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O67019 (PDXA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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:aq_852
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length320 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 – 3203204-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188796

Sites

Metal binding1611Divalent metal cation; shared with dimeric partner By similarity
Metal binding2051Divalent metal cation; shared with dimeric partner By similarity
Metal binding2581Divalent metal cation; shared with dimeric partner By similarity
Binding site1321Substrate By similarity
Binding site2661Substrate By similarity
Binding site2751Substrate By similarity
Binding site2841Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O67019 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 9A31DCECB3EA0AE0

FASTA32035,914
        10         20         30         40         50         60 
MNKKIGITLG DPAGIGPELI LKISKHFKEK FTYVIYGEEK TLLEASKLTG IKLNYKKIEK 

        70         80         90        100        110        120 
VEEAKERGVY LIDLNVLKVP VVEPSVSSGK AAVAYLARAV ADAIRGNIHG ILTMPINKFW 

       130        140        150        160        170        180 
AKKAGFQYEG QTEFLAKASG TKDYAMMMYS EKLKVVLLTT HIPLKDVPNY VKKEEILKKV 

       190        200        210        220        230        240 
RLIRKEFLEK FKFEPLIKVL GLNPHAGEMG ELGREEIEEI IPAVEEAKKE GIKVVGPLVP 

       250        260        270        280        290        300 
DVAFINPSEE DVFLCMYHDQ GLIPFKMLAF DEGVNFTLGL PFIRTSPDHG TAYDIAWKNK 

       310        320 
ARESSSLHAL RLIEDLLDKI 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC06973.1.
PIRH70373.
RefSeqNP_213580.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67019.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_852.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC06973; AAC06973; aq_852.
GeneID1193561.
KEGGaae:aq_852.
PATRIC20959084. VBIAquAeo85532_0667.

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAPINKLAW.
OrthoDBEOG6GN6ZC.
ProtClustDBCLSK2299523.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-610-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_AQUAE
AccessionPrimary (citable) accession number: O67019
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 86 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