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Q2N8X0 (PDXA_ERYLH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:ELI_08895
OrganismErythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]
Taxonomic identifier314225 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesErythrobacteraceaeErythrobacter

Protein attributes

Sequence length336 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 – 3363364-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000051500

Sites

Metal binding1711Divalent metal cation; shared with dimeric partner By similarity
Metal binding2161Divalent metal cation; shared with dimeric partner By similarity
Metal binding2711Divalent metal cation; shared with dimeric partner By similarity
Binding site1401Substrate By similarity
Binding site2791Substrate By similarity
Binding site2881Substrate By similarity
Binding site2971Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2N8X0 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 213B605C1BF17B80

FASTA33634,465
        10         20         30         40         50         60 
MGEPQRPLAV SLGDPAGIGP EIIVHAWRMR DSANLAPFAV AGGANVLRSA TEALGVPCPI 

        70         80         90        100        110        120 
QEIDDIAEAN SAFLEALPVI KGLDGAYLPG APDPIGAKLA LKSLEMATRL ATAGHASGVV 

       130        140        150        160        170        180 
TAPIAKGLLE QVGFTHPGQT EFLAAACGLP EDASVMMLAG PSLRAVPLTV HCPLAEVPGL 

       190        200        210        220        230        240 
LSIGLIVERG RIVASALQRD FGIERPRLAV TGLNPHAGED GKFGNEEQDV IAPAIAELLA 

       250        260        270        280        290        300 
DGITATGPHP ADALFSPHSR AGFDAALCMY HDQALIPVKA LDFDQGVNVT LGLPIVRTSP 

       310        320        330 
DHGTAFDIAG RGTAHPGAMV FALLMAGECA ARRADA 

« Hide

References

[1]"Complete genome sequence of Erythrobacter litoralis HTCC2594."
Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.
J. Bacteriol. 191:2419-2420(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTCC2594.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000157 Genomic DNA. Translation: ABC63871.1.
RefSeqYP_458668.1. NC_007722.1.

3D structure databases

ProteinModelPortalQ2N8X0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314225.ELI_08895.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC63871; ABC63871; ELI_08895.
GeneID3870181.
KEGGeli:ELI_08895.
PATRIC21860684. VBIEryLit102657_1765.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMAFHECARK.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycELIT314225:GHLE-1812-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_ERYLH
AccessionPrimary (citable) accession number: Q2N8X0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 57 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