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Protein

Dihydroneopterin aldolase

Gene

folB

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. Can also catalyze the epimerization of carbon 2' of dihydroneopterin to dihydromonapterin.2 Publications

Catalytic activityi

7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde.1 Publication
7,8-dihydroneopterin = 7,8-dihydromonapterin.By similarity

pH dependencei

Optimum pH is 9.5.1 Publication

Pathway:itetrahydrofolate biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Dihydroneopterin aldolase (folB)
  4. no protein annotated in this organism
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei22 – 221SubstrateCombined sources2 Publications
Binding sitei54 – 541SubstrateCombined sources2 Publications
Active sitei100 – 1001Proton donor/acceptor2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Biological processi

Folate biosynthesis

Enzyme and pathway databases

BRENDAi4.1.2.25. 3352.
UniPathwayiUPA00077; UER00154.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroneopterin aldolase1 Publication (EC:4.1.2.251 Publication)
Short name:
DHNA1 Publication
Alternative name(s):
7,8-dihydroneopterin 2'-epimerase
7,8-dihydroneopterin aldolase
7,8-dihydroneopterin epimerase (EC:5.1.99.-)
Dihydroneopterin epimerase
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.1 Publication

Protein-protein interaction databases

STRINGi93062.SACOL0559.

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[»]
ProteinModelPortaliP56740.
SMRiP56740. Positions 1-121.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56740.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 742Substrate bindingCombined sources2 Publications

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

Sequence databases

RefSeqiWP_001154303.1. NZ_LN626917.1.

Cross-referencesi

Sequence databases

RefSeqiWP_001154303.1. NZ_LN626917.1.

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[»]
ProteinModelPortaliP56740.
SMRiP56740. Positions 1-121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL0559.

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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH 6-HYDROXYMETHYL-7,8-DIHYDRONEOPTERIN, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, ACTIVE SITE, SUBUNIT.
    Strain: ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413.
  2. "Discovery of potent inhibitors of dihydroneopterin aldolase using CrystaLEAD high-throughput X-ray crystallographic screening and structure-directed lead optimization."
    Sanders W.J., Nienaber V.L., Lerner C.G., McCall J.O., Merrick S.M., Swanson S.J., Harlan J.E., Stoll V.S., Stamper G.F., Betz S.F., Condroski K.R., Meadows R.P., Severin J.M., Walter K.A., Magdalinos P., Jakob C.G., Wagner R., Beutel B.A.
    J. Med. Chem. 47:1709-1718(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH 7,8-DIHYDRONEOPTERIN ANALOGS.
  3. "Structural basis for the aldolase and epimerase activities of Staphylococcus aureus dihydroneopterin aldolase."
    Blaszczyk J., Li Y., Gan J., Yan H., Ji X.
    J. Mol. Biol. 368:161-169(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEXES WITH D-MONAPTERIN AND L-NEOPTERIN, FUNCTION, REACTION MECHANISM, ACTIVE SITE.

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: July 22, 2015
This is version 66 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.