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Protein

Dihydroneopterin aldolase

Gene

folB

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. dihydroneopterin aldolase activity Source: UniProtKB-EC

GO - Biological processi

  1. folic acid biosynthetic process Source: UniProtKB-KW
  2. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Folate biosynthesis

Enzyme and pathway databases

BRENDAi4.1.2.25. 3352.
UniPathwayiUPA00077; UER00154.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroneopterin aldolase (EC:4.1.2.25)
Short name:
DHNA
Gene namesi
Name:folB
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 121121Dihydroneopterin aldolasePRO_0000168283Add
BLAST

Interactioni

Subunit structurei

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.

Structurei

Secondary structure

1
121
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1411Combined sources
Beta strandi17 – 193Combined sources
Helixi20 – 256Combined sources
Beta strandi27 – 3711Combined sources
Helixi40 – 456Combined sources
Helixi48 – 503Combined sources
Helixi54 – 6512Combined sources
Beta strandi66 – 683Combined sources
Helixi73 – 8715Combined sources
Beta strandi91 – 10212Combined sources
Beta strandi112 – 1198Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
SMRiP56740. Positions 1-121.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56740.

Family & Domainsi

Sequence similaritiesi

Belongs to the DHNA family.Curated

Phylogenomic databases

eggNOGiCOG1539.

Family and domain databases

InterProiIPR006156. Dihydroneopterin_aldolase.
IPR006157. FolB_dom.
[Graphical view]
PfamiPF02152. FolB. 1 hit.
[Graphical view]
SMARTiSM00905. FolB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00525. folB. 1 hit.
TIGR00526. folB_dom. 1 hit.

Sequencei

Sequence statusi: Complete.

P56740-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQDTIFLKGM RFYGYHGALS AENEIGQIFK VDVTLKVDLS EAGRTDNVID
60 70 80 90 100
TVHYGEVFEE VKSIMEGKAV NLLEHLAERI ANRINSQYNR VMETKVRITK
110 120
ENPPIPGHYD GVGIEIVREN K
Length:121
Mass (Da):13,751
Last modified:May 30, 2000 - v1
Checksum:i55B267FB69CA3D8D
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
SMRiP56740. Positions 1-121.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL3217378.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG1539.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00154.
BRENDAi4.1.2.25. 3352.

Miscellaneous databases

EvolutionaryTraceiP56740.

Family and domain databases

InterProiIPR006156. Dihydroneopterin_aldolase.
IPR006157. FolB_dom.
[Graphical view]
PfamiPF02152. FolB. 1 hit.
[Graphical view]
SMARTiSM00905. FolB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00525. folB. 1 hit.
TIGR00526. folB_dom. 1 hit.
ProtoNetiSearch...

Publicationsi

  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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    Strain: ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413.

Entry informationi

Entry nameiFOLB_STAAU
AccessioniPrimary (citable) accession number: P56740
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: April 1, 2015
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.