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A1JJF5 (PDXA_YERE8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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:YE0631
OrganismYersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) [Complete proteome] [HAMAP]
Taxonomic identifier393305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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) By similarity. HAMAP-Rule MF_00536

Catalytic activity

4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH. HAMAP-Rule MF_00536

Cofactor

Binds 1 divalent metal cation per subunit. Can use ions such as zinc, magnesium or cobalt By similarity.

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 By similarity. HAMAP-Rule MF_00536

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00536.

Miscellaneous

The active site is located at the dimer interface By similarity.

Sequence similarities

Belongs to the PdxA family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3313314-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000061035

Sites

Metal binding1671Divalent metal cation; shared with dimeric partner By similarity
Metal binding2121Divalent metal cation; shared with dimeric partner By similarity
Metal binding2671Divalent metal cation; shared with dimeric partner By similarity
Binding site1371Substrate By similarity
Binding site1381Substrate By similarity
Binding site2751Substrate By similarity
Binding site2841Substrate By similarity
Binding site2931Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1JJF5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 52BF40C3951A4E59

FASTA33135,361
        10         20         30         40         50         60 
MQNHNNRIVI TPGEPAGVGP DLVIALAQQD WPVELVVCAD PALLLTRASQ LNLPLQLREY 

        70         80         90        100        110        120 
QQDKPALAQL AGTLTILPVK IAAEVIPGQL DVKNSHYVVE TLAKACDGAI SGEFAALVTG 

       130        140        150        160        170        180 
PVQKSIINDA GIPFIGHTEF FADRSHCSRV VMMLATEELR VALATTHLPL LAVPGAITQT 

       190        200        210        220        230        240 
SLHEVISILD NDLKTKFGIS QPQIYVCGLN PHAGEGGHMG HEEIETIIPA LATLRQQGIN 

       250        260        270        280        290        300 
LIGPLPADTL FQPKYLQHAD AVLAMYHDQG LPVLKYQGFG RAVNITLGLP FIRTSVDHGT 

       310        320        330 
ALELAATGTA DVGSFITALN LAIKMINNSN E 

« Hide

References

[1]"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081."
Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. expand/collapse author list , Quail M.A., Dougan G., Parkhill J., Prentice M.B.
PLoS Genet. 2:2039-2051(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 13174 / 8081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286415 Genomic DNA. Translation: CAL10743.1.
RefSeqYP_001004983.1. NC_008800.1.

3D structure databases

ProteinModelPortalA1JJF5.
SMRA1JJF5. Positions 7-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393305.YE0631.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL10743; CAL10743; YE0631.
GeneID4712934.
KEGGyen:YE0631.
PATRIC18560672. VBIYerEnt11519_0724.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK00232.

Enzyme and pathway databases

UniPathwayUPA00244; UER00312.

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...

Entry information

Entry namePDXA_YERE8
AccessionPrimary (citable) accession number: A1JJF5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 56 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

PATHWAY comments

Index of metabolic and biosynthesis pathways