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P58719 (PDXA_YERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:YPO0493, y3682, YP_3686
OrganismYersinia pestis [Reference proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length331 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 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.

Sequence caution

The sequence AAM87230.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAS63834.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3313314-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188841

Sites

Metal binding1671Divalent metal cation; shared with dimeric partner By similarity
Metal binding2121Divalent metal cation; shared with dimeric partner By similarity
Metal binding2671Divalent metal cation; shared with dimeric partner By similarity
Binding site1371Substrate By similarity
Binding site1381Substrate By similarity
Binding site2751Substrate By similarity
Binding site2841Substrate By similarity
Binding site2931Substrate By similarity

Secondary structure

.......................................................... 331
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P58719 [UniParc].

Last modified January 31, 2002. Version 1.
Checksum: 9E7675F0F7D64349

FASTA33135,270
        10         20         30         40         50         60 
MHNHNNRLVI TPGEPAGVGP DLAITLAQQD WPVELVVCAD PALLLARASQ LNLPLQLREY 

        70         80         90        100        110        120 
QADQPAIAQQ AGSLTILPVK TAVNVVPGKL DVGNSHYVVE TLAKACDGAI SGEFAALVTG 

       130        140        150        160        170        180 
PVQKSIINDA GIPFIGHTEF FADRSHCQRV VMMLATEELR VALATTHLPL LAVPGAITQA 

       190        200        210        220        230        240 
SLHEVITILD NDLKTKFGIT QPQIYVCGLN PHAGEGGHMG HEEIDTIIPA LNTLRQQGIN 

       250        260        270        280        290        300 
LIGPLPADTL FQPKYLQHAD AVLAMYHDQG LPVLKYQGFG RAVNITLGLP FIRTSVDHGT 

       310        320        330 
ALELAATGTA DVGSFITALN LAIKMINNSN E 

« Hide

References

[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM10+ / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590842 Genomic DNA. Translation: CAL19173.1.
AE009952 Genomic DNA. Translation: AAM87230.1. Different initiation.
AE017042 Genomic DNA. Translation: AAS63834.1. Different initiation.
PIRAC0061.
RefSeqNP_670979.1. NC_004088.1.
NP_994957.1. NC_005810.1.
YP_002345566.1. NC_003143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LXYX-ray1.70A1-331[»]
ProteinModelPortalP58719.
SMRP58719. Positions 7-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING214092.YPO0493.

Protocols and materials databases

DNASU1148629.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM87230; AAM87230; y3682.
AAS63834; AAS63834; YP_3686.
GeneID1148629.
1173338.
2764303.
KEGGype:YPO0493.
ypk:y3682.
ypm:YP_3686.

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK00232.

Enzyme and pathway databases

BioCycYPES214092:GKDD-489-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

EvolutionaryTraceP58719.

Entry information

Entry namePDXA_YERPE
AccessionPrimary (citable) accession number: P58719
Secondary accession number(s): Q0WJH2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: February 19, 2014
This is version 95 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