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A7IJ81 (PDXA_XANP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:Xaut_2834
OrganismXanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) [Complete proteome] [HAMAP]
Taxonomic identifier78245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeXanthobacter

Protein attributes

Sequence length350 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 – 3503504-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000128267

Sites

Metal binding1731Divalent metal cation; shared with dimeric partner By similarity
Metal binding2181Divalent metal cation; shared with dimeric partner By similarity
Metal binding2731Divalent metal cation; shared with dimeric partner By similarity
Binding site1381Substrate By similarity
Binding site1391Substrate By similarity
Binding site2811Substrate By similarity
Binding site2901Substrate By similarity
Binding site2991Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A7IJ81 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 2C9C5E058EEDC905

FASTA35036,158
        10         20         30         40         50         60 
MVAPAPLVLS LGDPAGIGPD ITLTAWAQRR ELGLPAFLVA GDPEALKARV RQLGLTVPLA 

        70         80         90        100        110        120 
ETGPEDAAGH FAEALPVMPA GPASTALPGA PDASSAPCVV ASLEAALGLV QAGRAAALVT 

       130        140        150        160        170        180 
NPLAKSVMYA GGFPFPGHTE FLAARAARPG RPAPHPVMMI WSEQLAVVPA TIHLPYADVP 

       190        200        210        220        230        240 
GHLTIDLLVE TGRIVAGDMA RRFGLAHPRL VFCGLNPHAG EEGTLGTEDE AIVRPAVEAL 

       250        260        270        280        290        300 
KREGIDARGP LPADTLFHPQ ARAGYDVAVG MYHDQVLIPA KTLAFHDGVN VTLGLPFIRT 

       310        320        330        340        350 
SPDHGTAFDI AGTGRANPSS LVAALRLARR LADAEARLAA REGHRAASVA 

« Hide

References

[1]"Complete sequence of chromosome of Xanthobacter autotrophicus Py2."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1158 / Py2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000781 Genomic DNA. Translation: ABS68074.1.
RefSeqYP_001417731.1. NC_009720.1.

3D structure databases

ProteinModelPortalA7IJ81.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING78245.Xaut_2834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS68074; ABS68074; Xaut_2834.
GeneID5423084.
KEGGxau:Xaut_2834.
PATRIC24047767. VBIXanAut29526_3168.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
ProtClustDBCLSK979874.

Enzyme and pathway databases

BioCycXAUT78245:GHS6-2862-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_XANP2
AccessionPrimary (citable) accession number: A7IJ81
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 50 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