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P56740 (FOLB_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Dihydroneopterin aldolase

Short name=DHNA
EC=4.1.2.25
Gene names
Name:folB
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length121 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.

Catalytic activity

2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.

Subunit structure

Homooctamer. Four molecules assemble into a ring, and two rings come together to give a cylinder with a hole of at least 13 a diameter.

Sequence similarities

Belongs to the DHNA family.

Ontologies

Keywords
   Biological processFolate biosynthesis
   Molecular functionLyase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processfolic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

tetrahydrofolate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functiondihydroneopterin aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 121121Dihydroneopterin aldolase
PRO_0000168283

Secondary structure

..................... 121
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56740 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: 55B267FB69CA3D8D

FASTA12113,751
        10         20         30         40         50         60 
MQDTIFLKGM RFYGYHGALS AENEIGQIFK VDVTLKVDLS EAGRTDNVID TVHYGEVFEE 

        70         80         90        100        110        120 
VKSIMEGKAV NLLEHLAERI ANRINSQYNR VMETKVRITK ENPPIPGHYD GVGIEIVREN 


K 

« Hide

References

[1]"Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus."
Hennig M., D'Arcy A., Hampele I.C., Page M.G., Oefner C., Dale G.E.
Nat. Struct. Biol. 5:357-362(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Strain: ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DHNX-ray1.65A1-121[»]
1RRIX-ray2.00A1-121[»]
1RRWX-ray2.21A1-121[»]
1RRYX-ray2.70A1-121[»]
1RS2X-ray2.31A1-121[»]
1RS4X-ray2.70A1-121[»]
1RSDX-ray2.50A1-121[»]
1RSIX-ray2.20A1-121[»]
1U68X-ray2.40A1-121[»]
2DHNX-ray2.20A1-121[»]
2NM2X-ray1.70A/B/C/D1-121[»]
2NM3X-ray1.68A1-121[»]
ProteinModelPortalP56740.
SMRP56740. Positions 1-121.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1539.

Enzyme and pathway databases

UniPathwayUPA00077; UER00154.

Family and domain databases

InterProIPR006156. Dihydroneopterin_aldolase.
IPR006157. FolB_dom.
[Graphical view]
PfamPF02152. FolB. 1 hit.
[Graphical view]
SMARTSM00905. FolB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00525. folB. 1 hit.
TIGR00526. folB_dom. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP56740.

Entry information

Entry nameFOLB_STAAU
AccessionPrimary (citable) accession number: P56740
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: October 16, 2013
This is version 58 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways