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C0QTA7 (PDXA_PERMH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. 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:PERMA_0123
OrganismPersephonella marina (strain DSM 14350 / EX-H1) [Complete proteome] [HAMAP]
Taxonomic identifier123214 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesHydrogenothermaceaePersephonella

Protein attributes

Sequence length319 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
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 – 3193194-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000146491

Sites

Metal binding1591Divalent metal cation; shared with dimeric partner By similarity
Metal binding2041Divalent metal cation; shared with dimeric partner By similarity
Metal binding2571Divalent metal cation; shared with dimeric partner By similarity
Binding site1291Substrate By similarity
Binding site1301Substrate By similarity
Binding site2651Substrate By similarity
Binding site2741Substrate By similarity
Binding site2831Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
C0QTA7 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 547F5F5A236D08C2

FASTA31935,461
        10         20         30         40         50         60 
MKKIGITLGD PSGISPEILI KSIDKLKKAI YVIYGSYKII EKVSSILDKK TEINIIDSPE 

        70         80         90        100        110        120 
EAEKEGVYLI NVYDRDFCVG KPDKETGKAS VLFLERAVKD ILSKKLDAIV TLPISKEYVM 

       130        140        150        160        170        180 
KAGFRYAGHT DYLADITKTE DYLMMLLCEK MKVALVTTHI PLKDVPENIK PEILESKIRL 

       190        200        210        220        230        240 
LNRELQSKFG IKKPKIAVLG LNPHAGDGGN IGREEIDIIN PVVQKLKSEG IDLEGSLSAD 

       250        260        270        280        290        300 
TAFNRYREFD AYLAMYHDQG LIPLKLLCFK KAVNITLGIP FIRTSPDHGT GFDIAGKGIA 

       310 
DPSSFIEAVK LALKLSKQY 

« Hide

References

[1]"Complete and draft genome sequences of six members of the Aquificales."
Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.
J. Bacteriol. 191:1992-1993(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14350 / EX-H1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001230 Genomic DNA. Translation: ACO03563.1.
RefSeqYP_002729922.1. NC_012440.1.

3D structure databases

ProteinModelPortalC0QTA7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING123214.PERMA_0123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO03563; ACO03563; PERMA_0123.
GeneID7675488.
KEGGpmx:PERMA_0123.
PATRIC22913725. VBIPerMar119911_0182.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAINPHSGD.
OrthoDBEOG6GN6ZC.
ProtClustDBCLSK2479599.

Enzyme and pathway databases

BioCycPMAR123214:GIZP-124-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_PERMH
AccessionPrimary (citable) accession number: C0QTA7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: February 19, 2014
This is version 38 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