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B8GMX6 (PDXA_THISH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:Tgr7_2716
OrganismThioalkalivibrio sp. (strain HL-EbGR7) [Complete proteome] [HAMAP]
Taxonomic identifier396588 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeThioalkalivibrio

Protein attributes

Sequence length331 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 – 3313314-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000146494

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
B8GMX6 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: EE79E5E289CE0811

FASTA33134,662
        10         20         30         40         50         60 
MTTTPRIAIT PGEPAGIGPD LVVAVAQVPC AAQRVVLSDP ALLRERARLL GLPLEIRPFD 

        70         80         90        100        110        120 
PQTPAAPDPA GCLTVMAHAL NAPVRPGHLD TANARHVLAT LESAVAGCLD GRFDALVTGP 

       130        140        150        160        170        180 
VHKGIINDAG IPFTGHTEFL AERSGAPTPV MLLAAGALRV ALATTHLPLR AVADAITPAG 

       190        200        210        220        230        240 
LEHVLRVLNQ DLKTKFAISE PRILVCGLNP HAGEGGHLGR EEIEVIGPVL ERLRTQGLHL 

       250        260        270        280        290        300 
IGPLPADTLF TPRHLEHADA ILAMYHDQGL PVLKHAGFGR AVNITLGLPL IRTSVDHGTA 

       310        320        330 
LELAGSGRAE AGSFMEAERL AIEMARSAHG L 

« Hide

References

[1]"Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7."
Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N., Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.
Stand. Genomic Sci. 4:23-35(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HL-EbGR7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001339 Genomic DNA. Translation: ACL73791.1.
RefSeqYP_002514778.1. NC_011901.1.

3D structure databases

ProteinModelPortalB8GMX6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING396588.Tgr7_2716.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL73791; ACL73791; Tgr7_2716.
GeneID7316878.
KEGGtgr:Tgr7_2716.
PATRIC23964942. VBIThiSp19295_2692.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycTSUL396588:GH5B-2760-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_THISH
AccessionPrimary (citable) accession number: B8GMX6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 40 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