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Q9RC88 (PDXA_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. 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:BH0804
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length334 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
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 – 3343344-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188797

Sites

Metal binding1701Divalent metal cation; shared with dimeric partner By similarity
Metal binding2141Divalent metal cation; shared with dimeric partner By similarity
Metal binding2691Divalent metal cation; shared with dimeric partner By similarity
Binding site1401Substrate By similarity
Binding site1411Substrate By similarity
Binding site2771Substrate By similarity
Binding site2951Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RC88 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 24436A1866079820

FASTA33436,632
        10         20         30         40         50         60 
MNKKPIIAIP MGDPAGIGPE ITVGALNKKE LYDVANPVVI GHGDMLEKML PVMKADLTIN 

        70         80         90        100        110        120 
RITTVDEAMF EYGTIDVIHL DNLNVAEVKM GTVQAQCGKA AFEYIRHAVQ LANDKKVDAL 

       130        140        150        160        170        180 
ATTPINKESL KAAEVPYIGH TEMLADLTKT EDPLTMFEVH SMRIFFLTRH LSLKDAIDQM 

       190        200        210        220        230        240 
TKERVHDYLL RCDKALEKLG VKERRFAVAG LNPHSGENGL FGREEMDEIT PGIELAKKDG 

       250        260        270        280        290        300 
INAVGPVPAD SVFHHALNGR YDAVLSLYHD QGHIAAKMTD FERTISITNG LPFLRTSVDH 

       310        320        330 
GTAFDIAGKG IASTVSMEEC IKLAAKYAPH FVTA 

« Hide

References

« Hide 'large scale' references
[1]"Genetic analysis of the chromosome of alkaliphilic Bacillus halodurans C-125."
Takami H., Takaki Y., Nakasone K., Sakiyama T., Maeno G., Sasaki R., Hirama C., Fuji F., Masui N.
Extremophiles 3:227-233(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
[2]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB024550 Genomic DNA. Translation: BAA83911.1.
BA000004 Genomic DNA. Translation: BAB04523.1.
PIRD83750.
RefSeqNP_241670.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9RC88.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH0804.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB04523; BAB04523; BAB04523.
GeneID892178.
KEGGbha:BH0804.
PATRIC18938608. VBIBacHal18977_0842.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000040097.
KOK00097.
OMAAIPMGDP.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-862-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_BACHD
AccessionPrimary (citable) accession number: Q9RC88
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 86 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