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Q89ZK3 (PDXA_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:
4-hydroxythreonine-4-phosphate dehydrogenase

EC=1.1.1.262
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase
Gene names
Name:pdxA
Ordered Locus Names:BT_4374
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP) By similarity. HAMAP-Rule MF_00536

Catalytic activity

4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH. HAMAP-Rule MF_00536

Cofactor

Binds 1 divalent metal cation per subunit By similarity.

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. HAMAP-Rule MF_00536

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00536

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00536.

Miscellaneous

The active site is located at the dimer interface By similarity.

Sequence similarities

Belongs to the PdxA family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpyridoxal phosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-hydroxythreonine-4-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

NAD binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3643644-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000051491

Sites

Metal binding1691Divalent metal cation; shared with dimeric partner By similarity
Metal binding2141Divalent metal cation; shared with dimeric partner By similarity
Metal binding2691Divalent metal cation; shared with dimeric partner By similarity
Binding site1381Substrate By similarity
Binding site1391Substrate By similarity
Binding site2771Substrate By similarity
Binding site2861Substrate By similarity
Binding site2951Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89ZK3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: FD60351E6D30985A

FASTA36440,325
        10         20         30         40         50         60 
MEENKIRIGI TQGDINGVGY EVILKTFSDP TMLELCTPII YGSPKVAAYH RKALDVQANF 

        70         80         90        100        110        120 
SIVNTASEAG YNRLSVVNCT DDEVKVEFSK PDPEAGKAAL GALERAIEEY REGLIDVIVT 

       130        140        150        160        170        180 
APINKHTIQS EEFSFPGHTE YIEERLGNGN KSLMILMKND FRVALVTTHI PVREIATTIT 

       190        200        210        220        230        240 
KELIQEKLMI FHRCLKQDFG IGAPRIAVLS LNPHAGDGGL LGMEEQEIII PAMKEMEEKG 

       250        260        270        280        290        300 
IICYGPYAAD GFMGSGNYTH FDGILAMYHD QGLAPFKALA MEDGVNYTAG LPVVRTSPAH 

       310        320        330        340        350        360 
GTAYDIAGKG LASEDSFRQA IYVAIDVFRN RQREKAARVN PLRKQYYEKR DDSDKLKLDT 


VDED 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015928 Genomic DNA. Translation: AAO79479.1.
RefSeqNP_813285.1. NC_004663.1.

3D structure databases

ProteinModelPortalQ89ZK3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226186.BT_4374.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO79479; AAO79479; BT_4374.
GeneID1071722.
KEGGbth:BT_4374.
PATRIC21063810. VBIBacThe70966_4451.

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAKALAMED.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-4454-MONOMER.
UniPathwayUPA00244; UER00312.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
HAMAPMF_00536. PdxA.
InterProIPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view]
PfamPF04166. PdxA. 1 hit.
[Graphical view]
TIGRFAMsTIGR00557. pdxA. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDXA_BACTN
AccessionPrimary (citable) accession number: Q89ZK3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 73 of the entry and version 1 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