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Q3AVH3 (PDXJ_SYNS9) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyridoxine 5'-phosphate synthase
Short name=PNP synthase
EC=2.6.99.2
Gene names
Name:pdxJ
Ordered Locus Names:Syncc9902_1414
OrganismSynechococcus sp. (strain CC9902) [Complete proteome] [HAMAP]
Taxonomic identifier316279 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus

Protein attributes

Sequence length249 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

Catalytic activity

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

Pathway

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

Subunit structure

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00279.

Sequence similarities

Belongs to the PNP synthase family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   Molecular functionTransferase
   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

Molecule processing

Chain1 – 249249Pyridoxine 5'-phosphate synthase HAMAP-Rule MF_00279
PRO_1000022411

Regions

Region9 – 1021-deoxy-D-xylulose 5-phosphate binding By similarity
Region212 – 21323-amino-2-oxopropyl phosphate binding By similarity

Sites

Active site431Proton acceptor By similarity
Active site701Proton acceptor By similarity
Active site1901Proton donor By similarity
Binding site713-amino-2-oxopropyl phosphate By similarity
Binding site1813-amino-2-oxopropyl phosphate By similarity
Binding site4511-deoxy-D-xylulose 5-phosphate By similarity
Binding site5011-deoxy-D-xylulose 5-phosphate By similarity
Binding site10011-deoxy-D-xylulose 5-phosphate By similarity
Binding site19113-amino-2-oxopropyl phosphate; via amide nitrogen By similarity
Site1511Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3AVH3 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: FF18984A5AB9E5C6

FASTA24927,077
        10         20         30         40         50         60 
MASLGVNIDH IANIREARRT VEPDPVPMAM LAELGGADGI TVHLREDRRH IQDRDVELLR 

        70         80         90        100        110        120 
QTVRSRLNLE MAATAEMVAI ALRVKPDMVT LVPEHRQEVT TEGGLDVVAQ LSELTGMVSQ 

       130        140        150        160        170        180 
LQTSGIPVSL FVDPVASQLR GCTDSGARWV ELHTGRYAEG SWNDQPHELA RLTEGTATAR 

       190        200        210        220        230        240 
AMGLRVNAGH GLTYQNVEPV AAIPGMEELN IGHTIVARAV VVGLQQAVRE MKALIQNPRR 


DPLFGQALG

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9902."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9902.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000097 Genomic DNA. Translation: ABB26378.1.
RefSeqYP_377422.1. NC_007513.1.

3D structure databases

ProteinModelPortalQ3AVH3.
SMRQ3AVH3. Positions 3-239.
ModBaseSearch...

Protein-protein interaction databases

STRING316279.Syncc9902_1414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB26378; ABB26378; Syncc9902_1414.
GeneID3742124.
KEGGsye:Syncc9902_1414.
PATRIC23800213. VBISynSp76179_1566.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0854.
HOGENOMHOG000258094.
KOK03474.
OMALHYHNVK.
ProtClustDBPRK05265.

Enzyme and pathway databases

BioCycSSP316279:GJCI-1428-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 namePDXJ_SYNS9
AccessionPrimary (citable) accession number: Q3AVH3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: May 29, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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