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Q9PN58 (PDXA_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:Cj1239
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3643644-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188802

Sites

Metal binding1771Divalent metal cation; shared with dimeric partner By similarity
Metal binding2161Divalent metal cation; shared with dimeric partner By similarity
Metal binding3011Divalent metal cation; shared with dimeric partner By similarity
Binding site1481Substrate By similarity
Binding site1491Substrate By similarity
Binding site3091Substrate By similarity
Binding site3181Substrate By similarity
Binding site3271Substrate By similarity

Secondary structure

........................................................... 364
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9PN58 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: DDD26465821FFC3E

FASTA36441,387
        10         20         30         40         50         60 
MKKLAISIGD INSIGLEILV RSHEELSKIC TPFYFIHESL LNKALKLLNL KLFNAKIVAF 

        70         80         90        100        110        120 
KDDKDYEFNF IKKENSLEIY SFCLPLGFKV DENFEIQAGE IDAKSGLYGF LSFKAASYFV 

       130        140        150        160        170        180 
YEKHAHALLT LPIHKKAWED AGLKYKGHTD ALRDFFKKNA IMMLGCKELF VGLFSEHIPL 

       190        200        210        220        230        240 
AKVSKKITFK NLSIFLKDFY KETHFKKMGL LGFNPHAGDY GVIGGEEEKI MEKAIAFVNA 

       250        260        270        280        290        300 
FLHSKKDEKF FKKALKDENL QKELLLNFKG KGVYLPYPLV ADTAFTKTGL KNCNRLVAMY 

       310        320        330        340        350        360 
HDLALAPLKA LYFDKSINVS LNLPIIRVSV DHGTAFDKAY KNAKINTKSY FEAAKFAINL 


HSKA 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL35354.1.
PIRA81331.
RefSeqYP_002344630.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TSNX-ray2.63A/B/C/D1-364[»]
ProteinModelPortalQ9PN58.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9PN58. 2 interactions.
STRING192222.Cj1239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL35354; CAL35354; Cj1239.
GeneID905530.
KEGGcje:Cj1239.
PATRIC20059438. VBICamJej33762_1221.

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAPINKLAW.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK03946.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-1211-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]
ProtoNetSearch...

Entry information

Entry namePDXA_CAMJE
AccessionPrimary (citable) accession number: Q9PN58
Secondary accession number(s): Q0P917
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: February 19, 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways