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Q9I5U4 (PDXA1_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. 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 1

EC=1.1.1.262
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase 1
Gene names
Name:pdxA1
Ordered Locus Names:PA0593
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length328 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 probably use ions such as zinc, magnesium or cobalt. Ref.2

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 – 3283284-hydroxythreonine-4-phosphate dehydrogenase 1 HAMAP-Rule MF_00536
PRO_0000188815

Sites

Metal binding1651Divalent metal cation; shared with dimeric partner
Metal binding2101Divalent metal cation; shared with dimeric partner
Metal binding2651Divalent metal cation; shared with dimeric partner
Binding site1351Substrate By similarity
Binding site1361Substrate By similarity
Binding site2731Substrate By similarity
Binding site2821Substrate By similarity
Binding site2911Substrate By similarity

Secondary structure

........................................................... 328
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9I5U4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 2C666738F21D7B8C

FASTA32834,923
        10         20         30         40         50         60 
MSLRFALTPG EPAGIGPDLC LLLARSAQPH PLIAIASRTL LQERAGQLGL AIDLKDVSPA 

        70         80         90        100        110        120 
AWPERPAKAG QLYVWDTPLA APVRPGQLDR ANAAYVLETL TRAGQGCLDG HFAGMITAPV 

       130        140        150        160        170        180 
HKGVINEAGI PFSGHTEFLA DLTHTAQVVM MLATRGLRVA LATTHLPLRE VADAISDERL 

       190        200        210        220        230        240 
TRVARILHAD LRDKFGIAHP RILVCGLNPH AGEGGHLGRE EIEVIEPCLE RLRGEGLDLI 

       250        260        270        280        290        300 
GPLPADTLFT PKHLEHCDAV LAMYHDQGLP VLKYKGFGAA VNVTLGLPII RTSVDHGTAL 

       310        320 
DLAGSGRIDS GSLQVALETA YQMAASRC 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Crystal structure of pyridoxal phosphate biosynthetic protein pdxA PA0593."
Midwest center for structural genomics (MCSG)
Submitted (APR-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG03982.1.
PIRA83572.
RefSeqNP_249284.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YXOX-ray2.01A/B1-328[»]
ProteinModelPortalQ9I5U4.
SMRQ9I5U4. Positions 1-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA0593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID880733.
KEGGpae:PA0593.
PATRIC19835458. VBIPseAer58763_0629.

Organism-specific databases

PseudoCAPPA0593.

Phylogenomic databases

eggNOGCOG1995.
KOK00097.
OMAYVWDTPL.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK00232.

Enzyme and pathway databases

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

EvolutionaryTraceQ9I5U4.

Entry information

Entry namePDXA1_PSEAE
AccessionPrimary (citable) accession number: Q9I5U4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 86 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