ID   XS20E_NEOPA             Reviewed;         671 AA.
AC   B8YG19;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Bifunctional acetylxylan esterase/xylanase XynS20E;
DE   Includes:
DE     RecName: Full=Acetylxylan esterase;
DE              EC=3.1.1.72;
DE   Includes:
DE     RecName: Full=Endo-1,4-beta-xylanase;
DE              Short=Xylanase;
DE              EC=3.2.1.8;
DE     AltName: Full=1,4-beta-D-xylan xylanohydrolase;
DE   Flags: Precursor;
GN   Name=xynS20E;
OS   Neocallimastix patriciarum (Rumen fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=4758;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION, CATALYTIC
RP   ACTIVITY, AND BIOPHISICOCHEMICAL PROPERTIES.
RC   STRAIN=S20;
RX   PubMed=19690850; DOI=10.1007/s00253-009-2175-5;
RA   Pai C.K., Wu Z.Y., Chen M.J., Zeng Y.F., Chen J.W., Duan C.H., Li M.L.,
RA   Liu J.R.;
RT   "Molecular cloning and characterization of a bifunctional xylanolytic
RT   enzyme from Neocallimastix patriciarum.";
RL   Appl. Microbiol. Biotechnol. 85:1451-1462(2010).
CC   -!- FUNCTION: Bifunctional acetylxylan esterase/xylanase involved in the
CC       hydrolysis of xylan, a major structural heterogeneous polysaccharide
CC       found in plant biomass representing the second most abundant
CC       polysaccharide in the biosphere, after cellulose. Degrades xylan from
CC       acetylxylan, beechwood, birchwood, and oat spelt, and releases acetate
CC       from 4-methylumbelliferyl acetate and beta-D-xylose tetraacetate. No
CC       activity is observed against carboxy methyl cellulose, beta-glucan, p-
CC       nitrophenol acetate, p-nitrophenol laurate, p-nitrophenol myristate, p-
CC       nitrophenol, palmitate, or beta-naphthol acetate.
CC       {ECO:0000269|PubMed:19690850}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC         EC=3.1.1.72; Evidence={ECO:0000269|PubMed:19690850};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000269|PubMed:19690850};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.48 mg/ml for birchwood xylan for endo-1,4-beta-xylanase
CC         activity;
CC         KM=16.72 mg/ml for birchwood xylan for acetylxylan esterase activity;
CC         Vmax=5.15 umol/min/mg enzyme toward birchwood xylan for acetylxylan
CC         esterase activity;
CC         Vmax=153.27 umol/min/mg enzyme toward birchwood xylan for Endo-1,4-
CC         beta-xylanase activity;
CC       pH dependence:
CC         Optimum pH is 5.8 for acetylxylan esterase activity, and 5.8 for
CC         endo-1,4-beta-xylanase activity.;
CC       Temperature dependence:
CC         Optimum temperature is 58 degrees Celsius for acetylxylan esterase
CC         activity, and 49 degrees Celsius for endo-1,4-beta-xylanase
CC         activity.;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19690850}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the axeA family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC       hydrolase 11 (cellulase G) family. {ECO:0000305}.
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DR   EMBL; FJ529209; ACL68347.1; -; mRNA.
DR   AlphaFoldDB; B8YG19; -.
DR   SMR; B8YG19; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; ZXA11E_NEOPA; -.
DR   BRENDA; 3.1.1.72; 6834.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   Gene3D; 3.90.1220.10; -; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR009034; Dockerin_dom_fun_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR003140; PLipase/COase/thioEstase.
DR   Pfam; PF02230; Abhydrolase_2; 1.
DR   Pfam; PF02013; CBM_10; 2.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF64571; SSF64571; 2.
DR   PROSITE; PS51763; CBM10; 2.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Repeat; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..671
FT                   /note="Bifunctional acetylxylan esterase/xylanase XynS20E"
FT                   /id="PRO_0000429665"
FT   DOMAIN          335..374
FT                   /note="CBM10 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   DOMAIN          383..422
FT                   /note="CBM10 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   DOMAIN          461..661
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   REGION          54..279
FT                   /note="Acetylxylan esterase"
FT   REGION          285..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        152
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        555
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        648
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   671 AA;  72469 MW;  EC02F1D1A775640D CRC64;
     MRLGVALSTI AVLLTATSAR NLDKRQWGWP NFGGGNGGNG GNGGKTINDY KREQGAGRDI
     HVYAPSNLAP NSPLLLSLHG MDQDPNYQQS NTHWETLADS EGFVVVYPRG GTGMSTWDIQ
     GTKDTQWVSQ IIDQMKKEYN IDTKRVYLSG FSMGGMFTYH AMSQIANKIA AFAPCSGPNV
     FGASKAQRPV PIFHVHGTND DVLNYQQVEG FLKNYRDQFH CPSQADTKTN YPNRENPNAT
     LYTWGPCDKG VYIKHLKLQG RGHSPSSADI QDIWDFVSQW TVDGPVSASG NGGGNTTPTN
     PSTGGNGNGN GGGNTTPTNP STGGNGNGNG GSTDKCSSNI TKQGYKCCAS NCEVVYTDSD
     GDWGVENDQW CGCGNRVTVG SGTCSAKILQ QGYKCCPSGC IIYYTDEDGT WGVNGEEWCG
     CGSGSSSTGG GNDAPSSGSG YQGANGTNFC NNAKHSGESV TVTSNKVGDI NGIGYELWAD
     SGNNSATFYD DGSFSCSFQR AKDYLCRSGL SFDSTKTHKQ IGHIYAEFKL VKQNIQNVDY
     SYVGIYGWTR NPLVEFYVVD NWLSQWRPGD WVGNKKHGDF TIGGAQYTVY ENTRYGPSID
     GDTNFKQYFS IRQQPRDCGT IDITAHFEQW EKLGMTMGKM HEAKVLGEAG SNNGGTSGTA
     DFPFAKVYVK N