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A1B0G5 (PDXA_PARDP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:Pden_0898
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length322 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 – 3223224-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000128256

Sites

Metal binding1601Divalent metal cation; shared with dimeric partner By similarity
Metal binding2051Divalent metal cation; shared with dimeric partner By similarity
Metal binding2601Divalent metal cation; shared with dimeric partner By similarity
Binding site1261Substrate By similarity
Binding site1271Substrate By similarity
Binding site2681Substrate By similarity
Binding site2771Substrate By similarity
Binding site2861Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1B0G5 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 60B2EF5329401A54

FASTA32233,869
        10         20         30         40         50         60 
MTEARPIILT CGEPAGVGPE LAPKALASGV PFVFLGDPRH LPEGTAWAEV TAPGEPVADG 

        70         80         90        100        110        120 
VLAVLRHDFP APARPGQPDP ANAPAVIEVI ARAVDLAMSG AAGGICTLPI NKEALKRGAG 

       130        140        150        160        170        180 
FGFPGHTEYL AHLAGDVPVV MMLASTTVQP PCRVVPVTIH IPLSEVPLAL TPLRLEQAIR 

       190        200        210        220        230        240 
ITDAAMRRDF GLAQPRLAIA GLNPHAGENG VMGDEEARWM APLIERLRRE GFDLRGPLPA 

       250        260        270        280        290        300 
DTMFHPAARA RYDAALCAYH DQALIPIKTL DFAGGVNITL GLPFVRTSPD HGTAFDIAGQ 

       310        320 
GIADAESVIA ALRMAHEMAA RR 

« Hide

References

[1]"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222."
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000489 Genomic DNA. Translation: ABL69009.1.
RefSeqYP_914705.1. NC_008686.1.

3D structure databases

ProteinModelPortalA1B0G5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318586.Pden_0898.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL69009; ABL69009; Pden_0898.
GeneID4578576.
KEGGpde:Pden_0898.
PATRIC22852954. VBIParDen97112_0874.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMACAYHDQA.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK05312.

Enzyme and pathway databases

BioCycPDEN318586:GCVQ-911-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_PARDP
AccessionPrimary (citable) accession number: A1B0G5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 54 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