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Q83AR8 (PDXB_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:CBU_1812
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length366 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. HAMAP-Rule MF_01825

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_01825.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily.

Sequence caution

The sequence AAO91305.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-phosphoerythronate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

NAD binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 366366Erythronate-4-phosphate dehydrogenase HAMAP-Rule MF_01825
PRO_0000075974

Sites

Active site2081 By similarity
Active site2331 By similarity
Active site2501Proton donor By similarity
Binding site461Substrate By similarity
Binding site671Substrate By similarity
Binding site1471NAD By similarity
Binding site1751NAD; via carbonyl oxygen By similarity
Binding site2281NAD By similarity
Binding site2531NAD; via amide nitrogen By similarity
Binding site2541Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83AR8 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: FC5F34670DCF8C1F

FASTA36640,969
        10         20         30         40         50         60 
MIKILADDRI PFVSELFGDF GELILKPGAH IQNRDLLAVN ALLTRSITSV DSALLEGTAV 

        70         80         90        100        110        120 
EFVGSATAGF DHIDSTWLKK QSIHWAYAPG ANATAVAEYV LHCVAYLHKK NLLPRKSATA 

       130        140        150        160        170        180 
AIIGVGHVGC VVSDRLRKIG FTVFHNDPPR AQLEKDFISV PLASLANVDL VCLHTPLVKT 

       190        200        210        220        230        240 
GNFPTYHLID NRFLKMLKPG SVLLNAGRGA VIDNNALLQC DHVITCLDVW ENEPTVNLQL 

       250        260        270        280        290        300 
LEKTTIATPH IAGYSKQAKL RATLMIYDAF LKYFHLSDTR RFSELQQLQE TMTLNIQDGR 

       310        320        330        340        350        360 
NAEDILLTLF DPGRESQRMR ETLAENPDQF EYLRRHFPLR NEFSAIQLTP TPSALLRKEL 


DDWGFK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO91305.1. Different initiation.
RefSeqNP_820791.1. NC_002971.3.

3D structure databases

ProteinModelPortalQ83AR8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_1812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO91305; AAO91305; CBU_1812.
GeneID1209723.
KEGGcbu:CBU_1812.
PATRIC17932359. VBICoxBur82552_1798.

Phylogenomic databases

eggNOGCOG0111.
HOGENOMHOG000234432.
KOK03473.
OMASAPGCNA.
OrthoDBEOG6VXFC3.
ProtClustDBCLSK915047.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-1785-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]
PROSITEPS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXB_COXBU
AccessionPrimary (citable) accession number: Q83AR8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: February 19, 2014
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names