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B8FEI1 (PDXA_DESAA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:Dalk_5293
OrganismDesulfatibacillum alkenivorans (strain AK-01) [Complete proteome] [HAMAP]
Taxonomic identifier439235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfatibacillum

Protein attributes

Sequence length333 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 – 3333334-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000211911

Sites

Metal binding1701Divalent 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 site1401Substrate By similarity
Binding site1411Substrate By similarity
Binding site2781Substrate By similarity
Binding site2871Substrate By similarity
Binding site2961Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B8FEI1 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: F442039774E6B81D

FASTA33336,026
        10         20         30         40         50         60 
MKSLPIIGIT MGDPVGVGPE IIVKTLKNKD IYKICRPLVI GDLKVMEQAE SLIRSGLDFR 

        70         80         90        100        110        120 
PAGSPEDAAY EYGRVDILPV SDLDPARLAP KTPCAKTGEA MVKYITTAVD YARDNRIQAV 

       130        140        150        160        170        180 
TTGPIQKAAV HAAGYTFAGH TELLAQRTGT SKYVMMLAGD KLRVVLVTIH MAVSEIPAHV 

       190        200        210        220        230        240 
TREKFIETVE VTGQALKERF GIPQPKMAVA ALNPHAGEEG AFGTEERDVI IPAMEHFKGS 

       250        260        270        280        290        300 
DIALDGPWPA DTLFYHAQQG KWDAVVCMYH DQGLIPFKMI HFHDGVNTTL GLPIIRTSVD 

       310        320        330 
HGTAYDLAGT GKADHGSMEA AIRMAALQAS NLK 

« Hide

References

[1]"Complete sequence of Desulfatibacillum alkenivorans AK-01."
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., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Wawrik B., Richardson P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AK-01.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001322 Genomic DNA. Translation: ACL06962.1.
RefSeqYP_002434430.1. NC_011768.1.

3D structure databases

ProteinModelPortalB8FEI1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439235.Dalk_5293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL06962; ACL06962; Dalk_5293.
GeneID7169266.
KEGGdal:Dalk_5293.
PATRIC21657548. VBIDesAlk8144_5592.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMAISIKLAM.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycDALK439235:GHP2-5359-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_DESAA
AccessionPrimary (citable) accession number: B8FEI1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 38 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