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A8FMU4 (PDXA_CAMJ8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:C8J_1182
OrganismCampylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) [Complete proteome] [HAMAP]
Taxonomic identifier407148 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length364 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 – 3643644-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000072540

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

Sequences

Sequence LengthMass (Da)Tools
A8FMU4 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: C399C46022E70AF7

FASTA36441,315
        10         20         30         40         50         60 
MKKLAISIGD INGIGLEILV RSHEELSKIC TPFYFIHENL LNKASKLLNL KLFNAKIVAF 

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

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

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

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

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


SLKT 

« Hide

References

[1]"The complete genome sequence of Campylobacter jejuni strain 81116 (NCTC11828)."
Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M., van Vliet A.H.M.
J. Bacteriol. 189:8402-8403(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 81116 / NCTC 11828.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000814 Genomic DNA. Translation: ABV52781.1.
RefSeqYP_001482758.1. NC_009839.1.

3D structure databases

ProteinModelPortalA8FMU4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING407148.C8J_1182.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV52781; ABV52781; C8J_1182.
GeneID5618490.
KEGGcju:C8J_1182.
PATRIC20055998. VBICamJej119085_1192.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAAIGTEDE.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycCJEJ407148:GHCS-1218-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_CAMJ8
AccessionPrimary (citable) accession number: A8FMU4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: November 13, 2007
Last modified: May 14, 2014
This is version 46 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