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Reviewed, UniProtKB/Swiss-Prot A3M810 (PDXB_ACIBT)

Last modified June 16, 2009. Version 21. 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: A1S_2637
OrganismAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]
Taxonomic identifier400667 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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Protein attributes

Sequence length355 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 – 355355Erythronate-4-phosphate dehydrogenase HAMAP MF_01825
PRO_0000297428

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

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Sequences

Sequence LengthMass (Da)Tools
A3M810-1 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 1492C13A920EEBF3

FASTA35539,488
        10         20         30         40         50         60 
MKIVADENLA FTDYFFSEFG DIQHKAGRTL THTDVQDAEA LLVRSVTAVN ESLIQNTALK 

        70         80         90        100        110        120 
YVGSATIGTD HLDIQALEKQ GITWANAAGC NAQAVAEYVI TALLHLDASL LEQQEKFTLG 

       130        140        150        160        170        180 
IVGLGNVGKR LAYMAQLLGW KVIGFDPFVQ LDSIENVSFQ TLLQQANAVS IHVPLTKKGE 

       190        200        210        220        230        240 
HATYHLFDEK AFAALQPNTI LINSARGPVV KEAALIEDIQ RTQRKVVLDV FEHEPVISEE 

       250        260        270        280        290        300 
LLNMLALATP HIAGYSLEGK ARGTQMIYEA FCQKFGYDIN KRFETQLPAC EDYFSRHDLK 

       310        320        330        340        350 
AVLKQKISQI YDIAQDDANI RACVKEGKVE QKAFDLLRKN YPLRREWAAH GGPQA

« Hide

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References

[1]"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000521 Genomic DNA. Translation: ABO13054.2.
RefSeqYP_001085656.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4920180.
GenomeReviewsGene locus A1S_2637 in contig CP000521_GR.
KEGGacb:A1S_2637.
NMPDRfig|400667.4.peg.2741.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_01825.
[Tree]
InterProIPR006139. D-isomer_2_OHA_DH.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
[Graphical view]
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. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePDXB_ACIBT
AccessionPrimary (citable) accession number: A3M810
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: June 16, 2009
This is version 21 of the entry and version 2 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