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P58718 (PDXA2_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:STM0163
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.2

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3273274-hydroxythreonine-4-phosphate dehydrogenase 2 HAMAP-Rule MF_00536
PRO_0000188828

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

Secondary structure

........................................................... 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P58718 [UniParc].

Last modified January 31, 2002. Version 1.
Checksum: 03BB6725F1896440

FASTA32735,065
        10         20         30         40         50         60 
METKTVAITM GDPAGIGPEI IVKALSEDGL NGAPLVVIGC LATLKRLQAK 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 
TARVETVIGI ADTFLKRVGY VKPRIAVAGV NPHAGENGLF GDEETRILTP AITDARAKGM 

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

       310        320 
TAFDIAWTGK AKSESMAVSI KLAMQLA 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"The structure of a putative 4-hydroxythreonine-4-phosphate dehydrogenase from Salmonella typhimurium."
Midwest center for structural genomics (MCSG)
Submitted (AUG-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL19127.1.
RefSeqNP_459168.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HI1X-ray2.30A/B1-327[»]
ProteinModelPortalP58718.
SMRP58718. Positions 2-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM0163.

Proteomic databases

PaxDbP58718.
PRIDEP58718.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL19127; AAL19127; STM0163.
GeneID1251681.
KEGGstm:STM0163.
PATRIC32378607. VBISalEnt20916_0173.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSENT99287:GCTI-162-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]
TIGRFAMsTIGR00557. pdxA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP58718.

Entry information

Entry namePDXA2_SALTY
AccessionPrimary (citable) accession number: P58718
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: February 19, 2014
This is version 84 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways