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A3MM39 (A3MM39_BURM7) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 43. 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 EMBL ABO07071.1
Ordered Locus Names:BMA10247_1786
OrganismBurkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]
Taxonomic identifier320389 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group ›

Protein attributes

Sequence length257 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 EMBL ABO07071.1
   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

Region18 – 1921-deoxy-D-xylulose 5-phosphate binding By similarity HAMAP-Rule MF_00279
Region222 – 22323-amino-2-oxopropyl phosphate binding By similarity HAMAP-Rule MF_00279

Sites

Active site521Proton acceptor By similarity HAMAP-Rule MF_00279
Active site791Proton acceptor By similarity HAMAP-Rule MF_00279
Active site2001Proton donor By similarity HAMAP-Rule MF_00279
Binding site1613-amino-2-oxopropyl phosphate By similarity HAMAP-Rule MF_00279
Binding site2713-amino-2-oxopropyl phosphate By similarity HAMAP-Rule MF_00279
Binding site5411-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site5911-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site10911-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site20113-amino-2-oxopropyl phosphate; via amide nitrogen By similarity HAMAP-Rule MF_00279
Site1601Transition state stabilizer By similarity HAMAP-Rule MF_00279

Sequences

Sequence LengthMass (Da)Tools
A3MM39 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: A1BC148BD3318247

FASTA25727,539
        10         20         30         40         50         60 
MSFFLTTPTA IDLGVNIDHV ATLRNARGTA YPDPVRAALA AEDAGADAIT LHLREDRRHI 

        70         80         90        100        110        120 
VDADVRTLRP RVKTRMNLEC AVTPEMLDIA CEIRPHDACL VPEKRSELTT EGGLDVVGHF 

       130        140        150        160        170        180 
DAVRAACKQL ADAGVRVSLF IDPDEAQIRA AHETGAPVIE LHTGRYADAH DAAEQQREFE 

       190        200        210        220        230        240 
RIATGVDAGI ALGLKVNAGH GLHYTNVQAI AALPGIAELN IGHAIVAHAV FVGWDNAVRE 

       250 
MKAIMVAARV AALHGGR

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 10247.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000548 Genomic DNA. Translation: ABO07071.1.
RefSeqYP_001081325.1. NC_009080.1.

3D structure databases

ProteinModelPortalA3MM39.
SMRA3MM39. Positions 13-249.
ModBaseSearch...

Protein-protein interaction databases

STRING320389.BMA10247_1786.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO07071; ABO07071; BMA10247_1786.
GeneID4891840.
KEGGbmn:BMA10247_1786.
PATRIC19145964. VBIBurMal96640_4026.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0854.
HOGENOMHOG000258094.
KOK03474.
OMALHYHNVK.
ProtClustDBPRK05265.

Enzyme and pathway databases

BioCycBMAL320389:GH97-1804-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 nameA3MM39_BURM7
AccessionPrimary (citable) accession number: A3MM39
Entry history
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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