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B2VGP9 (PDXA_ERWT9) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:ETA_07250
OrganismErwinia tasmaniensis (strain DSM 17950 / Et1/99) [Complete proteome] [HAMAP]
Taxonomic identifier338565 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeErwinia

Protein attributes

Sequence length330 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 – 3303304-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000128248

Sites

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

Sequences

Sequence LengthMass (Da)Tools
B2VGP9 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: C511959C5572CE10

FASTA33035,502
        10         20         30         40         50         60 
MLSKQRVVIT SGEPAGIGPD LVVQLAQQDW PVELVVCADP ELLRDRAAVL RLPLTLREYQ 

        70         80         90        100        110        120 
PGTDAQPQQA GSLTVLPAHL AQPVNAGELC VDNSHYVLET LARACDGCLS GEFAALITGP 

       130        140        150        160        170        180 
VHKGAINDAG IPFSGHTEFF AERARCERVV MMLATEELRV ALATTHLPLK DVAASITRTT 

       190        200        210        220        230        240 
LHEVITILYQ DLQSKFGRAE PHIFVCGLNP HAGEGGHMGR EEIDVIIPAL DELRQQGMKL 

       250        260        270        280        290        300 
TGPLPADTLF QPKYLQHADA VLAMYHDQGL PVLKYQGFGR AVNITLGLPF IRTSVDHGTA 

       310        320        330 
LELAGSGQAD AGSFKTALNL AITMIKSSNE 

« Hide

References

[1]"The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic bacterium in the genus Erwinia."
Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R., Geider K.
Environ. Microbiol. 10:2211-2222(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17950 / Et1/99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU468135 Genomic DNA. Translation: CAO95771.1.
RefSeqYP_001906669.1. NC_010694.1.

3D structure databases

ProteinModelPortalB2VGP9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING465817.ETA_07250.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAO95771; CAO95771; ETA_07250.
GeneID6299238.
KEGGeta:ETA_07250.
PATRIC20427168. VBIErwTas9546_0775.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycETAS465817:GI36-764-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_ERWT9
AccessionPrimary (citable) accession number: B2VGP9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: May 14, 2014
This is version 48 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