Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q1GI38 (PDXA_RUEST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:TM1040_0945
OrganismRuegeria sp. (strain TM1040) (Silicibacter sp.) [Complete proteome] [HAMAP]
Taxonomic identifier292414 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

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_1000051519

Sites

Metal binding1621Divalent metal cation; shared with dimeric partner By similarity
Metal binding2071Divalent metal cation; shared with dimeric partner By similarity
Metal binding2621Divalent metal cation; shared with dimeric partner By similarity
Binding site1321Substrate By similarity
Binding site1331Substrate By similarity
Binding site2701Substrate By similarity
Binding site2791Substrate By similarity
Binding site2881Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GI38 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 85584BAFB9B8E179

FASTA32634,339
        10         20         30         40         50         60 
MTGAPQVIAL SCGEPAGIGP EIAVAAWDQL RADCPFVWIG DPRHLPSSHP WQPVSAPAEA 

        70         80         90        100        110        120 
LQVSADALPV WPLEFAGNTT KGEADPQNAS GVIQSIKTGV ELVTSGKAAA LCTAPIHKKA 

       130        140        150        160        170        180 
LIDGAGFAYP GHTEFLAALG GVDHVVMMLA SAALRVVPAT IHIPLSAVPE VLTPDHLRRV 

       190        200        210        220        230        240 
ITLTDRGLRD QFGLTAPRIA VTGLNPHAGE GGAMGQEEGD WIEALIREMQ TEGYRLTGPH 

       250        260        270        280        290        300 
PADTLFHAAA RARYDAAIAM YHDQALIPIK TLDFDKGVNV TLGLPFIRTS PDHGTAFDIA 

       310        320 
GKGLANPSSL IEALRLAQTM AKTRQP 

« Hide

References

[1]"Complete sequence of chromosome of Silicibacter sp. TM1040."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F., Richardson P.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TM1040.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000377 Genomic DNA. Translation: ABF63678.1.
RefSeqYP_612940.1. NC_008044.1.

3D structure databases

ProteinModelPortalQ1GI38.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292414.TM1040_0945.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF63678; ABF63678; TM1040_0945.
GeneID4077339.
KEGGsit:TM1040_0945.
PATRIC23386010. VBIRueSp69653_1831.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK05312.

Enzyme and pathway databases

BioCycRSP292414:GHCT-962-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_RUEST
AccessionPrimary (citable) accession number: Q1GI38
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 65 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