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B1ZAJ4 (PDXA_METPB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Mpop_3923
OrganismMethylobacterium populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001) [Complete proteome] [HAMAP]
Taxonomic identifier441620 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length349 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 – 3493494-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000128255

Sites

Metal binding1761Divalent metal cation; shared with dimeric partner By similarity
Metal binding2211Divalent metal cation; shared with dimeric partner By similarity
Metal binding2761Divalent metal cation; shared with dimeric partner By similarity
Binding site1411Substrate By similarity
Binding site1421Substrate By similarity
Binding site2841Substrate By similarity
Binding site2931Substrate By similarity
Binding site3021Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B1ZAJ4 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: A0EDF8D996F5D0DE

FASTA34936,690
        10         20         30         40         50         60 
MASDDRPLAL TLGDPSGIGP EIALAAWRLR GERGVPPFQL IGDPEFLEAT AYRLGLSVPV 

        70         80         90        100        110        120 
AEVEPDDAVE VFARALPVLP LPSGAKVSAT PGAPDSANAG AIVESITAAV DLVRSGAASA 

       130        140        150        160        170        180 
VVTNPIAKFV LTRVGFAHPG HTEFLAALAA REGREPPLPV MMLWSELLAV VPVTIHVALR 

       190        200        210        220        230        240 
RVPDLLTQEL VERTARIVHA DLRARFGLEA PRLVLSGLNP HAGESGTMGT EDRDVLAPAV 

       250        260        270        280        290        300 
AALRAEGIDI RGPLPADTLF HERARATYDV ALAPTHDQAL IPIKTLAFDE GVNVTLGLPF 

       310        320        330        340 
VRTSPDHGTA FDIAGKGVAK PDSLIAALRL AQRLAQRPAN NVTPFPVRA 

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium populi BJ001."
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., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Marx C., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-705 / NCIMB 13946 / BJ001.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001029 Genomic DNA. Translation: ACB82050.1.
RefSeqYP_001926585.1. NC_010725.1.

3D structure databases

ProteinModelPortalB1ZAJ4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING441620.Mpop_3923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB82050; ACB82050; Mpop_3923.
GeneID6312240.
KEGGmpo:Mpop_3923.
PATRIC22565112. VBIMetPop124700_3959.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.
ProtClustDBCLSK2331789.

Enzyme and pathway databases

BioCycMPOP441620:GHMI-3981-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_METPB
AccessionPrimary (citable) accession number: B1ZAJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 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