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Q1CR24 (PDXA_HELPH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:HPAG1_1531
OrganismHelicobacter pylori (strain HPAG1) [Complete proteome] [HAMAP]
Taxonomic identifier357544 [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_1000051504

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
Q1CR24 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 8DCBBA3ABAE3B4A5

FASTA30733,780
        10         20         30         40         50         60 
MAKKKIAISC GDIQGVGLEL ILKSHKEVSA FCEPLYLIDG ELLERANQLL HNAYETKTLN 

        70         80         90        100        110        120 
TLAIHSPLPL LNSSTIGKVS AQSGAYSFES FKKACELADD KEVDGVCTLP INKLAWQQAQ 

       130        140        150        160        170        180 
IPFVGHTDFL KQRYKDHQII MMLGCSKLFV GLFSDHVPLG AVSQLIQVKE LVKFLLAFQK 

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

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


NAIKYLA 

« Hide

References

[1]"The complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression."
Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HPAG1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000241 Genomic DNA. Translation: ABF85598.1.
RefSeqYP_628272.1. NC_008086.1.

3D structure databases

ProteinModelPortalQ1CR24.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357544.HPAG1_1531.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF85598; ABF85598; HPAG1_1531.
GeneID4098403.
KEGGhpa:HPAG1_1531.
PATRIC20604535. VBIHelPyl56048_1586.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAERLNTIH.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycHPYL357544:GH1F-1569-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_HELPH
AccessionPrimary (citable) accession number: Q1CR24
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: May 14, 2014
This is version 54 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