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A8ZUN0 (PDXA_DESOH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:Dole_0633
OrganismDesulfococcus oleovorans (strain DSM 6200 / Hxd3) [Complete proteome] [HAMAP]
Taxonomic identifier96561 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfococcus

Protein attributes

Sequence length338 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 – 3383384-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000211913

Sites

Metal binding1691Divalent metal cation; shared with dimeric partner By similarity
Metal binding2141Divalent metal cation; shared with dimeric partner By similarity
Metal binding2701Divalent metal cation; shared with dimeric partner By similarity
Binding site1391Substrate By similarity
Binding site1401Substrate By similarity
Binding site2781Substrate By similarity
Binding site2871Substrate By similarity
Binding site2961Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A8ZUN0 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 2F821914F8A5FDD8

FASTA33835,285
        10         20         30         40         50         60 
MNPRPLIGIT MGDPVGIGPE IILTALAGTS VYEKCRPLVI GDPGVLGQAM AVAGYAPVIH 

        70         80         90        100        110        120 
MTDTPETGVY RPGTISMFSP APPLSPVTWG EPTPETGGAM EAWITTAVDM AMAGAISAMV 

       130        140        150        160        170        180 
TCPINKEALK MAGSAFAGHT EMLAMRTGTN RYAMMLAGNR LRVVLVTIHT ALQNVPGLLS 

       190        200        210        220        230        240 
VDAIADTILL TVESLKQRFG MNAPRVAVAG LNPHAGEGGL FGDEEARLIT PAIEAARRKT 

       250        260        270        280        290        300 
EAAITGPWPP DTVFVKAAAG DFDAVVCMYH DQGLIPFKLL HFEDGVNTTL GLPIIRTSVD 

       310        320        330 
HGTAYDIAGT GRADCRSLTA AIDMAIDQAA CLGKRPAA 

« Hide

References

[1]"Complete sequence of Desulfococcus oleovorans Hxd3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Wawrik B., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6200 / Hxd3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000859 Genomic DNA. Translation: ABW66443.1.
RefSeqYP_001528520.1. NC_009943.1.

3D structure databases

ProteinModelPortalA8ZUN0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING96561.Dole_0633.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW66443; ABW66443; Dole_0633.
GeneID5693462.
KEGGdol:Dole_0633.
PATRIC21691273. VBIDesOle35880_0654.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMAADTLFHF.
OrthoDBEOG6GN6ZC.
ProtClustDBCLSK2401939.

Enzyme and pathway databases

BioCycDOLE96561:GHF3-648-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_DESOH
AccessionPrimary (citable) accession number: A8ZUN0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 52 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