Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q7VRU9 (PDXB_BLOFL)

Last modified June 16, 2009. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Erythronate-4-phosphate dehydrogenase
    EC=1.1.1.290
Gene names
Name: pdxB
Ordered Locus Names: Bfl497
OrganismBlochmannia floridanus [Complete proteome] [HAMAP]
Taxonomic identifier203907 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeant endosymbiontsCandidatus Blochmannia

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate By similarity.

Catalytic activity

4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH. HAMAP MF_01825

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5. HAMAP MF_01825

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

pyridoxine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function4-phosphoerythronate dehydrogenase activity

Inferred from electronic annotation. Source: EC

NAD or NADH binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Erythronate-4-phosphate dehydrogenase HAMAP MF_01825
PRO_0000075973

Sites

Active site2091 By similarity
Active site2381 By similarity
Active site2551Proton donor By similarity
Binding site451Substrate By similarity
Binding site661Substrate By similarity
Binding site1461NAD By similarity
Binding site2331NAD By similarity
Binding site2581NAD; via amide nitrogen By similarity
Binding site2591Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VRU9-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 1DB671FF109F5486

FASTA37242,534
        10         20         30         40         50         60 
MRILADQAIP YVYKLFGSDN YVQVCDGRSI SANMLKDVDV LIIRSITKVN HMLLYDSSIK 

        70         80         90        100        110        120 
FIGTVTSGVD HIDQNYLKNN NIRCVSTPGS NAVSVVEYVC ATLFWLAQRD CFFLRDKTVG 

       130        140        150        160        170        180 
IIGVGNIGNL LYQRLNSLGV HTLLYDPYKS KCDTDRMSWK SLDILVSKSD ILTLHVPLTY 

       190        200        210        220        230        240 
TGAYPTWHMI NKDILDALPS NSILINTSRG AVVNNDDLLA ILRCGKKINV ILDVWESEPK 

       250        260        270        280        290        300 
LSLPLLSYVD IGTAHIAGYS FESRIRSIKK IYDDYCDYFN VKNKVNWISL GLSDIRYIAV 

       310        320        330        340        350        360 
SRLDECIINR LIQLVYNVYY DHIALKNNVL RLRGFDKLRE YYCFRREWSS LLVDSKNGYN 

       370 
NDILFKFGFS TL 

« Hide

References

[1]"The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes."
Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., van Ham R.C.H.J., Gross R., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003) [PubMed: 12886019] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

BX248583 Genomic DNA. Translation: CAD83186.1.
RefSeqNP_878780.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1499697.
GenomeReviewsGene locus Bfl497 in contig BX248583_GR.
KEGGbfl:Bfl497.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7VRU9.
OMAQ7VRU9. SAPGCNA.

Enzyme and pathway databases

BioCycCBLO203907:BFL497-MON.

Family and domain databases

HAMAPMF_01825.
[Tree]
InterProIPR006139. D-isomer_2_OHA_DH.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. False negative.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXB_BLOFL
AccessionPrimary (citable) accession number: Q7VRU9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents