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Q87ST5 (PDXA_VIBPA) 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:VP0337
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length332 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 – 3323324-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188834

Sites

Metal binding1681Divalent metal cation; shared with dimeric partner By similarity
Metal binding2131Divalent metal cation; shared with dimeric partner By similarity
Metal binding2691Divalent metal cation; shared with dimeric partner By similarity
Binding site1381Substrate By similarity
Binding site1391Substrate By similarity
Binding site2771Substrate By similarity
Binding site2861Substrate By similarity
Binding site2951Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87ST5 [UniParc].

Last modified May 30, 2003. Version 1.
Checksum: 614012482F81B45A

FASTA33236,067
        10         20         30         40         50         60 
MTTNSIRRIV VTAGEPAGIG PDLVLALSKE DWAHQIVVCA DKNMLLERAK MLGIDVQLFD 

        70         80         90        100        110        120 
YNPEEAPKAQ KAGTLIVDHV EIAENAIAGQ LNEANGHYVL KTLERAALGC MNDEFDAIVT 

       130        140        150        160        170        180 
GPVHKGVINR AGVAFSGHTE FFAEKSNTPL VVMMLATEGL RVALVTTHIP LAYVSKAVTE 

       190        200        210        220        230        240 
ERLEKIIDIL HKDLVEKFAI AEPNIYVCGL NPHAGEDGCL GREEIETITP TLEKIQKEKG 

       250        260        270        280        290        300 
IKLIGPLPAD TIFNEKYLND ADAVLGMYHD QVLPVLKYKG FGRSVNITLG LPFIRTSVDH 

       310        320        330 
GTALELAGTG QADTGSFRTA LTHAIELVEK KQ 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC58600.1.
RefSeqNP_796716.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87ST5.
SMRQ87ST5. Positions 5-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP0337.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC58600; BAC58600; BAC58600.
GeneID1187804.
KEGGvpa:VP0337.
PATRIC20138898. VBIVibPar50997_0324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycVPAR223926:GHK4-348-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...

Entry information

Entry namePDXA_VIBPA
AccessionPrimary (citable) accession number: Q87ST5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: May 30, 2003
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