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Q89MT9 (PDXA2_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. 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 2

EC=1.1.1.262
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase 2
Gene names
Name:pdxA2
Ordered Locus Names:bll4103
OrganismBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length345 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3453454-hydroxythreonine-4-phosphate dehydrogenase 2 HAMAP-Rule MF_00536
PRO_0000188799

Sites

Metal binding1821Divalent metal cation; shared with dimeric partner By similarity
Metal binding2271Divalent metal cation; shared with dimeric partner By similarity
Metal binding2821Divalent metal cation; shared with dimeric partner By similarity
Binding site1481Substrate By similarity
Binding site1491Substrate By similarity
Binding site2901Substrate By similarity
Binding site2991Substrate By similarity
Binding site3081Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89MT9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 2E6FCD4B37B3DDE4

FASTA34536,145
        10         20         30         40         50         60 
MANHAAKPLA LTLGEPAGIG PDITIAGWLR RRELNLPAFY LLGDEALIAR RAKTLDKTLG 

        70         80         90        100        110        120 
KALGAEIRIA SVSAHEAAAA FTEALPVVAT GERATAEPGQ PDASSAPAAL ASIRQAVADV 

       130        140        150        160        170        180 
RAGRAGAVVT NPIAKSVLYR AGFRHPGHTE FLAELAAKDG RVPQPVMMLW SPRLAVVPVT 

       190        200        210        220        230        240 
IHVSLRDALS QLTSELIVST VRIVATELKS RFGIARPRIA VSGLNPHAGE DGSLGHEEQT 

       250        260        270        280        290        300 
IIAPALKTLR NDGIDARGPL PADTMFHEAA RSSYDCAVCM YHDQALIPIK TVAFDDAVNV 

       310        320        330        340 
TLGLPFIRTS PDHGTAFDIA GTGKANPASL IAALELASRM AAAKT 

« Hide

References

[1]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000040 Genomic DNA. Translation: BAC49368.1.
RefSeqNP_770743.1. NC_004463.1.

3D structure databases

ProteinModelPortalQ89MT9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.bll4103.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC49368; BAC49368; BAC49368.
GeneID1049759.
KEGGbja:bll4103.
PATRIC21191712. VBIBraJap65052_4112.

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OrthoDBEOG6GN6ZC.
PhylomeDBQ89MT9.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-4129-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 namePDXA2_BRADU
AccessionPrimary (citable) accession number: Q89MT9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 79 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