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Q6AB12 (PDXA_PROAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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:PPA0296
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length346 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 – 3463464-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000211915

Sites

Metal binding1711Divalent metal cation; shared with dimeric partner By similarity
Metal binding2151Divalent metal cation; shared with dimeric partner By similarity
Metal binding2701Divalent metal cation; shared with dimeric partner By similarity
Binding site1411Substrate By similarity
Binding site1421Substrate By similarity
Binding site2781Substrate By similarity
Binding site2961Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AB12 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 431C4C2534887BFD

FASTA34636,659
        10         20         30         40         50         60 
MPKTPLLGIT EGDPAGIGPE ITVQAIHNMA DDRSFIPIVY GDPAIISRAC SVTGLSETVR 

        70         80         90        100        110        120 
RVTSEEHIEP ESNVINVVDT GTVPHADSIE WGSVQELAGR AAIASIEAAT DAALSGKTDG 

       130        140        150        160        170        180 
VVTSPINKEA IWKTGSEFLG HTEMLGSLCG TPDTDTMFVV SGLKIFFATR HMSLREAVDS 

       190        200        210        220        230        240 
IRRDLIDHEI HKALRALKVF GCNSPKLAVA ALNPHAGEGG HFGTEEIEVL RPAVKSACAE 

       250        260        270        280        290        300 
GHNVVGPVPA DSVFHKGVIR EYDGVLSLYH DQGHIASKTL DFDGTVSVTA GLPILRTSVD 

       310        320        330        340 
HGTAFDIAGQ GAASPMTMQS ALHVASDFAR FVPVIREEYL PSTGRN 

« Hide

References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017283 Genomic DNA. Translation: AAT82054.1.
RefSeqYP_055012.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6AB12.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267747.PPA0296.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT82054; AAT82054; PPA0296.
GeneID2932160.
KEGGpac:PPA0296.
PATRIC23035247. VBIProAcn64440_0308.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMAKINTILY.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycPACN267747:GHO9-298-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_PROAC
AccessionPrimary (citable) accession number: Q6AB12
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 13, 2004
Last modified: May 14, 2014
This is version 67 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