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Q2JSC8 (PDXA_SYNJA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:CYA_2324
OrganismSynechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime) [Complete proteome] [HAMAP]
Taxonomic identifier321327 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length349 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 – 3493494-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000051521

Sites

Metal binding1701Divalent metal cation; shared with dimeric partner By similarity
Metal binding2151Divalent metal cation; shared with dimeric partner By similarity
Metal binding2761Divalent metal cation; shared with dimeric partner By similarity
Binding site1351Substrate By similarity
Binding site2841Substrate By similarity
Binding site2931Substrate By similarity
Binding site3021Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2JSC8 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: EFC1717F80A0341E

FASTA34937,136
        10         20         30         40         50         60 
MSLLLPKLAL TLGDPAGIGP EIVLKALADP QVQACAQITV VGERQVLEAT YCLLRQRGAT 

        70         80         90        100        110        120 
DLADPAGIPV LEGGSGFYLE PSRVGRGDVA SGAASFAYLK TAIEEALRGQ FQGIVTAPIA 

       130        140        150        160        170        180 
KYLWHQAGYP FPGQTEVLAQ LSGSERYGML FVARSPHSGW QIRVLLATTH IPLSQVPLTL 

       190        200        210        220        230        240 
TPELVRAKLD LLVGSLRKLF GIVNPVIAVA GLNPHAGEQG QLGQEEKTWL AELLRTYPHA 

       250        260        270        280        290        300 
KIWGPLPPDT MWLAPAQAWY GQGAPAVADA YLALYHDQGL IPVKLLAFDR AVNLTLGLPF 

       310        320        330        340 
IRTSPDHGTA FDLAGQGVAR AESLKQAILL AAELALSSAA ASRSLQAQR 

« Hide

References

[1]"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JA-3-3Ab.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000239 Genomic DNA. Translation: ABD00453.1.
RefSeqYP_475716.1. NC_007775.1.

3D structure databases

ProteinModelPortalQ2JSC8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321327.CYA_2324.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD00453; ABD00453; CYA_2324.
GeneID3897323.
KEGGcya:CYA_2324.
PATRIC23812908. VBISynSp90045_2281.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAISIKLAM.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycSSP321327:GHFX-2317-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_SYNJA
AccessionPrimary (citable) accession number: Q2JSC8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: May 14, 2014
This is version 58 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