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Q3V7Q4 (PDXA_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:YPTB0634
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [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_1000061037

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
Q3V7Q4 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 9E7F0A5C87D0909C

FASTA33135,240
        10         20         30         40         50         60 
MHNHNNRLVI TPGEPAGVGP DLAIALAQQD WPVELVVCAD PALLLARASQ LNLPLQLREY 

        70         80         90        100        110        120 
QADQPAIAQQ AGSLTILPVK TAVNVVPGKL DVGNSHYVVE TLAKACDGAI SGEFAALVTG 

       130        140        150        160        170        180 
PVQKSIINDA GIPFIGHTEF FADRSHCQRV VMMLATEELR VALATTHLPL LAVPGAITQA 

       190        200        210        220        230        240 
SLHEVITILD NDLKTKFGIT QPQIYVCGLN PHAGEGGHMG HEEIDTIIPA LNTLRQQGIN 

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

       310        320        330 
ALELAATGTA DVGSFITALN LAIKMINNSN E 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH19874.1.
RefSeqYP_069176.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ3V7Q4.
SMRQ3V7Q4. Positions 7-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273123.YPTB0634.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH19874; CAH19874; YPTB0634.
GeneID2956222.
KEGGyps:YPTB0634.
PATRIC18639516. VBIYerPse22266_0850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-675-MONOMER.
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_YERPS
AccessionPrimary (citable) accession number: Q3V7Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 11, 2005
Last modified: May 14, 2014
This is version 61 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