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Q9CKG8 (PDXA_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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:PM1650
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length337 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 – 3373374-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188814

Sites

Metal binding1721Divalent metal cation; shared with dimeric partner By similarity
Metal binding2161Divalent metal cation; shared with dimeric partner By similarity
Metal binding2711Divalent metal cation; shared with dimeric partner By similarity
Binding site2791Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CKG8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 7D0955556B98D657

FASTA33737,033
        10         20         30         40         50         60 
MTKSTVALTL GDPAGIGPEL VAKLLAKQNI REKANIVLVA DKDELEKGME IAKAQFVYEE 

        70         80         90        100        110        120 
VSFHQLGQYE FKTGVPVLIS HKSSHPKPFE YGKVTEQSGV YILETLKVAL NLAKMGYVQA 

       130        140        150        160        170        180 
ICFAPLNKQA MHKGGLRYRD ELHWFAEQTD FNEFVCELNV VDDIWAARVT SHIPFKDIVP 

       190        200        210        220        230        240 
NLSIKGVFDC IHLLYRSLVQ AGVENPKIAV QALNPHGGEG GVFGDEEMTI IQPGMEQARK 

       250        260        270        280        290        300 
AGIDVYGPFP GDTTMREVER LKINGVVSMY HDQFSTALKI LGFERGVTVQ GGIPIPITTA 

       310        320        330 
NHGTAFDLHG KNIAIPTAFE AAFNIAVRMG QGVLNQK 

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004439 Genomic DNA. Translation: AAK03734.1.
RefSeqNP_246589.1. NC_002663.1.

3D structure databases

ProteinModelPortalQ9CKG8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM1650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK03734; AAK03734; PM1650.
GeneID1244997.
KEGGpmu:PM1650.
PATRIC22872591. VBIPasMul88067_1669.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMAINPHSGD.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK00232.

Enzyme and pathway databases

BioCycPMUL272843:GC8W-1712-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_PASMU
AccessionPrimary (citable) accession number: Q9CKG8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: June 1, 2001
Last modified: February 19, 2014
This is version 74 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