Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q0HGA1 (Q0HGA1_SHESM) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:Shewmr4_2845
OrganismShewanella sp. (strain MR-4) [Complete proteome] [HAMAP] EMBL ABI39916.1
Taxonomic identifier60480 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length245 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. HAMAP-Rule MF_00279

Ontologies

Keywords
   Biological processPyridoxine biosynthesis HAMAP-Rule MF_00279
   Cellular componentCytoplasm HAMAP-Rule MF_00279
   Molecular functionTransferase HAMAP-Rule MF_00279
   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

Region11 – 1221-deoxy-D-xylulose 5-phosphate binding By similarity HAMAP-Rule MF_00279
Region215 – 21623-amino-2-oxopropyl phosphate binding By similarity HAMAP-Rule MF_00279

Sites

Active site451Proton acceptor By similarity HAMAP-Rule MF_00279
Active site721Proton acceptor By similarity HAMAP-Rule MF_00279
Active site1931Proton donor By similarity HAMAP-Rule MF_00279
Binding site913-amino-2-oxopropyl phosphate By similarity HAMAP-Rule MF_00279
Binding site2013-amino-2-oxopropyl phosphate By similarity HAMAP-Rule MF_00279
Binding site4711-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site5211-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site10211-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site19413-amino-2-oxopropyl phosphate; via amide nitrogen By similarity HAMAP-Rule MF_00279
Site1531Transition state stabilizer By similarity HAMAP-Rule MF_00279

Sequences

Sequence LengthMass (Da)Tools
Q0HGA1 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 44D71F498D064724

FASTA24526,460
        10         20         30         40         50         60 
MSRILLGVNI DHIATLRQAR GTSYPDPVHA AAVAEHAGAD GITIHLREDR RHIIDRDVYL 

        70         80         90        100        110        120 
LAKTLKTRMN FECAVTEEML NIACEVKPTY VCLVPEKRQE VTTEGGLDVA GQLDKITAAV 

       130        140        150        160        170        180 
SRLAANGIQV SLFIDADKTQ IDAAVESGAP LIEIHTGCYA DAKTAEEEAK ELARISEMAK 

       190        200        210        220        230        240 
YAHGKGLVVN AGHGLHYHNV KPIAAIPELY ELNIGHAIVA RAAIDGLATA VKDMKALMLE 


GRRGE

« Hide

References

[1]"Complete sequence of Shewanella sp. MR-4."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MR-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000446 Genomic DNA. Translation: ABI39916.1.
RefSeqYP_734973.1. NC_008321.1.

3D structure databases

ProteinModelPortalQ0HGA1.
SMRQ0HGA1. Positions 2-242.
ModBaseSearch...

Protein-protein interaction databases

STRING60480.Shewmr4_2845.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI39916; ABI39916; Shewmr4_2845.
GeneID4253416.
KEGGshe:Shewmr4_2845.
PATRIC23582468. VBISheSp133532_2949.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0854.
HOGENOMHOG000258094.
KOK03474.
OMALHYHNVK.
ProtClustDBPRK05265.

Enzyme and pathway databases

BioCycSSP60480:GI2N-2962-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 nameQ0HGA1_SHESM
AccessionPrimary (citable) accession number: Q0HGA1
Entry history
Integrated into UniProtKB/TrEMBL: October 3, 2006
Last sequence update: October 3, 2006
Last modified: May 29, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info