Skip Header

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

Q6F943 (PDXB_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. 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:ACIAD2667
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length355 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.

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 – 355355Erythronate-4-phosphate dehydrogenase HAMAP-Rule MF_01825
PRO_0000297429

Sites

Active site2061 By similarity
Active site2341 By similarity
Active site2511Proton donor By similarity
Binding site451Substrate By similarity
Binding site661Substrate By similarity
Binding site1461NAD By similarity
Binding site2291NAD By similarity
Binding site2541NAD; via amide nitrogen By similarity
Binding site2551Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6F943 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: CD56F8D95E2DBF3A

FASTA35539,464
        10         20         30         40         50         60 
MKIVADENLA FTDYFFSEFG EIQHRAGRLL TAHDVSDAEA LLVRSVTKVN QALIEHSQLK 

        70         80         90        100        110        120 
FVGSATIGTD HLDISALQQQ DILWSNAPGC NAQAVAEYVI TALYHLDSDV FERGQDFTLG 

       130        140        150        160        170        180 
IIGLGNVGRR LAKMAALLGW NVIGCDPFVQ LPDIHNLSFD DVLQKSDAIS VHVPLTHSGS 

       190        200        210        220        230        240 
HPTFHLFDQH AFASMPASTI LINSARGPVI EEQALIQDIY QTGRKVVLDV FEHEPVISEQ 

       250        260        270        280        290        300 
LLDVVNLVTP HIAGYSLEGK ARGTQMIYDA FCKVFGYEAS KKFETQLPVC EPFFQQQDLK 

       310        320        330        340        350 
QILKAHLRAI YDIAQDDHNL RACVKDGQVD QCAFDQLRKE YPLRREWAAH GGPVA 

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR543861 Genomic DNA. Translation: CAG69422.1.
RefSeqYP_047244.1. NC_005966.1.

3D structure databases

HSSPHSSP built from PDB template 1SC6 based on UniProtKB P0A9T0.
ProteinModelPortalQ6F943.
ModBaseSearch...

Protein-protein interaction databases

STRING62977.ACIAD2667.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG69422; CAG69422; ACIAD2667.
GeneID2878298.
KEGGaci:ACIAD2667.
PATRIC20742933. VBIAciSp98416_2407.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0111.
HOGENOMHOG000234432.
KOK03473.
OMASSAPGCN.
ProtClustDBCLSK707643.

Enzyme and pathway databases

BioCycASP62977:GJVV-2481-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. 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_ACIAD
AccessionPrimary (citable) accession number: Q6F943
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 19, 2004
Last modified: May 1, 2013
This is version 69 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