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Q9ZJ28 (PDXA_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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:jhp_1490
OrganismHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length307 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 – 3073074-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188810

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
Q9ZJ28 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 77C5FD2DD9A71A81

FASTA30733,706
        10         20         30         40         50         60 
MAKKKIAISC GDIQGVGLEL ILKSHKEVSA LCEPLYLVHS ELLERANQLL DNAYETKTLN 

        70         80         90        100        110        120 
AIAIDAPLPL LNSSTIGKVS TQSGAYSFES FKKACELADS KEVDGICTLP INKLAWQQAQ 

       130        140        150        160        170        180 
IPFVGHTDFL KQRYKDHQII MMLGCSKLFV GLFSDHVPLS AVSQLIQVKA LVKFLLAFQK 

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

       250        260        270        280        290        300 
KITPFYVSMS HDVGLAPLKA LYFDESINVS LNAPILRAST DHGTAFDIAY QNKANHKSYL 


NAIKYLA 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99 / ATCC 700824.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD07064.1.
PIRD71801.
RefSeqNP_224208.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZJ28.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85963.jhp1490.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD07064; AAD07064; jhp_1490.
GeneID889008.
KEGGhpj:jhp1490.
PATRIC20607880. VBIHelPyl98156_1618.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
KOK00097.
OMAISIKLAM.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-1530-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_HELPJ
AccessionPrimary (citable) accession number: Q9ZJ28
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 84 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