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Q5HTM4 (PDXA_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:CJE1374
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [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_1000051494

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
Q5HTM4 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: D7429A212F0FF89F

FASTA36441,381
        10         20         30         40         50         60 
MKKLAISIGD INGIGLEILV RSHEELSKIC TPFYFIHESL LDKASKLLNL KLFNAKIVAF 

        70         80         90        100        110        120 
KDGKDYEFNF VKKENSLEIY SFYLPLDFKV DENFEIKAGE IDTKSGLYGF 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 KGVYLPHPLV ADTAFTKTGL KNCNRLVAMY 

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


HSKA 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW35694.1.
RefSeqYP_179361.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HTM4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE1374.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW35694; AAW35694; CJE1374.
GeneID3231880.
KEGGcjr:CJE1374.
PATRIC20044548. VBICamJej134361_1391.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAINCWEED.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK03946.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-1401-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_CAMJR
AccessionPrimary (citable) accession number: Q5HTM4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 15, 2005
Last modified: February 19, 2014
This is version 59 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