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B2FPG6 (PDXA_STRMK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:Smlt0819
OrganismStenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP]
Taxonomic identifier522373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Protein attributes

Sequence length326 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. Can use ions such as zinc, magnesium or cobalt 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3263264-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000128264

Sites

Metal binding1601Divalent metal cation; shared with dimeric partner By similarity
Metal binding2051Divalent metal cation; shared with dimeric partner By similarity
Metal binding2601Divalent metal cation; shared with dimeric partner By similarity
Binding site1321Substrate By similarity
Binding site2681Substrate By similarity
Binding site2771Substrate By similarity
Binding site2861Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2FPG6 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: DE8F3CFFC8C14554

FASTA32634,032
        10         20         30         40         50         60 
MRPELALVPG EPAGIGPELC VRLVQQPRED CRLLAFADPD TLRAAAAALN LPLQLLPEGA 

        70         80         90        100        110        120 
EARVPGDLRL RVVANATPSR FGQADPANAG AVIGALLGAG QACLSGELHG VVTGPVHKAV 

       130        140        150        160        170        180 
INEGGIAYSG TTELLADQAG VKVVMMLANH IVRVALATTH LPLREVADAI TAPSLEHTLR 

       190        200        210        220        230        240 
TVHAALRREF GLPAPRIAVL GLNPHAGEDG HLGREELDLV IPLLQRLRAE GMDLIGPLPA 

       250        260        270        280        290        300 
DTAFLPAKLA GFDTVLAMYH DQGLPVLKYS GFEQAVNLTL GLPYPRVAVD HGTALDLAGR 

       310        320 
GVADPSSLQA ATTLCAQLAR QRTLSA 

« Hide

References

[1]"The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. expand/collapse author list , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K279a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM743169 Genomic DNA. Translation: CAQ44395.1.
RefSeqYP_001970709.1. NC_010943.1.

3D structure databases

ProteinModelPortalB2FPG6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING522373.Smlt0819.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ44395; CAQ44395; Smlt0819.
GeneID6392638.
KEGGsml:Smlt0819.
PATRIC23697359. VBISteMal45202_0788.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycSMAL522373:GJE8-791-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_STRMK
AccessionPrimary (citable) accession number: B2FPG6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 49 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