Skip Header

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

A8ADQ9 (PDXB_CITK8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:CKO_00466
OrganismCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) [Complete proteome] [HAMAP]
Taxonomic identifier290338 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter

Protein attributes

Sequence length378 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 MF_01825

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. HAMAP MF_01825

Subcellular location

Cytoplasm Potential HAMAP 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: UniProtKB-KW

   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

protein dimerization activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Erythronate-4-phosphate dehydrogenase HAMAP MF_01825
PRO_1000088414

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

Sequences

Sequence LengthMass (Da)Tools
A8ADQ9 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 92131F4B731A0B15

FASTA37841,017
        10         20         30         40         50         60 
MKILVDENMP YARELFSRLG EVKAVPGRPI PVAELDDADA LMVRSVTKVN EALLGGKSIK 

        70         80         90        100        110        120 
FVGTATAGTD HVDEAWLKQA GVGFSAAPGC NAIAVVEYVF SALLMLAERD GFALSDRTVG 

       130        140        150        160        170        180 
IVGVGNVGAR LQARLEALGI RTLLCDPPRA DRGDEGDFRS LDELVQEADI LTFHTPLYKE 

       190        200        210        220        230        240 
GPYKTLHLAD EALIGRLKPG TILINACRGP VVDNTALLAR LNAGQSLSVV LDVWEGEPDL 

       250        260        270        280        290        300 
NVALLEKIDI GTSHIAGYTL EGKARGTTQV FEAYSTFIGR AQKVALDTLL PAPEFGRITL 

       310        320        330        340        350        360 
HGPLDQPTLK RLAHLVYDVR RDDAPLRKVA GIPGEFDKLR KNYLERREWS SLYVMCDDAS 

       370 
AATLLHKLGF NAVHHPAH 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000822 Genomic DNA. Translation: ABV11622.1.
RefSeqYP_001452058.1. NC_009792.1.

3D structure databases

ProteinModelPortalA8ADQ9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8ADQ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5584431.
GenomeReviewsGene locus CKO_00466 in contig CP000822_GR.
KEGGcko:CKO_00466.
PATRIC20384322. VBICitKos71230_0392.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0111.
HOGENOMHBG289972.
OMASAPGCNA.
ProtClustDBPRK15438.

Family and domain databases

HAMAPMF_01825. PdxB.
[Tree]
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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
KOK03473.
PANTHERPTHR10996:SF4. Erythronate-4-P_DHase. 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. 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_CITK8
AccessionPrimary (citable) accession number: A8ADQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 35 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