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Q8RGR0 (PDXA_FUSNN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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:FN0226
OrganismFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131) [Reference proteome] [HAMAP]
Taxonomic identifier190304 [NCBI]
Taxonomic lineageBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium

Protein attributes

Sequence length332 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 – 3323324-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188808

Sites

Metal binding1681Divalent metal cation; shared with dimeric partner By similarity
Metal binding2111Divalent metal cation; shared with dimeric partner By similarity
Metal binding2661Divalent metal cation; shared with dimeric partner By similarity
Binding site1381Substrate By similarity
Binding site1391Substrate By similarity
Binding site2741Substrate By similarity
Binding site2921Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8RGR0 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: A9032E3F6E7081FC

FASTA33236,547
        10         20         30         40         50         60 
MRTKIAIPMG DPAGVGPEIV VKTAVSKEIL DLCDLVVIGD KKVLEKATKI CQVDLKIHTI 

        70         80         90        100        110        120 
KNIEEGKYEK GILNVIDLEN VDMNTLEYGQ VQGMCGKAAF EYIKKCVELA MEYKVDAIAT 

       130        140        150        160        170        180 
TPINKESLRA GNVNYIGHTE ILGDLSNSRD PLTMFEVDNM RVFFLTRHMS LRKACDAITK 

       190        200        210        220        230        240 
ERVLEYIERC TKALKQLGVT GKMAVAGLNP HSGEHGLFGN EEVKEITPAI EEAQKLGYDV 

       250        260        270        280        290        300 
VGPIGADSVF HQALQGRYVA VLSLYHDQGH IATKTYDFER TIAITLDMPF LRTSVDHGTA 

       310        320        330 
FDIAGKGIVS AISMIEAVKL AAKYAPNFKN IK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009951 Genomic DNA. Translation: AAL94432.1.
RefSeqNP_603133.1. NC_003454.1.

3D structure databases

ProteinModelPortalQ8RGR0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190304.FN0226.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL94432; AAL94432; FN0226.
GeneID993114.
KEGGfnu:FN0226.
PATRIC21950229. VBIFusNuc122357_0807.

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMAAIPMGDP.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

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_FUSNN
AccessionPrimary (citable) accession number: Q8RGR0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 2002
Last modified: May 14, 2014
This is version 80 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