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A6WQ07 (PDXB_SHEB8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. 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:
Erythronate-4-phosphate dehydrogenase

EC=1.1.1.290
Gene names
Name:pdxB
Ordered Locus Names:Shew185_2762
OrganismShewanella baltica (strain OS185) [Complete proteome] [HAMAP]
Taxonomic identifier402882 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate By similarity. HAMAP-Rule MF_01825

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01825

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_01825.

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_processpyridoxine 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 binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 376376Erythronate-4-phosphate dehydrogenase HAMAP-Rule MF_01825
PRO_1000070407

Sites

Active site2091 By similarity
Active site2381 By similarity
Active site2551Proton donor By similarity
Binding site451Substrate By similarity
Binding site671Substrate By similarity
Binding site1471NAD By similarity
Binding site2331NAD By similarity
Binding site2581NAD; via amide nitrogen By similarity
Binding site2591Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A6WQ07 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 464CCA52ACD27D03

FASTA37641,362
        10         20         30         40         50         60 
MKILVDENMP YVEPLFGDLG DIIPVNGRTL TAEQVRDADV LLVRSVTKVN AELLSGNNKL 

        70         80         90        100        110        120 
KFVGSATIGT DHVDLAYLAE RNIPFSNAPG CNATAVGEFA FIAMLELAQR FNSPLKGKVV 

       130        140        150        160        170        180 
GIVGAGNTGT ATAKCLQAYG IKVLLNDPIK AAEGDPRSFV SLDTITAQAD IISLHVPITR 

       190        200        210        220        230        240 
TGEHKTKHLF DEARLKALKP NTWLVNCCRG DVIDNQALIK VKRQRDDLKL VLDVWEGEPT 

       250        260        270        280        290        300 
PLPELVPLAE FATPHIAGYS LEGKARGTFM LYQKLCQLLN ITADKSLLDL LPTFNIKAVE 

       310        320        330        340        350        360 
LATAPNEKAL LQLARFVYDL RDDDKMFRNT FLNENGFDTM RKNHQHRREF SALALAYDGQ 

       370 
SEVDWLSNLG FSGVGQ 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS185."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS185.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000753 Genomic DNA. Translation: ABS08896.1.
RefSeqYP_001366959.1. NC_009665.1.

3D structure databases

ProteinModelPortalA6WQ07.
ModBaseSearch...

Protein-protein interaction databases

STRING402882.Shew185_2762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS08896; ABS08896; Shew185_2762.
GeneID5371620.
KEGGsbm:Shew185_2762.
PATRIC23462425. VBISheBal127872_2998.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0111.
HOGENOMHOG000234432.
KOK03473.
OMASSAPGCN.
ProtClustDBCLSK906984.

Enzyme and pathway databases

BioCycSBAL402882:GJ99-2843-MONOMER.
UniPathwayUPA00244; UER00310.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
HAMAPMF_01825. PdxB.
InterProIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR020921. Erythronate-4-P_DHase.
IPR024531. Erythronate-4-P_DHase_dimer.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR10996:SF4. PTHR10996:SF4. 1 hit.
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
PF11890. DUF3410. 1 hit.
[Graphical view]
PROSITEPS00065. D_2_HYDROXYACID_DH_1. False negative.
PS00670. D_2_HYDROXYACID_DH_2. False negative.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXB_SHEB8
AccessionPrimary (citable) accession number: A6WQ07
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families