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B7KYJ1 (PDXA_METC4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Mchl_3930
OrganismMethylobacterium extorquens (strain CM4 / NCIMB 13688) (Methylobacterium chloromethanicum) [Complete proteome] [HAMAP]
Taxonomic identifier440085 [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_1000146490

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
B7KYJ1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 5C41DBDAFDF48A06

FASTA34936,842
        10         20         30         40         50         60 
MASDDRPLAL TLGDPSGIGP EIALAAWQLR SERGVPPFQL IGDPEFLEAT AYRLGLSVPV 

        70         80         90        100        110        120 
AEVEPDDACE VFPRALPVLP LPSGAKVIAT PGAPDSANAG AIVESITAAV DLVRSGAASA 

       130        140        150        160        170        180 
VVTNPIAKFV LTRVGFAHPG HTEFLAALAA REGREPSLPV MMIWSDTLAV VPVTIHVALR 

       190        200        210        220        230        240 
RVPELLTQDL VERTARIVHA DLRARFGLEH PRLVLSGLNP HAGESGTMGT EDRDVLAPAV 

       250        260        270        280        290        300 
AVLRSEGIDI RGPLPADTLF HERARATYDV ALTPTHDQAL IPVKTLAFDE GVNVTLGLPF 

       310        320        330        340 
VRTSPDHGTA FDIAGKGLAK PDSLIAALRL AHRLAHRPAD TVLPFPARA 

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium chloromethanicum CM4."
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., Mikhailova N., Marx C., Richardson P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CM4 / NCIMB 13688.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001298 Genomic DNA. Translation: ACK84742.1.
RefSeqYP_002422670.1. NC_011757.1.

3D structure databases

ProteinModelPortalB7KYJ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING440085.Mchl_3930.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK84742; ACK84742; Mchl_3930.
GeneID7117128.
KEGGmch:Mchl_3930.
PATRIC22502156. VBIMetChl132133_3898.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMCHL440085:GCXT-3994-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_METC4
AccessionPrimary (citable) accession number: B7KYJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: February 19, 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