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A1W0M2 (PDXA_CAMJJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:CJJ81176_1253
OrganismCampylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) [Complete proteome] [HAMAP]
Taxonomic identifier354242 [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_1000051493

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
A1W0M2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: C763D460320EFD2E

FASTA36441,333
        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 ADTAFTKAGL KNCNRLVAMY 

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


NSKA 

« Hide

References

[1]Fouts D.E., Nelson K.E., Sebastian Y.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 81-176.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000538 Genomic DNA. Translation: EAQ72898.1.
RefSeqYP_001000913.1. NC_008787.1.

3D structure databases

ProteinModelPortalA1W0M2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING354242.CJJ81176_1253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEAQ72898; EAQ72898; CJJ81176_1253.
GeneID4682344.
KEGGcjj:CJJ81176_1253.
PATRIC20052483. VBICamJej103413_1253.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCJEJ354242:GC51-1230-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_CAMJJ
AccessionPrimary (citable) accession number: A1W0M2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 53 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