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Q0AQC2 (PDXA_MARMM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Mmar10_1222
OrganismMaricaulis maris (strain MCS10) [Complete proteome] [HAMAP]
Taxonomic identifier394221 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeMaricaulis

Protein attributes

Sequence length340 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 – 3403404-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000081867

Sites

Metal binding1771Divalent metal cation; shared with dimeric partner By similarity
Metal binding2221Divalent metal cation; shared with dimeric partner By similarity
Metal binding2771Divalent metal cation; shared with dimeric partner By similarity
Binding site1411Substrate By similarity
Binding site1421Substrate By similarity
Binding site2851Substrate By similarity
Binding site2941Substrate By similarity
Binding site3031Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AQC2 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: A848338DB11C6121

FASTA34035,313
        10         20         30         40         50         60 
MTQLSPVAVS MGDPAGIGPE IILKAWQSWR RRNGVPPLIA LGDIDAFTAT AQALGLPAPC 

        70         80         90        100        110        120 
PLPTPTREAA ETLDGLPVFD VGVKIAAPVR PGQPDTANAA CTKAAIETGV RLALDGQVSA 

       130        140        150        160        170        180 
LVTAPIAKSV MYEAGFAFPG HTEFLAELCA DHPVDGPKGP AMMLAGGGLR VVLVTIHEPL 

       190        200        210        220        230        240 
VRALSLITPQ RVEATARITD AALRRDFGIA RPRLALAGLN PHAGEGGALG DEEIDILDPL 

       250        260        270        280        290        300 
AARLRADGID ITDAQPPDTL FHAEARAGYD AAICLYHDQG LIPVKTLDFH GGVNITLGLP 

       310        320        330        340 
IVRTSPDHGT AFNIAGQGVA RPDSLLAALE QAVKIAECRA 

« Hide

References

[1]"Complete sequence of Maricaulis maris MCS10."
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., Mikhailova N., Viollier P., Stephens C., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000449 Genomic DNA. Translation: ABI65515.1.
RefSeqYP_756453.1. NC_008347.1.

3D structure databases

ProteinModelPortalQ0AQC2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING394221.Mmar10_1222.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI65515; ABI65515; Mmar10_1222.
GeneID4286475.
KEGGmmr:Mmar10_1222.
PATRIC22450514. VBIMarMar77530_1250.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMACAYHDQA.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK05312.

Enzyme and pathway databases

BioCycMMAR394221:GHNB-1246-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_MARMM
AccessionPrimary (citable) accession number: Q0AQC2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 60 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