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Q3V7R9 (PDXA_RHOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:RPA3065
OrganismRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [Complete proteome] [HAMAP]
Taxonomic identifier258594 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length337 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 – 3373374-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000051511

Sites

Metal binding1731Divalent metal cation; shared with dimeric partner By similarity
Metal binding2181Divalent metal cation; shared with dimeric partner By similarity
Metal binding2731Divalent metal cation; shared with dimeric partner By similarity
Binding site1391Substrate By similarity
Binding site1401Substrate By similarity
Binding site2811Substrate By similarity
Binding site2901Substrate By similarity
Binding site2991Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3V7R9 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 7C7AECA3938A5127

FASTA33734,927
        10         20         30         40         50         60 
MTGMAKPLAL TLGEPAGIGP DIALAAWLKR EQHGLPPFYL LGDAGCLSRC AKLLGLDVPL 

        70         80         90        100        110        120 
AEVKAEDAAA AFATTLPVVS TGQIATATPG QPDATSAPAA IASIEHAVAD VRSGRAAAVV 

       130        140        150        160        170        180 
TNPIAKSVLY QAGFHHPGHT EFLAELAKRD GIVPQPVMML WCPALAVVPV TIHVSLRDAI 

       190        200        210        220        230        240 
TQLTTDLIVS TARIVVKDLR ERLGIAQPRL ALAGLNPHAG EDGALGQEDR AVVAPAVAIL 

       250        260        270        280        290        300 
RREGVDARGP LPADTMFHAA ARKTYDCAIC MYHDQALIPI KTIAFDEGVN VTLGLPFIRT 

       310        320        330 
SPDHGTAFDI AGSGQANPSS LIAALKLAAQ MASAKTA 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris."
Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S.
Nat. Biotechnol. 22:55-61(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-98 / CGA009.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX572602 Genomic DNA. Translation: CAE28506.1.
RefSeqNP_948404.1. NC_005296.1.

3D structure databases

ProteinModelPortalQ3V7R9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING258594.RPA3065.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE28506; CAE28506; RPA3065.
GeneID2690551.
KEGGrpa:RPA3065.
PATRIC23290597. VBIRhoPal84835_3222.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK05312.

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_RHOPA
AccessionPrimary (citable) accession number: Q3V7R9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 11, 2005
Last modified: February 19, 2014
This is version 61 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