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B2V9E6 (PDXA_SULSY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:SYO3AOP1_0946
OrganismSulfurihydrogenibium sp. (strain YO3AOP1) [Complete proteome] [HAMAP]
Taxonomic identifier436114 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesHydrogenothermaceaeSulfurihydrogenibium

Protein attributes

Sequence length322 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 – 3223224-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000146493

Sites

Metal binding1611Divalent metal cation; shared with dimeric partner By similarity
Metal binding2061Divalent metal cation; shared with dimeric partner By similarity
Metal binding2591Divalent metal cation; shared with dimeric partner By similarity
Binding site1311Substrate By similarity
Binding site1321Substrate By similarity
Binding site2671Substrate By similarity
Binding site2761Substrate By similarity
Binding site2851Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2V9E6 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: B5AFA28A3EAECBEE

FASTA32235,609
        10         20         30         40         50         60 
MVKLAITLGD PSGINSEILL KALNKLPKRN ISYVIYGSKK ALEKAKKLTG VDLNIKEIKS 

        70         80         90        100        110        120 
INDVVKSGIY LINLYDLDVE FGSSSKETGK ASVVYLENAV KDVLEKKADA LITLPISKQW 

       130        140        150        160        170        180 
IMESGFPYAG HTDYLAEVSG AKEYAMVLMC KKLKVALITT HIPLKDVPSQ ITKEKIISKV 

       190        200        210        220        230        240 
RLINREFKEK FGISKPKIAI LGLNPHASDN GNIGNEEQNI ILPAVKTLRE DGIEITDPLS 

       250        260        270        280        290        300 
PDTAFNRYKD FDIYVAMYHD QGLIPLKLLC FRKAVNITLG LPFIRTSPDH GTGYDIAGKN 

       310        320 
IADPSSTIEA VELAILLKRV RK 

« Hide

References

[1]"Complete and draft genome sequences of six members of the Aquificales."
Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.
J. Bacteriol. 191:1992-1993(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YO3AOP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001080 Genomic DNA. Translation: ACD66569.1.
RefSeqYP_001931123.1. NC_010730.1.

3D structure databases

ProteinModelPortalB2V9E6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436114.SYO3AOP1_0946.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD66569; ACD66569; SYO3AOP1_0946.
GeneID6331017.
KEGGsul:SYO3AOP1_0946.
PATRIC23766709. VBISulSp94719_0986.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAAPINKHN.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycSSP436114:GI6I-989-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_SULSY
AccessionPrimary (citable) accession number: B2V9E6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 1, 2008
Last modified: May 14, 2014
This is version 47 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