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B7KAA8 (PDXA_CYAP7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:PCC7424_4519
OrganismCyanothece sp. (strain PCC 7424) (Synechococcus sp. (strain ATCC 29155)) [Complete proteome] [HAMAP]
Taxonomic identifier65393 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length343 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 – 3433434-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000128240

Sites

Metal binding1701Divalent metal cation; shared with dimeric partner By similarity
Metal binding2151Divalent metal cation; shared with dimeric partner By similarity
Metal binding2821Divalent metal cation; shared with dimeric partner By similarity
Binding site1351Substrate By similarity
Binding site2901Substrate By similarity
Binding site2991Substrate By similarity
Binding site3081Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B7KAA8 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 9E479E2A31053509

FASTA34336,976
        10         20         30         40         50         60 
MKSLALTLGD PAGIGSEVIL KALADPSVGE NYNITVVGSR SLLEESYHQL RSLPHVNHSD 

        70         80         90        100        110        120 
LVDPANLLIL DIPLDKTTKS QIQLGKGNAA SGEASFTYLQ AAIAGTLKGE FAGIVTAPIA 

       130        140        150        160        170        180 
KSCWKAAGYH YPGQTEVLAQ AAGVEKFGML FVARSPYTGW MLRTLLATTH IPLSQVPTVL 

       190        200        210        220        230        240 
TPELMTLKLE LLIDCLKNDF RLDHPKIAIA GLNPHSGEQG QLGTEERDWL TPWLEEEKKR 

       250        260        270        280        290        300 
HCEVELVGLV PPDTMWVTPG QAWYGNAPHP QHGADGYLAL YHDQGLIPVK LMAFDQAINT 

       310        320        330        340 
TIGLPFIRTS PDHGTAFDIA GKGIARPASM IEAIKLAQAL VNG 

« Hide

References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001291 Genomic DNA. Translation: ACK72882.1.
RefSeqYP_002379750.1. NC_011729.1.

3D structure databases

ProteinModelPortalB7KAA8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING65393.PCC7424_4519.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK72882; ACK72882; PCC7424_4519.
GeneID7110385.
KEGGcyc:PCC7424_4519.
PATRIC21558056. VBICyaSp136448_4624.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAISIKLAM.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycCSP65393:GJP7-4569-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_CYAP7
AccessionPrimary (citable) accession number: B7KAA8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 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