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B5EL82 (PDXA_ACIF5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:Lferr_0344
OrganismAcidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993)) [Complete proteome] [HAMAP]
Taxonomic identifier380394 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

Protein attributes

Sequence length333 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 – 3333334-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000128235

Sites

Metal binding1661Divalent metal cation; shared with dimeric partner By similarity
Metal binding2111Divalent metal cation; shared with dimeric partner By similarity
Metal binding2661Divalent metal cation; shared with dimeric partner By similarity
Binding site1361Substrate By similarity
Binding site1371Substrate By similarity
Binding site2741Substrate By similarity
Binding site2831Substrate By similarity
Binding site2921Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B5EL82 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 0EE262B70D2090C7

FASTA33335,007
        10         20         30         40         50         60 
MITEPRLLLT VGEPAGIGPD ICLQLAFHAL PSGVLLIGDL HCLRSRALTL GLSLRLEPWL 

        70         80         90        100        110        120 
EGNPWPALER GVLHVLDVPL AQPCRPGRLD MANAPAVLAT LDKAMHLLRA GAADALVTAP 

       130        140        150        160        170        180 
VHKGIINDAG IPFTGHTEYL AAACGSPKVV MLLAGRGLRV ALATTHLPLA QVAAAVTQEG 

       190        200        210        220        230        240 
LEGTLRILHR ALREDFALSE PRILVAGLNP HAGEGGHLGH EEQDVIAPVI AALQGESLRI 

       250        260        270        280        290        300 
SGPWPADTLF TPRLLEDADA VLAMYHDQGL PVLKYHAFGE AVNITLGLPI VRTSVDHGTA 

       310        320        330 
LDIAGTGRAE GGSLLRALDN AAEIVRNRRA AGC 

« Hide

References

[1]"Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Borole A.P.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53993.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001132 Genomic DNA. Translation: ACH82598.1.
RefSeqYP_002218805.1. NC_011206.1.

3D structure databases

ProteinModelPortalB5EL82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING380394.Lferr_0344.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH82598; ACH82598; Lferr_0344.
GeneID6876295.
KEGGafe:Lferr_0344.
PATRIC20658208. VBIAciFer6930_0329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.
ProtClustDBCLSK2407271.

Enzyme and pathway databases

BioCycAFER380394:GHE0-346-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_ACIF5
AccessionPrimary (citable) accession number: B5EL82
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 14, 2008
Last modified: February 19, 2014
This is version 45 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