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Reviewed, UniProtKB/Swiss-Prot A7ZPD6 (PDXB_ECO24)

Last modified June 16, 2009. Version 17. 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

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Names and origin

Protein namesRecommended name:
    Erythronate-4-phosphate dehydrogenase
    EC=1.1.1.290
Gene names
Name: pdxB
Ordered Locus Names: EcE24377A_2614
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Erythronate-4-phosphate dehydrogenase HAMAP MF_01825
PRO_1000088417

Sites

Active site2081 By similarity
Active site2371 By similarity
Active site2541Proton donor By similarity
Binding site451Substrate By similarity
Binding site661Substrate By similarity
Binding site1461NAD By similarity
Binding site1751NAD; via carbonyl oxygen By similarity
Binding site2321NAD By similarity
Binding site2571NAD; via amide nitrogen By similarity
Binding site2581Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
A7ZPD6-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 9962833F8972D301

FASTA37841,516
        10         20         30         40         50         60 
MKILVDENMP YARELFSRLG EVKAVPGRPI PVVQLDDADA LMVRSVTKVN ESLLAGKPIK 

        70         80         90        100        110        120 
FVGTATAGTD HVDEVWLKQA GIGFSAAPGC NAIAVVEYVF SSLLMLAERD GFSLHERTVG 

       130        140        150        160        170        180 
IVGVGNVGRR LQARLEVLGI KTLLCDPPRA DRGDEGDFRS LDELVQHADI LTFHTPLFKD 

       190        200        210        220        230        240 
GPYKTLHLAD EKLIRSLKPG AILINACRGA VVDNTALLTC LNEGQKLSVV LDVWEGEPEL 

       250        260        270        280        290        300 
NVELLKKVDI GTPHIAGYTL EGKARGTTQV FEAYSKFIGH EQHVALDTLL PAPEFGRITL 

       310        320        330        340        350        360 
HGPLDQPTLK RLVHLVYDVR RDDAPLRKVA GIPGEFDKLR KNYLERREWS SLYVICDDAS 

       370 
AASLLCKLGF NAVHHPAR

« Hide

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References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000800 Genomic DNA. Translation: ABV21185.1.
RefSeqYP_001463665.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5590697.
GenomeReviewsGene locus EcE24377A_2614 in contig CP000800_GR.
KEGGecw:EcE24377A_2614.
NMPDRfig|331111.3.peg.351.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA7ZPD6. SAPGCNA.

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...

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Entry information

Entry namePDXB_ECO24
AccessionPrimary (citable) accession number: A7ZPD6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: June 16, 2009
This is version 17 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)

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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