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Q89NF3 (PDXA1_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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 1

EC=1.1.1.262
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase 1
Gene names
Name:pdxA1
Ordered Locus Names:blr3887
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 1 HAMAP-Rule MF_00536
PRO_0000188798

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 site2951Substrate By similarity
Binding site3041Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89NF3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: C67EB244DD7470A2

FASTA34536,065
        10         20         30         40         50         60 
MTSRHLAITM GDPAGIGPEI IVKACLGLKG RIATGDLRLL IIGSGAALDG AKAALGTDVA 

        70         80         90        100        110        120 
IPQVSADDRE WPNLCYLQAD AEGDPIKPGV LSADGGRFAY KAIEQGVRLT QAGRTAAIVT 

       130        140        150        160        170        180 
APLNKEALNK AGYHFPGHTE MLAHLTGVRG SVMLLAHGNM RVSHVSTHVA LEDVPKRLTP 

       190        200        210        220        230        240 
ERLRMVIDLT NDALRRLGIA KPKIAVAALN PHAGEGGLFG RQDIDVSAPT IAKAVADGLD 

       250        260        270        280        290        300 
VIGPVPGDTI FVKLRAGQFD AAVAMYHDQG HIPVKLLGFQ VDPATGRWQE LSGVNITLGL 

       310        320        330        340 
PIIRTSVDHG TAFDIAGKGI ANEHSLIEAI DYAERLAAGA SASKS 

« 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: BAC49152.1.
RefSeqNP_770527.1. NC_004463.1.

3D structure databases

ProteinModelPortalQ89NF3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.blr3887.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC49152; BAC49152; BAC49152.
GeneID1053741.
KEGGbja:blr3887.
PATRIC21191273. VBIBraJap65052_3894.

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMAGTIDCID.
OrthoDBEOG6GN6ZC.
ProtClustDBCLSK911123.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-3911-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 namePDXA1_BRADU
AccessionPrimary (citable) accession number: Q89NF3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 75 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