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Q3V818 (PDXA_SYMTH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:STH2300
OrganismSymbiobacterium thermophilum (strain T / IAM 14863) [Complete proteome] [HAMAP]
Taxonomic identifier292459 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium

Protein attributes

Sequence length335 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
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 – 3353354-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000211916

Sites

Metal binding1701Divalent metal cation; shared with dimeric partner By similarity
Metal binding2141Divalent metal cation; shared with dimeric partner By similarity
Metal binding2691Divalent metal cation; shared with dimeric partner By similarity
Binding site1401Substrate By similarity
Binding site1411Substrate By similarity
Binding site2771Substrate By similarity
Binding site2951Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3V818 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: C6B4D45E97B0DEDE

FASTA33536,102
        10         20         30         40         50         60 
MDTRPLIGIT MGDPASIGPE IAAKALANPE IYALCRPLLI GDSRVMARAF ETTGVKLNLN 

        70         80         90        100        110        120 
PVATPAEGKY AHGTVDLIDL PVVDMGTLQW GQVQAQAGAA AFAYIKRSIE LALEGAVDAV 

       130        140        150        160        170        180 
TTGPINKEAL KAARIDFIGH TEIFGELTGS HDPLTMFETK GLRIFFLTRH VSLAQACRMI 

       190        200        210        220        230        240 
TRDRVLDYIR RCTAALEQLG LVRPKLAVAG LNPHCGEHGL FGDEEVREIE PAVQQAQAEG 

       250        260        270        280        290        300 
YNVSGPHPAD SVFWHAAQGR FDAVLSLYHD QGHIAAKMYD FERTVSITAG LPFLRSSVDH 

       310        320        330 
GTAFDIAGTG RASAVSLEEA IRVGAKYAAA FRRTR 

« Hide

References

[1]"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T / IAM 14863.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006840 Genomic DNA. Translation: BAD41285.1.
RefSeqYP_076129.1. NC_006177.1.

3D structure databases

ProteinModelPortalQ3V818.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292459.STH2300.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD41285; BAD41285; STH2300.
GeneID2979467.
KEGGsth:STH2300.
PATRIC23782778. VBISymThe116959_2303.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMAINPHSGD.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK03743.

Enzyme and pathway databases

BioCycSTHE292459:GJMM-2375-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_SYMTH
AccessionPrimary (citable) accession number: Q3V818
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: October 11, 2005
Last modified: February 19, 2014
This is version 65 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