Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydroneopterin aldolase

Gene

folB

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: -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

Pathwayi: tetrahydrofolate 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. 7,8-dihydroneopterin aldolase (folB), 7,8-dihydroneopterin aldolase (folB), Dihydroneopterin aldolase (folB), 7,8-dihydroneopterin aldolase (BSZ10_07805), 7,8-dihydroneopterin aldolase (BTN44_10190), 7,8-dihydroneopterin aldolase (folB), 7,8-dihydroneopterin aldolase (folB), 7,8-dihydroneopterin aldolase (folB), 7,8-dihydroneopterin aldolase (HMPREF3211_00344)
  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)DescriptionActionsGraphical viewLength
Binding sitei22SubstrateCombined sources2 Publications1
Binding sitei54SubstrateCombined sources2 Publications1
Active sitei100Proton donor/acceptor2 Publications1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Lyase
Biological processFolate 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:5.1.99.8By similarity)
Dihydroneopterin epimerase
Gene namesi
Name:folB
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3217378
DrugBankiDB06906 2-AMINO-4-HYDROXYPYRIMIDINE-5-CARBOXYLIC ACID ETHYL ESTER
DB04168 2-Amino-5-Bromo-6-Phenylpyrimidin-4-Ol
DB02489 9-Methylguanine

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001682831 – 121Dihydroneopterin aldolaseAdd BLAST121

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

Structurei

Secondary structure

1121
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 14Combined sources11
Beta strandi17 – 19Combined sources3
Helixi20 – 25Combined sources6
Beta strandi27 – 37Combined sources11
Helixi40 – 45Combined sources6
Helixi48 – 50Combined sources3
Helixi54 – 65Combined sources12
Beta strandi66 – 68Combined sources3
Helixi73 – 87Combined sources15
Beta strandi91 – 102Combined sources12
Beta strandi112 – 119Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56740

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni73 – 74Substrate bindingCombined sources2 Publications2

Sequence similaritiesi

Belongs to the DHNA family.Curated

Phylogenomic databases

eggNOGiENOG4105KRF Bacteria
COG1539 LUCA

Family and domain databases

CDDicd00534 DHNA_DHNTPE, 1 hit
InterProiView protein in InterPro
IPR006156 Dihydroneopterin_aldolase
IPR006157 FolB_dom
PfamiView protein in Pfam
PF02152 FolB, 1 hit
SMARTiView protein in SMART
SM00905 FolB, 1 hit
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_PNGH01000019.1

Similar proteinsi

Entry informationi

Entry nameiFOLB_STAAU
AccessioniPrimary (citable) accession number: P56740
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: May 23, 2018
This is version 84 of the entry and version 1 of the sequence. See 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health