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A1U6F9 (PDXA_MARAV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Maqu_3508
OrganismMarinobacter aquaeolei (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter hydrocarbonoclasticus (strain DSM 11845)) [Complete proteome] [HAMAP]
Taxonomic identifier351348 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeMarinobacter

Protein attributes

Sequence length336 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 – 3363364-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000051507

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A1U6F9 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: EEBB9ED10E708F1F

FASTA33635,346
        10         20         30         40         50         60 
MSTPVILALT AGEPAGIGPE LCLQLATGSR DAGLVVIASG ELLRDRASQL GLQIELHDWQ 

        70         80         90        100        110        120 
PGVAAATRAG HLSVRHVEGC GSTVAGRLDK ANSQYVLDTL TIAARGCLNG DFDGMVTAPV 

       130        140        150        160        170        180 
HKGVINEAGI VFSGHTEFLQ ELCGVERVVM MLATEELRVA LVTTHLPLKD VSAAITPDRL 

       190        200        210        220        230        240 
TQVTRILNAD LKAFFGIDQP RILVAGLNPH AGEGGHLGRE EIEVIEPTLE QLRAEGIQLT 

       250        260        270        280        290        300 
GPLPADTLFT PHWLDNADAV LAMYHDQGLP VLKFQGFGRA VNITLGLPIV RTSVDHGTAL 

       310        320        330 
DLAGTGKADA GSLHTAIRVG EQMAQCRKAT GAGELS 

« Hide

References

[1]"Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."
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., Kiss H., 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., Edwards K., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700491 / DSM 11845 / VT8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000514 Genomic DNA. Translation: ABM20578.1.
RefSeqYP_960765.1. NC_008740.1.

3D structure databases

ProteinModelPortalA1U6F9.
SMRA1U6F9. Positions 7-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351348.Maqu_3508.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM20578; ABM20578; Maqu_3508.
GeneID4657262.
KEGGmaq:Maqu_3508.
PATRIC22462380. VBIMarAqu65105_3930.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMAIMANEMA.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycMHYD351348:GHYZ-3570-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_MARAV
AccessionPrimary (citable) accession number: A1U6F9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 50 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