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Reviewed, UniProtKB/Swiss-Prot Q6F943 (PDXB_ACIAD)

Last modified June 16, 2009. Version 39. 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: ACIAD2667
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length355 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 – 355355Erythronate-4-phosphate dehydrogenase HAMAP 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
Q6F943-1 [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: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR543861 Genomic DNA. Translation: CAG69422.1.
RefSeqYP_047244.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2878298.
GenomeReviewsGene locus ACIAD2667 in contig CR543861_GR.
KEGGaci:ACIAD2667.
NMPDRfig|62977.3.peg.2437.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6F943.
OMAQ6F943. SAPGCNA.

Enzyme and pathway databases

BioCycASP62977:ACIAD2667-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_ACIAD
AccessionPrimary (citable) accession number: Q6F943
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 19, 2004
Last modified: June 16, 2009
This is version 39 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