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C6W4V5 (C6W4V5_DYAFD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyridoxine 5'-phosphate synthase HAMAP-Rule MF_00279
Short name=PNP synthase HAMAP-Rule MF_00279
EC=2.6.99.2 HAMAP-Rule MF_00279
Gene names
Name:pdxJ HAMAP-Rule MF_00279
Ordered Locus Names:Dfer_4728
OrganismDyadobacter fermentans (strain ATCC 700827 / DSM 18053 / NS114) [Complete proteome] [HAMAP] EMBL ACT95929.1
Taxonomic identifier471854 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Cytophagia › Cytophagales › Cytophagaceae › Dyadobacter ›

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate By similarity. HAMAP-Rule MF_00279 SAAS SAAS004569

Catalytic activity

1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2 H2O. HAMAP-Rule MF_00279 SAAS SAAS004569

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5. HAMAP-Rule MF_00279 SAAS SAAS004569

Subunit structure

Homooctamer; tetramer of dimers By similarity. HAMAP-Rule MF_00279 SAAS SAAS004569

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00279 SAAS SAAS004569.

Sequence similarities

Belongs to the PNP synthase family. HAMAP-Rule MF_00279

Ontologies

Keywords
   Biological processPyridoxine biosynthesis HAMAP-Rule MF_00279 SAAS SAAS004569
   Cellular componentCytoplasm HAMAP-Rule MF_00279 SAAS SAAS004569
   Molecular functionTransferase HAMAP-Rule MF_00279 SAAS SAAS004569
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpyridoxine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpyridoxine 5'-phosphate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region214 – 21523-amino-2-oxopropyl phosphate binding By similarity HAMAP-Rule MF_00279

Sites

Active site431Proton acceptor By similarity HAMAP-Rule MF_00279
Active site701Proton acceptor By similarity HAMAP-Rule MF_00279
Active site1911Proton donor By similarity HAMAP-Rule MF_00279
Binding site713-amino-2-oxopropyl phosphate By similarity HAMAP-Rule MF_00279
Binding site1813-amino-2-oxopropyl phosphate By similarity HAMAP-Rule MF_00279
Binding site4511-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site5011-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site10111-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site19213-amino-2-oxopropyl phosphate; via amide nitrogen By similarity HAMAP-Rule MF_00279
Site1521Transition state stabilizer By similarity HAMAP-Rule MF_00279

Sequences

Sequence LengthMass (Da)Tools
C6W4V5 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: 864514217D8C818A

FASTA23926,565
        10         20         30         40         50         60 
MTRLSVNINK IATLRNSRGG DNPNVLKVAL DCERFGAQGI TVHPRPDERH IRYQDVYDLR 

        70         80         90        100        110        120 
ELVTTEFNIE GNPSEKKFVE LVLANKPDQV TLVPDALGAI TSNAGWDTIT HRSVLTDLVG 

       130        140        150        160        170        180 
TFKSAGIRVS VFVDPDEDMV EGAKICGADR VELYTEPFAA GYFENRQKAV LPFVKAAEKA 

       190        200        210        220        230 
REVGLGLNAG HDLSLDNLHF LKQSIPWMDE VSIGHALICD ALYIGLENTI QMYLRELEL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001619 Genomic DNA. Translation: ACT95929.1.
RefSeqYP_003089094.1. NC_013037.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING471854.Dfer_4728.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT95929; ACT95929; Dfer_4728.
GeneID8228334.
KEGGdfe:Dfer_4728.
PATRIC21831075. VBIDyaFer416_4856.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0854.
HOGENOMHOG000258095.
KOK03474.
OMALHYHNVK.
ProtClustDBPRK05265.

Enzyme and pathway databases

BioCycDFER471854:GI24-4769-MONOMER.
UniPathwayUPA00244; UER00313.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00279. PdxJ.
InterProIPR013785. Aldolase_TIM.
IPR004569. PyrdxlP_synth_PdxJ.
[Graphical view]
PfamPF03740. PdxJ. 1 hit.
[Graphical view]
SUPFAMSSF63892. PyrdxlP_synth_PdxJ. 1 hit.
TIGRFAMsTIGR00559. pdxJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC6W4V5_DYAFD
AccessionPrimary (citable) accession number: C6W4V5
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: May 1, 2013
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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