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Q17ZN0 (PDXA_HELAH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:Hac_0032
OrganismHelicobacter acinonychis (strain Sheeba) [Complete proteome] [HAMAP]
Taxonomic identifier382638 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length310 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. Can use ions such as zinc, magnesium or cobalt 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3103104-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000051503

Sites

Metal binding1561Divalent metal cation; shared with dimeric partner By similarity
Metal binding1951Divalent metal cation; shared with dimeric partner By similarity
Metal binding2511Divalent metal cation; shared with dimeric partner By similarity
Binding site1261Substrate By similarity
Binding site1271Substrate By similarity
Binding site2591Substrate By similarity
Binding site2681Substrate By similarity
Binding site2771Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q17ZN0 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 3FBFB4E3817BF438

FASTA31034,293
        10         20         30         40         50         60 
MVKKKIAISC GDIQGIGLEL ILKSHKEVSV LCEPLYLIHS ELLGRANQLL TNAYEVKPLN 

        70         80         90        100        110        120 
AIAINSPLPS FNSSTIGKVS AQSGAYSFES FRKACELADD KEVDSICTMP INKLAWQQAQ 

       130        140        150        160        170        180 
IPFVGHTDFL KQRYKEHQII MMLGCPKLFV GLFSDHVPLR AVSQLIQVKA LVQFLLAFQK 

       190        200        210        220        230        240 
STQAQIIQVC GFNPHAGEEG LFGEEDEKIL KAIQESNQTL GFECFLGPLP ADSAFAPNKR 

       250        260        270        280        290        300 
QITPFYVSMS HDVGLAPLKA LYFDESINVS LNAPILRAST DHGTAFDIAY QNKANNKSYL 

       310 
NAIKYLSQRL 

« Hide

References

[1]"Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines."
Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.
PLoS Genet. 2:1097-1110(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sheeba.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260522 Genomic DNA. Translation: CAJ98896.1.
RefSeqYP_663895.1. NC_008229.1.

3D structure databases

ProteinModelPortalQ17ZN0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382638.Hac_0032.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ98896; CAJ98896; Hac_0032.
GeneID4176742.
KEGGhac:Hac_0032.
PATRIC20584000. VBIHelAci71660_0033.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAISIKLAM.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycHACI382638:GJAU-30-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_HELAH
AccessionPrimary (citable) accession number: Q17ZN0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 25, 2006
Last modified: May 14, 2014
This is version 57 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