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Reviewed, UniProtKB/Swiss-Prot A6VXM3 (PDXB_MARMS)

Last modified June 16, 2009. Version 19. 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: Mmwyl1_2280
OrganismMarinomonas sp. (strain MWYL1) [Complete proteome] [HAMAP]
Taxonomic identifier400668 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesMarinomonas

Protein attributes

Sequence length380 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 – 380380Erythronate-4-phosphate dehydrogenase HAMAP MF_01825
PRO_1000088422

Sites

Active site2071 By similarity
Active site2371 By similarity
Active site2541Proton donor By similarity
Binding site451Substrate By similarity
Binding site661Substrate By similarity
Binding site1461NAD By similarity
Binding site2321NAD By similarity
Binding site2571NAD; via amide nitrogen By similarity
Binding site2581Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A6VXM3-1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: BC0C7CB0DFDA8507

FASTA38041,881
        10         20         30         40         50         60 
MKIIADENMP NAKVLFSHLG DVELVNGRTL THEQVREADV LLVRSVTKVT KELLEGSSVR 

        70         80         90        100        110        120 
FVGSATIGVD HIDLDYLSKA NIGFSSAPGC NAEAVADYVF SALSHLYLTK KINWLSKKIG 

       130        140        150        160        170        180 
VIGYGNVGKT VYTRFANMGC QVHVYDPIRE KEGGSANFVS LDEILSCDVI SLHAPLTHTG 

       190        200        210        220        230        240 
SYPTKGMIGR KELAKLSAGV TIISAGRGGV IDESALFDRH KQLNGNLHLV LDVWDGEPAI 

       250        260        270        280        290        300 
NQKLIAIVDI ATPHIAGYSK QGREKGTWMV YQALCQYLAL DANVISKHDA ISAGWLSFVN 

       310        320        330        340        350        360 
VSAEEPQEEM LARSMHAIYD VSRDDIRLRF KYRENKEKNV FDWLRKHYVE RDEFNTCIIG 

       370        380 
VSSSDASNLM SAAGFSVDNK 

« Hide

References

[1]"Complete sequence of Marinomonas sp. MWYL1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000749 Genomic DNA. Translation: ABR71202.1.
RefSeqYP_001341137.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5365538.
GenomeReviewsGene locus Mmwyl1_2280 in contig CP000749_GR.
KEGGmmw:Mmwyl1_2280.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA6VXM3. 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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXB_MARMS
AccessionPrimary (citable) accession number: A6VXM3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: June 16, 2009
This is version 19 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