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B4U950 (PDXA_HYDS0) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:HY04AAS1_0974
OrganismHydrogenobaculum sp. (strain Y04AAS1) [Complete proteome] [HAMAP]
Taxonomic identifier380749 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeHydrogenobaculum

Protein attributes

Sequence length310 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 – 3103104-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000146489

Sites

Metal binding1581Divalent metal cation; shared with dimeric partner By similarity
Metal binding2021Divalent metal cation; shared with dimeric partner By similarity
Metal binding2501Divalent metal cation; shared with dimeric partner By similarity
Binding site1291Substrate By similarity
Binding site2581Substrate By similarity
Binding site2671Substrate By similarity
Binding site2761Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4U950 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 2C1FDF60B25CB139

FASTA31034,242
        10         20         30         40         50         60 
MKIFGITMGD PAGIGPELIL KLQKDMEDEN AYVIYGEEYI LKHASSVLGQ NFYYEKVNSV 

        70         80         90        100        110        120 
DDVKDKGIYL ISLSLKGALE PSPSSGKLAI AYLARATADA ISKKLNGILT MPINKYFAKA 

       130        140        150        160        170        180 
SGFSFNGQTE YLAFADNKKD FAMMMYSDAI KVVLATIHIP LKDIANAINV ELIKQKIKLI 

       190        200        210        220        230        240 
KDYIPKYFRF IPTIKVLGLN PHAGEGGLIG DEEAKIIIPA IRDEDVVGPI PPDTAFIDIK 

       250        260        270        280        290        300 
KDDIFLCMYH DQGLIPFKML AFDKGSNVTI GLSFLRTSPD HGTAYDIAYK GLARVDSAGY 

       310 
SLELLKRYGY 

« 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: Y04AAS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001130 Genomic DNA. Translation: ACG57661.1.
RefSeqYP_002121639.1. NC_011126.1.

3D structure databases

ProteinModelPortalB4U950.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING380749.HY04AAS1_0974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACG57661; ACG57661; HY04AAS1_0974.
GeneID6743786.
KEGGhya:HY04AAS1_0974.
PATRIC22136638. VBIHydSp64203_0982.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAGTIDCID.
OrthoDBEOG6GN6ZC.
ProtClustDBCLSK2299523.

Enzyme and pathway databases

BioCycHSP380749:GH30-1008-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_HYDS0
AccessionPrimary (citable) accession number: B4U950
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 46 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