(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Archaea: NE > Euryarchaeota: NE > Archaeoglobi: NE > Archaeoglobales: NE > Archaeoglobaceae: NE > Archaeoglobus: NE > Archaeoglobus fulgidus: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Archaeoglobus fulgidus DSM 8774: N, E.
Archaeoglobus fulgidus DSM 4304: N, E.
Molecular evidence
Database
No mutation 4 structures(e.g. : 2ZYH, 2ZYI, 2ZYR... more)(less) 2ZYH: mutant A. Fulgidus lipase S136A complexed with fatty acid fragment, 2ZYI: A. Fulgidus lipase with fatty acid fragment and calcium, 2ZYR: A. Fulgidus lipase with fatty acid fragment and magnesium, 2ZYS: A. Fulgidus lipase with fatty acid fragment and chloride No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MRGLAVLVLLVFAVQVAAAEDFRPVVFVHGLAGSAGQFESQGMRFAANGY PAEYVKTFEYDTISWALVVETDMLFSGLGSEFGLNISQIIDPETLDKILS KSRERLIDETFSRLDRVIDEALAESGADKVDLVGHSMGTFFLVRYVNSSP ERAAKVAHLILLDGVWGVDAPEGIPTLAVFGNPKALPALGLPEEKVVYNA TNVYFNNMTHVQLCTSPETFAVMFEFINGYKPATTDIVPQDGDYVKVKGK FLAFATNGDVSGWLSIYPIDENGKRLTRLPVKFMRVKGDFEVRLRKGQLY EFQFRKDFSPIIYHYYRAPFVRDDLWARFLVSKPPLDVELLILPERLSPA AKETSGLLLIRYKEMIGEYDEEIGGVDEVYVNGVNVCTERICPIERAVNG LWVFDRGADGKSDLDREVVRYSIMPFMSAADLVVPAEGTISIAVKSRTGG EESFTIPAWSADRHSIIVQFSDYI
References
Title: Structure of the alkalohyperthermophilic Archaeoglobus fulgidus lipase contains a unique C-terminal domain essential for long-chain substrate binding Chen CK, Lee GC, Ko TP, Guo RT, Huang LM, Liu HJ, Ho YF, Shaw JF, Wang AH Ref: Journal of Molecular Biology, 390:672, 2009 : PubMed
Several crystal structures of AFL, a novel lipase from the archaeon Archaeoglobus fulgidus, complexed with various ligands, have been determined at about 1.8 A resolution. This enzyme has optimal activity in the temperature range of 70-90 degrees C and pH 10-11. AFL consists of an N-terminal alpha/beta-hydrolase fold domain, a small lid domain, and a C-terminal beta-barrel domain. The N-terminal catalytic domain consists of a 6-stranded beta-sheet flanked by seven alpha-helices, four on one side and three on the other side. The C-terminal lipid binding domain consists of a beta-sheet of 14 strands and a substrate covering motif on top of the highly hydrophobic substrate binding site. The catalytic triad residues (Ser136, Asp163, and His210) and the residues forming the oxyanion hole (Leu31 and Met137) are in positions similar to those of other lipases. Long-chain lipid is located across the two domains in the AFL-substrate complex. Structural comparison of the catalytic domain of AFL with a homologous lipase from Bacillus subtilis reveals an opposite substrate binding orientation in the two enzymes. AFL has a higher preference toward long-chain substrates whose binding site is provided by a hydrophobic tunnel in the C-terminal domain. The unusually large interacting surface area between the two domains may contribute to thermostability of the enzyme. Two amino acids, Asp61 and Lys101, are identified as hinge residues regulating movement of the lid domain. The hydrogen-bonding pattern associated with these two residues is pH dependent, which may account for the optimal enzyme activity at high pH. Further engineering of this novel lipase with high temperature and alkaline stability will find its use in industrial applications.
Title: Homology modeling and identification of serine 160 as nucleophile of the active site in a thermostable carboxylesterase from the archaeon Archaeoglobus fulgidus Manco G, Camardella L, Febbraio F, Adamo G, Carratore V, Rossi M Ref: Protein Engineering, 13:197, 2000 : PubMed
The hyperthermophilic Archaeon Archaeoglobus fulgidus has a gene (AF1763) which encodes a thermostable carboxylesterase belonging to the hormone-sensitive lipase (HSL)-like group of the esterase/lipase family. Based on secondary structure predictions and a secondary structure-driven multiple sequence alignment with remote homologous proteins of known three-dimensional structure, we previously hypothesized for this enzyme the alpha/beta-hydrolase fold typical of several lipases and esterases and identified Ser160, Asp 255 and His285 as the putative members of the catalytic triad. In this paper we report the building of a 3D model for this enzyme based on the structure of the homologous brefeldin A esterase from Bacillus subtilis whose structure has been recently elucidated. The model reveals the topological organization of the fold corroborating our predictions. As regarding the active-site residues, Ser160, Asp255 and His285 are located close each other at hydrogen bond distances. The catalytic role of Ser160 as the nucleophilic member of the triad is demonstrated by the [(3)H]diisopropylphosphofluoridate (DFP) active-site labeling and sequencing of a radioactive peptide containing the signature sequence GDSAGG.
Archaeoglobus fulgidus is the first sulphur-metabolizing organism to have its genome sequence determined. Its genome of 2,178,400 base pairs contains 2,436 open reading frames (ORFs). The information processing systems and the biosynthetic pathways for essential components (nucleotides, amino acids and cofactors) have extensive correlation with their counterparts in the archaeon Methanococcus jannaschii. The genomes of these two Archaea indicate dramatic differences in the way these organisms sense their environment, perform regulatory and transport functions, and gain energy. In contrast to M. jannaschii, A. fulgidus has fewer restriction-modification systems, and none of its genes appears to contain inteins. A quarter (651 ORFs) of the A. fulgidus genome encodes functionally uncharacterized yet conserved proteins, two-thirds of which are shared with M. jannaschii (428 ORFs). Another quarter of the genome encodes new proteins indicating substantial archaeal gene diversity.
Archaeoglobus fulgidus AF1763 gene, putative lipase or thermostable carboxylesterase
