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B4S6L0 (PDXA_PROA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:Paes_0718
OrganismProsthecochloris aestuarii (strain DSM 271 / SK 413) [Complete proteome] [HAMAP]
Taxonomic identifier290512 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris

Protein attributes

Sequence length338 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 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

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpyridoxal phosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-hydroxythreonine-4-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

NAD binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3383384-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000146492

Sites

Metal binding1721Divalent metal cation; shared with dimeric partner By similarity
Metal binding2171Divalent metal cation; shared with dimeric partner By similarity
Metal binding2711Divalent metal cation; shared with dimeric partner By similarity
Binding site1401Substrate By similarity
Binding site1411Substrate By similarity
Binding site2791Substrate By similarity
Binding site2881Substrate By similarity
Binding site2971Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4S6L0 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: B625A431436286D5

FASTA33836,521
        10         20         30         40         50         60 
MKTTAWTIGD IHGIGPEIIL KTFDESLRST GQPEEKPIVI GSAEALLYYS KRLGLSIDIR 

        70         80         90        100        110        120 
TIDAPEKAAA YPQGVLPVIS VGEPSSPLQP GTISAEAGRL SMLAIEKAAN LCLEGRCAAM 

       130        140        150        160        170        180 
VTAPIHKEAV ARAGYPHTGH TDFLADLCAT DNPTMLFRDP VSGLMVALAT IHVALHRVPE 

       190        200        210        220        230        240 
LIRSMDMSAF FSNLNRSLQS DFRIEQPRIA VLGLNPHASD GGVMGREEKE IILPCIDALA 

       250        260        270        280        290        300 
DRQNIEGPFA ADGFFGSGKY RNYDVTVAMY HDQGLLPFKV LAFDTGINVT LGLPLVRTSP 

       310        320        330 
DHGTSFDIAG QGRASHRSFS EAAKLAWEIA FNRLMEHS 

« Hide

References

[1]"Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271."
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., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 271 / SK 413.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001108 Genomic DNA. Translation: ACF45765.1.
RefSeqYP_002015412.1. NC_011059.1.

3D structure databases

ProteinModelPortalB4S6L0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290512.Paes_0718.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF45765; ACF45765; Paes_0718.
GeneID6459914.
KEGGpaa:Paes_0718.
PATRIC23041122. VBIProAes37017_0749.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMASIDIRTI.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycPAES290512:GHUT-742-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_PROA2
AccessionPrimary (citable) accession number: B4S6L0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 45 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