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P58716 (PDXA2_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. 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 2

EC=1.1.1.262
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase 2
Gene names
Name:pdxA2
Ordered Locus Names:STY0185, t0168
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length327 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 – 3273274-hydroxythreonine-4-phosphate dehydrogenase 2 HAMAP-Rule MF_00536
PRO_0000188827

Sites

Metal binding1691Divalent metal cation; shared with dimeric partner By similarity
Metal binding2131Divalent metal cation; shared with dimeric partner By similarity
Metal binding2681Divalent metal cation; shared with dimeric partner By similarity
Binding site1391Substrate By similarity
Binding site1401Substrate By similarity
Binding site2761Substrate By similarity
Binding site2851Substrate By similarity
Binding site2941Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P58716 [UniParc].

Last modified January 31, 2002. Version 1.
Checksum: F7F563DEB5326FEB

FASTA32735,042
        10         20         30         40         50         60 
METKTVAITM GDPAGIGPEI IVKALSEDGL NGAPLVVIGC LATLKCLQAK GITPNVELRA 

        70         80         90        100        110        120 
IERVAEARFA PGIIHVIDEP LAQPEALEAG KVQAQAGDLA YRCVKRATEL ALRGDVQAIA 

       130        140        150        160        170        180 
TAPLNKEALH LAGHNYPGHT ELLATLTHSR DYAMVLYTDK LKVIHVSTHI ALRKFLDTLS 

       190        200        210        220        230        240 
TTRVETVIGI ADTFLKRVGY VKPRIAVAGV NPHAGENGLF GDEETRILTP AITDARAKGM 

       250        260        270        280        290        300 
DVYGPCPPDT VFLQAYEGQY DMVVAMYHDQ GHIPLKLLGF YDGVNITAGL PFIRTSADHG 

       310        320 
TAFDIAWTGK AKSESMAVSI KLAMQLA 

« Hide

References

[1]"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. expand/collapse author list , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.
[2]"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL513382 Genomic DNA. Translation: CAD01321.1.
AE014613 Genomic DNA. Translation: AAO67900.1.
RefSeqNP_454776.1. NC_003198.1.
NP_804051.1. NC_004631.1.

3D structure databases

ProteinModelPortalP58716.
SMRP58716. Positions 2-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220341.STY0185.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO67900; AAO67900; t0168.
CAD01321; CAD01321; CAD01321.
GeneID1246679.
PATRIC18538192. VBISalEnt120419_0188.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMAPINKLAW.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK03371.

Enzyme and pathway databases

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]
TIGRFAMsTIGR00557. pdxA. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDXA2_SALTI
AccessionPrimary (citable) accession number: P58716
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: April 16, 2014
This is version 87 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