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Gene_locus Report for: clotm-xyny

Clostridium thermocellum (strains DSM 2360; JW20; ATCC 27405 / DSM 1237) Feruloyl Esterase Domain (1,4-beta-d-xylan xylanohydrolase y)

Comment
The 297 last aa of (1,4-beta-d-xylan xylanohydrolase y) correspond to the feruloyl domain and is an alpha/beta-fold structure (here the modules CBM_4_9, Glyco_hydro_10, CBM_4_9 and Dockerin_1 are excluded). Structure solution revealed an error in the deposited sequence. Residues 1017 and 1018, Asp-His in the deposited sequence, were corrected to Glu-Asp The Asp is in the catalytic triad the numbering from only the esterase portion is S166 (954) H270 (1058) D230 (1018) structure 1ohz has only a fragment outside the domain


Relationship
Family|A85-Feruloyl-Esterase
Block| X
Position in NCBI Life Tree|Clostridium thermocellum
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Bacteria: N E > Terrabacteria group: N E > Firmicutes: N E > Clostridia: N E > Clostridiales: N E > Ruminococcaceae: N E > Ruminiclostridium: N E > Ruminiclostridium thermocellum: N E
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data


Molecular evidence
Database
1 mutation: clotm-xyny
12 structures (e.g. : 1GKK, 1GKL, 1WB4... more)
No kinetic





3 substrates: Methyl-sinapate, Methyl-syringate, Methyl-vanillate
No inhibitor
>3 Genbank links 1 more: X83269, ACVX01000012, ABVG02000001
2 UniProt : P51584, A3DDW7
>3 Structure links 9 more: 6Y8G, 6SWW, 6FJ4
2 UniProt : P51584, A3DDW7
2 Interpro : P51584, A3DDW7
2 Prodom : P51584, A3DDW7
2 Pfam : P51584, A3DDW7
2 PIRSF : P51584, A3DDW7
2 SUPERFAM : P51584, A3DDW7
Sequence
Graphical view for this peptide sequence: clotm-xyny
Colored MSA for A85-Feruloyl-Esterase (raw)
MASDKFPVAENPSSSFKYESAVQYRPAPDSYLNPCPQAGRIVKETYTGIN
GTKSLNVYLPYGYDPNKKYNIFYLMHGGGENENTIFSNDVKLQNILDHAI
MNGELEPLIVVTPTFNGGNCTAQNFYQEFRQNVIPFVESKYSTYAESTTP
QGIAASRMHRGFGGFSMGGLTTWYVMVNCLDYVAYFMPLSGDYWYGNSPQ
DKANSIAEAINRSGLSKREYFVFAATGSEDIAYANMNPQIEAMKALPHFD
YTSDFSKGNFYFLVAPGATHWWGYVRHYIYDALPYFFHE
Legend This 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

MASDKFPVAENPSSSFKYESAVQYRPAPDSYLNPCPQAGRIVKETYTGIN
GTKSLNVYLPYGYDPNKKYNIFYLMHGGGENENTIFSNDVKLQNILDHAI
MNGELEPLIVVTPTFNGGNCTAQNFYQEFRQNVIPFVESKYSTYAESTTP
QGIAASRMHRGFGGFSMGGLTTWYVMVNCLDYVAYFMPLSGDYWYGNSPQ
DKANSIAEAINRSGLSKREYFVFAATGSEDIAYANMNPQIEAMKALPHFD
YTSDFSKGNFYFLVAPGATHWWGYVRHYIYDALPYFFHE


References
5 more
    Title: ID30A-3 (MASSIF-3) - a beamline for macromolecular crystallography at the ESRF with a small intense beam
    von Stetten D, Carpentier P, Flot D, Beteva A, Caserotto H, Dobias F, Guijarro M, Giraud T, Lentini M and Mueller-Dieckmann C <8 more author(s)>
    Ref: J Synchrotron Radiat, 27:844, 2020 : PubMed

            

    Title: RoboDiff: combining a sample changer and goniometer for highly automated macromolecular crystallography experiments
    Nurizzo D, Bowler MW, Caserotto H, Dobias F, Giraud T, Surr J, Guichard N, Papp G, Guijarro M and Leonard GA <5 more author(s)>
    Ref: Acta Crystallographica D Struct Biol, 72:966, 2016 : PubMed

            

    Title: Evidence for a general role for non-catalytic thermostabilizing domains in xylanases from thermophilic bacteria.
    Fontes CM, Hazelwood GP, Morag E, Hall J, Hirst BH, Gilbert HJ
    Ref: Biochemical Journal, 307:151, 1995 : PubMed

            


Other Papers


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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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