVCGLNP HAGEGGHMGT EEIDTIIPVL NELRAQGMKL 

       250        260        270        280        290        300 
NGPLPADTLF QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA 

       310        320 
LELAGRGKAD VGSFITALNL AIKMIVNTQ 

« Hide

References

« Hide 'large scale' references
[1]"Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12."
Roa B.B., Connolly D.M., Winkler M.E.
J. Bacteriol. 171:4767-4777(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Biosynthesis of vitamin B6: the oxidation of 4-hydroxy-L-threonine 4-phosphate by pdxA."
Cane D.E., Hsiung Y., Cornish J.A., Robinson J.K., Spenser I.D.
J. Am. Chem. Soc. 120:1936-1937(1998)
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
[6]"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."
Banks J., Cane D.E.
Bioorg. Med. Chem. Lett. 14:1633-1636(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[7]"Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway."
Sivaraman J., Li Y., Banks J., Cane D.E., Matte A., Cygler M.
J. Biol. Chem. 278:43682-43690(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ZINC IONS, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M68521 Genomic DNA. Translation: AAA24305.1.
U00096 Genomic DNA. Translation: AAC73163.1.
AP009048 Genomic DNA. Translation: BAB96619.1.
PIRBVECXA. JV0026.
RefSeqNP_414594.1. NC_000913.3.
YP_488358.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PS6X-ray2.25A/B2-329[»]
1PS7X-ray2.47A/B/C/D1-329[»]
1PTMX-ray1.96A/B1-329[»]
ProteinModelPortalP19624.
SMRP19624. Positions 1-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10448N.
IntActP19624. 5 interactions.
STRING511145.b0052.

Proteomic databases

PaxDbP19624.
PRIDEP19624.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73163; AAC73163; b0052.
BAB96619; BAB96619; BAB96619.
GeneID12932019.
944919.
KEGGecj:Y75_p0052.
eco:b0052.
PATRIC32115203. VBIEscCol129921_0053.

Organism-specific databases

EchoBASEEB0685.
EcoGeneEG10691. pdxA.

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.
PhylomeDBP19624.

Enzyme and pathway databases

BioCycEcoCyc:PDXA-MONOMER.
ECOL316407:JW0051-MONOMER.
MetaCyc:PDXA-MONOMER.
UniPathwayUPA00244; UER00312.

Gene expression databases

GenevestigatorP19624.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
HAMAPMF_00536. PdxA.
InterProIPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view]
PfamPF04166. PdxA. 1 hit.
[Graphical view]
TIGRFAMsTIGR00557. pdxA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP19624.
PROP19624.

Entry information

Entry namePDXA_ECOLI
AccessionPrimary (citable) accession number: P19624
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene