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Q7UMZ2 (PDXA_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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:RB7885
OrganismRhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula

Protein attributes

Sequence length351 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 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

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpyridoxal phosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-hydroxythreonine-4-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

NAD binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3513514-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188824

Sites

Metal binding1891Divalent metal cation; shared with dimeric partner By similarity
Metal binding2381Divalent metal cation; shared with dimeric partner By similarity
Metal binding2941Divalent metal cation; shared with dimeric partner By similarity
Binding site1531Substrate By similarity
Binding site1541Substrate By similarity
Binding site3021Substrate By similarity
Binding site3111Substrate By similarity
Binding site3201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UMZ2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 6624680A06166B9F

FASTA35137,488
        10         20         30         40         50         60 
MTDANQTRPK LAITMGDAAG IGPEISLRVW DSPEVQSQGY PLLFGDAAIY HRAAKKLGCD 

        70         80         90        100        110        120 
CPGTISLAEF LDMPKQSIPS DAPHGVIVDC GKLTTEELGS FTPGKFSAAT GRASYQSVTD 

       130        140        150        160        170        180 
AIDAAVSGHV DAIVTGPIQK EAWHQAGIDF PGHTELLADR AGRAVQGEPA DVRMMLASDT 

       190        200        210        220        230        240 
IACVLETIHI PLADVASQLN TESLVRTINL AGETVQRRNQ NRGSLLPPRI AVCGLNPHAG 

       250        260        270        280        290        300 
ENGLFSHQEE EQIILPAIEA ARQSGWTIEG PLSPDTAFTP AMRERIDIYV CMYHDQGLIP 

       310        320        330        340        350 
LKALSFDDAV NVTLGLPIIR TSVDHGTAMD LAWQGKASIN SMLAAIRWAV P 

« Hide

References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294146 Genomic DNA. Translation: CAD75627.1.
RefSeqNP_868080.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UMZ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243090.RB7885.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD75627; CAD75627; RB7885.
GeneID1796393.
KEGGrba:RB7885.
PATRIC23249079. VBIRhoBal59814_3813.

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAADTLFHF.
OrthoDBEOG6GN6ZC.
ProtClustDBCLSK2305569.

Enzyme and pathway databases

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_RHOBA
AccessionPrimary (citable) accession number: Q7UMZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 73 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