Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q39Q58 (PDXA_GEOMG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:Gmet_3404
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP]
Taxonomic identifier269799 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length339 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 – 3393394-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000051501

Sites

Metal binding1711Divalent metal cation; shared with dimeric partner By similarity
Metal binding2151Divalent metal cation; shared with dimeric partner By similarity
Metal binding2701Divalent metal cation; shared with dimeric partner By similarity
Binding site1411Substrate By similarity
Binding site1421Substrate By similarity
Binding site2781Substrate By similarity
Binding site2871Substrate By similarity
Binding site2961Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39Q58 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 7D2A3BFA7F1C7DF8

FASTA33936,281
        10         20         30         40         50         60 
MPNTKPRIVI TMGDPTGVGP EIIAATLAEP EVRQCCRFLV VGDSAAMARG ITVAGAALRV 

        70         80         90        100        110        120 
ERTDTLNWEE SKEGVLPLWE ISSLTEADMQ YGCPTVASGD AMYRAICEAA RLCLEGNADA 

       130        140        150        160        170        180 
MATAPISKEA LNRAGHRYPG HTELLAELAG AERVVMMLAG FRLRVTLVTI HEALADVPRL 

       190        200        210        220        230        240 
VTFERVLETI RITHRDLHRY FRRNPRIAVL ALNPHCGEGG MFGDEEARII APAVAAARQE 

       250        260        270        280        290        300 
GIDAIGPLSA DTLFHFAVQG AYDAVVCMYH DQGLIPLKLL HFDDGVNVTL GLPIIRTSVD 

       310        320        330 
HGTAYDLAGT GRASAESMKA AILMAAEMAR VKGSGGGTP 

« Hide

References

[1]"Complete sequence of Geobacter metallireducens GS-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GS-15 / ATCC 53774 / DSM 7210.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000148 Genomic DNA. Translation: ABB33616.1.
RefSeqYP_006722358.1. NC_007517.1.

3D structure databases

ProteinModelPortalQ39Q58.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269799.Gmet_3404.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB33616; ABB33616; Gmet_3404.
GeneID3741182.
KEGGgme:Gmet_3404.
PATRIC22006088. VBIGeoMet55070_3446.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221593.
KOK00097.
OMAWPERPAK.
OrthoDBEOG6CVV6Z.

Enzyme and pathway databases

BioCycGMET269799:GHNY-3453-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_GEOMG
AccessionPrimary (citable) accession number: Q39Q58
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: May 14, 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