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Q164G2 (PDXA_ROSDO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:RD1_3123
OrganismRoseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans) [Complete proteome] [HAMAP]
Taxonomic identifier375451 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRoseobacter

Protein attributes

Sequence length326 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 – 3263264-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000051512

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 site1321Substrate By similarity
Binding site1331Substrate By similarity
Binding site2711Substrate By similarity
Binding site2801Substrate By similarity
Binding site2891Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q164G2 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 118B06B5980A5AE5

FASTA32633,952
        10         20         30         40         50         60 
MSPATAPVLI SCGEPAGIGP EIAVAAWDAL QGTIPLAWVG DPRHLPASTT FTAITHPRAV 

        70         80         90        100        110        120 
ADVPTGSLPV LVHDFAAPST PGHPDPANAQ GVIDVIAACV AWVQEGAAAA LCTAPIHKKA 

       130        140        150        160        170        180 
LIDGADFKHP GHTEYLQALA GGRSRAVMML ASDALRVVPT TIHIALEDVP RVLTPALLRE 

       190        200        210        220        230        240 
TITITHAALQ RQFGIQAPRI VVAGLNPHAG EGGAMGLEEQ DWIADVISAL AASGMNLRGP 

       250        260        270        280        290        300 
LPADTMFHAR AREGYDAAIA MYHDQALIPI KTLDFDRGVN VTLGLPFIRT SPDHGTAFDI 

       310        320 
AGKGIANPTS MIEAIKLAAH MAARHV 

« Hide

References

[1]"The complete genome sequence of Roseobacter denitrificans reveals a mixotrophic rather than photosynthetic metabolism."
Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K., O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T., Touchman J.W.
J. Bacteriol. 189:683-690(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33942 / OCh 114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000362 Genomic DNA. Translation: ABG32631.1.
RefSeqYP_683317.1. NC_008209.1.

3D structure databases

ProteinModelPortalQ164G2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING375451.RD1_3123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG32631; ABG32631; RD1_3123.
GeneID4198668.
KEGGrde:RD1_3123.
PATRIC23364221. VBIRosDen86677_2982.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMACAYHDQA.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK05312.

Enzyme and pathway databases

BioCycRDEN375451:GJIZ-2938-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_ROSDO
AccessionPrimary (citable) accession number: Q164G2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 25, 2006
Last modified: February 19, 2014
This is version 63 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