Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3IFD2 (PDXA_PSEHT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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:PSHAa2634
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length330 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 – 3303304-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000128258

Sites

Metal binding1641Divalent metal cation; shared with dimeric partner By similarity
Metal binding2091Divalent metal cation; shared with dimeric partner By similarity
Metal binding2641Divalent metal cation; shared with dimeric partner By similarity
Binding site1341Substrate By similarity
Binding site1351Substrate By similarity
Binding site2721Substrate By similarity
Binding site2811Substrate By similarity
Binding site2901Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3IFD2 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: FF12BF416F5F8AFF

FASTA33035,458
        10         20         30         40         50         60 
MTLRIAITPG EPAGIGPDLL LKLAQQTWDA QLVAIADANM LKQRAKHLGL SIKLIEFDQH 

        70         80         90        100        110        120 
AAATPAPAGS LYLHQVDVAE PVELGVLNDA NGQYVLDTLR IASEKNMDGT FAAVVTGPVH 

       130        140        150        160        170        180 
KGIINKAGIS FSGHTEYFAQ QSNTADVVMM LATQGLRVAL VTTHIPLAYV SRAITEDRLI 

       190        200        210        220        230        240 
KVASILNHDL QTKFGIEKPR ILVCGLNPHA GEDGHLGREE IDTIIPTLEI LNNQGMNLIG 

       250        260        270        280        290        300 
PLPADTLFQD KYLNEADAVL AMYHDQGLPV LKYKGFGNSV NITLGLPFIR TSVDHGTALD 

       310        320        330 
LAGKGTADVG SFELAIREAI KLAQEKAQNQ 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TAC 125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954246 Genomic DNA. Translation: CAI87682.1.
RefSeqYP_341124.1. NC_007481.1.

3D structure databases

ProteinModelPortalQ3IFD2.
SMRQ3IFD2. Positions 2-322.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326442.PSHAa2634.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI87682; CAI87682; PSHAa2634.
GeneID3709962.
KEGGpha:PSHAa2634.
PATRIC32298853. VBIPseHal105694_2544.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycPHAL326442:GJIU-2689-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_PSEHT
AccessionPrimary (citable) accession number: Q3IFD2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 8, 2005
Last modified: February 19, 2014
This is version 64 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