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Q15QB2 (PDXA_PSEA6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:Patl_3420
OrganismPseudoalteromonas atlantica (strain T6c / ATCC BAA-1087) [Complete proteome] [HAMAP]
Taxonomic identifier342610 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length326 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 – 3263264-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000128257

Sites

Metal binding1631Divalent metal cation; shared with dimeric partner By similarity
Metal binding2081Divalent metal cation; shared with dimeric partner By similarity
Metal binding2631Divalent metal cation; shared with dimeric partner By similarity
Binding site1331Substrate By similarity
Binding site1341Substrate By similarity
Binding site2711Substrate By similarity
Binding site2801Substrate By similarity
Binding site2891Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q15QB2 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 65BD0237F78722A7

FASTA32635,063
        10         20         30         40         50         60 
MTIKLAITPG EPAGVGPDLI ITLAQQQWQA MLVVFANAEL MRTRANELNI PLTLLPYDAS 

        70         80         90        100        110        120 
RTDIQPAGSL YIVDIPLQDE VIAGKLNPTN SQYVLDTLHQ ACQMNLNGEF QALVTGPVHK 

       130        140        150        160        170        180 
GVINEAGIPF SGHTEFFAQQ SNTPEVVMML ATEGLRVTLA TTHIPVTAVS AAITQPKLDN 

       190        200        210        220        230        240 
VIRIIDHDLR TKFGIAKPHI FVCGLNPHAG EDGHIGREEI DTIIPALNAL RQEGITLTGP 

       250        260        270        280        290        300 
LPADTIFNPK YLQQADTVLA MYHDQGLPVL KYKGFSQAVN ITLGLPFIRT SVDHGTALDL 

       310        320 
AATGQADVGS FSIAIKEAIS LAKSTQ 

« Hide

References

[1]"Complete sequence of Pseudoalteromonas atlantica T6c."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T6c / ATCC BAA-1087.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000388 Genomic DNA. Translation: ABG41926.1.
RefSeqYP_662980.1. NC_008228.1.

3D structure databases

ProteinModelPortalQ15QB2.
SMRQ15QB2. Positions 2-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342610.Patl_3420.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG41926; ABG41926; Patl_3420.
GeneID4175197.
KEGGpat:Patl_3420.
PATRIC23052164. VBIPseAtl25434_3635.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycPATL342610:GHGT-3489-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_PSEA6
AccessionPrimary (citable) accession number: Q15QB2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 25, 2006
Last modified: May 14, 2014
This is version 65 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