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C0QBU5 (PDXA_DESAH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:HRM2_18550
OrganismDesulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2) [Complete proteome] [HAMAP]
Taxonomic identifier177437 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfobacterium

Protein attributes

Sequence length340 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 – 3403404-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000211912

Sites

Metal binding1711Divalent metal cation; shared with dimeric partner By similarity
Metal binding2161Divalent metal cation; shared with dimeric partner By similarity
Metal binding2711Divalent metal cation; shared with dimeric partner By similarity
Binding site1411Substrate By similarity
Binding site1421Substrate By similarity
Binding site2791Substrate By similarity
Binding site2881Substrate By similarity
Binding site2971Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
C0QBU5 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: D10C3F53007C3BA4

FASTA34036,215
        10         20         30         40         50         60 
MTDNRPVIGI TMGDPVGIGP EIIVSALDDP FVYTVCRPLV LGDEGVMERA IDLKSARMDV 

        70         80         90        100        110        120 
HTTDTPAGGK YCHGTMDIVP LSRLDAATLL AGHPTPGTGK AMIDYITTGV DLAMDGKIQA 

       130        140        150        160        170        180 
IATCPITKTA MKLAGSKFHG HTELIADRTH TPRVAMMMAG DRLRVVLVTI HIPLCEVSAR 

       190        200        210        220        230        240 
LNQAEILATI SLTSETLKTK FGIPEPRIAV AGLNPHGGED GMFGSEELEI IAPAVEQARS 

       250        260        270        280        290        300 
KGITVSGPFP PDTLFFNAAN HKFDAVVCMY HDQGLIPFKM IHFSDGVNTT LGLPIIRTSV 

       310        320        330        340 
DHGTAYDIAW RGTADPSSLI AAIKMAALQA TITGANRINR 

« Hide

References

[1]"Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate reducer oxidizing organic carbon completely to carbon dioxide."
Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S., Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A., Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O., Meyerdierks A., Gottschalk G., Amann R.
Environ. Microbiol. 11:1038-1055(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43914 / DSM 3382 / HRM2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001087 Genomic DNA. Translation: ACN14957.1.
RefSeqYP_002603121.1. NC_012108.1.

3D structure databases

ProteinModelPortalC0QBU5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177437.HRM2_18550.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACN14957; ACN14957; HRM2_18550.
GeneID7500958.
KEGGdat:HRM2_18550.
PATRIC21683381. VBIDesAut25181_1961.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycDAUT177437:GHLR-1854-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_DESAH
AccessionPrimary (citable) accession number: C0QBU5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 5, 2009
Last modified: February 19, 2014
This is version 40 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