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A1K9J6 (PDXA_AZOSB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:azo2885
OrganismAzoarcus sp. (strain BH72) [Complete proteome] [HAMAP]
Taxonomic identifier62928 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzoarcus

Protein attributes

Sequence length330 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 – 3303304-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000051489

Sites

Metal binding1631Divalent metal cation; shared with dimeric partner By similarity
Metal binding2081Divalent metal cation; shared with dimeric partner By similarity
Metal binding2631Divalent metal cation; shared with dimeric partner By similarity
Binding site1331Substrate By similarity
Binding site1341Substrate By similarity
Binding site2711Substrate By similarity
Binding site2801Substrate By similarity
Binding site2891Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1K9J6 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 6479DC89D6006E5C

FASTA33033,928
        10         20         30         40         50         60 
MAALPVLAVT SGEPAGVGPE LCARLLARDW PARLVVLGDA DLIAARAAAV GSPIAVRHYS 

        70         80         90        100        110        120 
RGQAQAAGVL EVLHIPLAEP SDAGRLAVGN ARYVLALLDR ALAGCVGGEF AGMVTAPVHK 

       130        140        150        160        170        180 
GVICESGIAF SGHTEYLAEH TATPLVVMML VGGGMRVALA TTHLPLAAVS AAITRPVLEQ 

       190        200        210        220        230        240 
TLRILHADLV QRFGIAAPRI LVAGLNPHAG EGGHMGREEI EVITPVLDRL RAEGLQLVGP 

       250        260        270        280        290        300 
LPADTLFAPH TLAHGDAVLA MYHDQGLPVL KHASFGGGVN VTLGLPVIRT SVDHGTALDL 

       310        320        330 
AGSGRADPGS LYAAVELAVS MAEARARQPR 

« Hide

References

[1]"Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72."
Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S. expand/collapse author list , Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.
Nat. Biotechnol. 24:1385-1391(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BH72.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM406670 Genomic DNA. Translation: CAL95501.1.
RefSeqYP_934388.1. NC_008702.1.

3D structure databases

ProteinModelPortalA1K9J6.
SMRA1K9J6. Positions 7-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING62928.azo2885.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL95501; CAL95501; azo2885.
GeneID4609107.
KEGGazo:azo2885.
PATRIC21014192. VBIAzoSp26047_2925.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMAFHECARK.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

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_AZOSB
AccessionPrimary (citable) accession number: A1K9J6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 56 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