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P56740

- FOLB_STAAU

UniProt

P56740 - FOLB_STAAU

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Protein

Dihydroneopterin aldolase

Gene

folB

Organism
Staphylococcus aureus
Status
Reviewed - 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

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:
PDBe
RCSB PDB
PDBj
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

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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DHN X-ray 1.65 A 1-121 [» ]
1RRI X-ray 2.00 A 1-121 [» ]
1RRW X-ray 2.21 A 1-121 [» ]
1RRY X-ray 2.70 A 1-121 [» ]
1RS2 X-ray 2.31 A 1-121 [» ]
1RS4 X-ray 2.70 A 1-121 [» ]
1RSD X-ray 2.50 A 1-121 [» ]
1RSI X-ray 2.20 A 1-121 [» ]
1U68 X-ray 2.40 A 1-121 [» ]
2DHN X-ray 2.20 A 1-121 [» ]
2NM2 X-ray 1.70 A/B/C/D 1-121 [» ]
2NM3 X-ray 1.68 A 1-121 [» ]
ProteinModelPortali P56740.
SMRi P56740. Positions 1-121.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG1539.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00154 .

Miscellaneous databases

EvolutionaryTracei P56740.

Family and domain databases

InterProi IPR006156. Dihydroneopterin_aldolase.
IPR006157. FolB_dom.
[Graphical view ]
Pfami PF02152. FolB. 1 hit.
[Graphical view ]
SMARTi SM00905. FolB. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00525. folB. 1 hit.
TIGR00526. folB_dom. 1 hit.
ProtoNeti Search...

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 (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: October 29, 2014
This is version 60 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