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B3E252 (PDXA_GEOLS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:Glov_3452
OrganismGeobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) [Complete proteome] [HAMAP]
Taxonomic identifier398767 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

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_1000128250

Sites

Metal binding1721Divalent metal cation; shared with dimeric partner By similarity
Metal binding2171Divalent metal cation; shared with dimeric partner By similarity
Metal binding2741Divalent metal cation; shared with dimeric partner By similarity
Binding site1421Substrate By similarity
Binding site1431Substrate By similarity
Binding site2821Substrate By similarity
Binding site2911Substrate By similarity
Binding site3001Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B3E252 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: B31782D52694E307

FASTA33635,378
        10         20         30         40         50         60 
MNTPKPQIAI TMGDPCGVGP EIIVAALSDP AIRSACKPLV LGDRRAMQRA LTVCNSPLEL 

        70         80         90        100        110        120 
ITVSSPAEAA DLPDSVIPLL ELSSLANTDI DYGKPSELSG DAVYRYIRRA AELCLTGEVA 

       130        140        150        160        170        180 
AMATAPISKE AMHRAGHHYP GHTELLAELC RCDEFVMMLA GDVLRVALVT IHEALAHVPA 

       190        200        210        220        230        240 
LISTEQVLKT IRVTANGVAP LCGNRSPRIA VLALNPHCGE GGMFGSEEAD AIIPAITAAQ 

       250        260        270        280        290        300 
SEGLDVAGPF SADTFFHFAV QEPAPYDAVV AMYHDQGLIP LKMRHFDDGI NITLGLPIIR 

       310        320        330 
TSVDHGTAYN LAGTGTASAT SMKASIRIAA KLAATR 

« Hide

References

[1]"Complete sequence of chromosome of Geobacter lovleyi SZ."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1151 / DSM 17278 / SZ.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001089 Genomic DNA. Translation: ACD97155.1.
RefSeqYP_001953675.1. NC_010814.1.

3D structure databases

ProteinModelPortalB3E252.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398767.Glov_3452.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD97155; ACD97155; Glov_3452.
GeneID6366788.
KEGGglo:Glov_3452.
PATRIC21998571. VBIGeoLov31523_3374.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMAISIKLAM.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycGLOV398767:GH32-3504-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_GEOLS
AccessionPrimary (citable) accession number: B3E252
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 22, 2008
Last modified: May 14, 2014
This is version 46 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