Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8DHB4 (PDXA_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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:tll2045
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length341 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 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

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpyridoxal phosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-hydroxythreonine-4-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

NAD binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3413414-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188831

Sites

Metal binding1611Divalent metal cation; shared with dimeric partner By similarity
Metal binding2061Divalent metal cation; shared with dimeric partner By similarity
Metal binding2721Divalent metal cation; shared with dimeric partner By similarity
Binding site1261Substrate By similarity
Binding site2801Substrate By similarity
Binding site2891Substrate By similarity
Binding site2981Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DHB4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 66DAC85253DE0D23

FASTA34136,500
        10         20         30         40         50         60 
MSLALTLGDP AGIGPEILLK ALAHLPSELL GQFFIAGTGQ VLEETYARLC QQGQVAIDPA 

        70         80         90        100        110        120 
QLQLWEHPLD EVIVPGRPSV ASGTASFAYL KTAIQRAIAG EVAGIVTAPI SKACWQAAGY 

       130        140        150        160        170        180 
SFPGQTEVLA HLTGTAHVGM LFLGRSPVTH WVLTTLLATT HIPLQAVPRA LTPEGLNEKL 

       190        200        210        220        230        240 
ALLIQFLRER RHLERPRIAI AGLNPHSGEQ GHLGQEEVTW LIPWLAAAQQ QYPEVELIGP 

       250        260        270        280        290        300 
VPPDTLWIGA ADAWWGRPAP ATAYDAYLAL YHDQGLIPVK MLAFREAVNT TIGLPFIRTS 

       310        320        330        340 
PDHGTAFDIA GTGVADPQSF LAAIAWAQTL SKGSVFPLTL A 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC09597.1.
RefSeqNP_682835.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DHB4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tll2045.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC09597; BAC09597; BAC09597.
GeneID1011601.
KEGGtel:tll2045.
PATRIC23929506. VBITheElo119873_2140.

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK02746.

Enzyme and pathway databases

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_THEEB
AccessionPrimary (citable) accession number: Q8DHB4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 71 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