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B2IDU5 (PDXA_BEII9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:Bind_3318
OrganismBeijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712) [Complete proteome] [HAMAP]
Taxonomic identifier395963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBeijerinckiaceaeBeijerinckia

Protein attributes

Sequence length337 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 – 3373374-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000128236

Sites

Metal binding1681Divalent metal cation; shared with dimeric partner By similarity
Metal binding2121Divalent metal cation; shared with dimeric partner By similarity
Metal binding2671Divalent metal cation; shared with dimeric partner By similarity
Binding site1381Substrate By similarity
Binding site1391Substrate By similarity
Binding site2751Substrate By similarity
Binding site2841Substrate By similarity
Binding site2931Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2IDU5 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 3321DC56A477BFA8

FASTA33735,408
        10         20         30         40         50         60 
MVMLDHPLAV TMGDPSGIGP EIIAKMYLRR PDKRNWIVVG DPLVMEHAIA NLGVAVQIRR 

        70         80         90        100        110        120 
IATVEEAGCE DGVLNVLASS SLATLPAVGR VSAVSGQAAY DAIVTAIGLA RQGTIRGIVT 

       130        140        150        160        170        180 
APIHKEALAA AGIHYPGHTE ILAEQGGAQH VAMMLANDEI RTVLVTIHCS LADAIRKADF 

       190        200        210        220        230        240 
PAQMQAIRLA HEGARALGIV QPRIAVAGLN PHAGEGGLFG DEEIRIITPA IAAARAEGID 

       250        260        270        280        290        300 
ATGPWPGDTV FMQARLGKFD VVVAQYHDQG LIPVKFMGLE KGVNITLGLP FVRTSPDHGT 

       310        320        330 
AFDIAGRGIA DSSSLETAFD YATRLKVPTP FFSGAMS 

« Hide

References

[1]"Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC 9039."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N. expand/collapse author list , Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9039 / DSM 1715 / NCIB 8712.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001016 Genomic DNA. Translation: ACB96877.1.
RefSeqYP_001834366.1. NC_010581.1.

3D structure databases

ProteinModelPortalB2IDU5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395963.Bind_3318.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB96877; ACB96877; Bind_3318.
GeneID6199731.
KEGGbid:Bind_3318.
PATRIC21089729. VBIBeiInd21058_3772.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMAADTLFHF.
OrthoDBEOG6GN6ZC.
ProtClustDBCLSK984533.

Enzyme and pathway databases

BioCycBIND395963:GJA7-3373-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_BEII9
AccessionPrimary (citable) accession number: B2IDU5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 43 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