XYND_TALFU
ID XYND_TALFU Reviewed; 407 AA.
AC Q5ZNB1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Endo-1,4-beta-xylanase D;
DE Short=Xylanase D;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase D;
DE Flags: Precursor;
GN Name=xynD;
OS Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium
OS funiculosum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=28572;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 186-199 AND 217-235,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=IMI 134756;
RX AGRICOLA=IND43674834;
RA Furniss C.S.M., Williamson G., Kroon P.A.;
RT "The substrate specificity and susceptibility to wheat inhibitor proteins
RT of Penicillium funiculosum xylanases from a commercial enzyme
RT preparation.";
RL J. Sci. Food Agric. 85:574-582(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21466666; DOI=10.1186/1475-2859-10-20;
RA Lafond M., Tauzin A., Desseaux V., Bonnin E., Ajandouz E.L.-H.,
RA Giardina T.;
RT "GH10 xylanase D from Penicillium funiculosum: biochemical studies and
RT xylooligosaccharide production.";
RL Microb. Cell Fact. 10:20-20(2011).
CC -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a
CC major structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose. Shows an endo-mode of action on xylan forming mainly
CC xylobiose and short-chain xylooligosaccharides (XOS).
CC {ECO:0000269|PubMed:21466666}.
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:21466666,
CC ECO:0000269|Ref.1};
CC -!- ACTIVITY REGULATION: Inhibited by wheat xylanase inhibiting protein I
CC (XIP-I). {ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 mg/ml for birchwood xylan {ECO:0000269|PubMed:21466666,
CC ECO:0000269|Ref.1};
CC KM=11 mg/ml for insoluble fractions of wheat arabinoxylans
CC {ECO:0000269|PubMed:21466666, ECO:0000269|Ref.1};
CC Vmax=130 umol/min/mg enzyme toward birchwood xylan
CC {ECO:0000269|PubMed:21466666, ECO:0000269|Ref.1};
CC Vmax=535 umol/min/mg enzyme toward insoluble fractions of wheat
CC arabinoxylans {ECO:0000269|PubMed:21466666, ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 4.2-5.2 for birchwood xylan and 4.0 for CM cellulose.
CC {ECO:0000269|PubMed:21466666, ECO:0000269|Ref.1};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; AJ634957; CAG25554.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5ZNB1; -.
DR SMR; Q5ZNB1; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR CLAE; XYN10D_PENFN; -.
DR BRENDA; 3.2.1.8; 4616.
DR UniPathway; UPA00114; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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 InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00236; fCBD; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..407
FT /note="Endo-1,4-beta-xylanase D"
FT /id="PRO_5000072571"
FT DOMAIN 20..333
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT DOMAIN 371..407
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 337..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 283..289
FT /evidence="ECO:0000250"
SQ SEQUENCE 407 AA; 43235 MW; 104AF7A4A339459C CRC64;
MTLVKSILLA LAAGHVAQAQ LNTAAKAAGL LYFGTAVDNP DLSDSKYLVN LETADFGQIT
PANAMKWQPT EPSQGSYTFT QGDQIASLAK SNNDYLRCHN LVWYNQLPSY ITSGSWTNAT
LIAALKEHIN GVVTHYKGQC YAWDVVNEAL NEDGTYRQNV FYQHIGEAYI PIAFAAAAAA
DPNAKLYYND YNIEYAGAKA TGAQGIVKLI QAAGGRIDGV GLQSHFIVGQ TPSLATQKAN
MAAFTALGVD VAITELDIRM TLPDTSALQT QQSTDYQTTT TACVQTKGCV GITLWDYTDK
YSWVPGTFSG QGDACPWDSN YNKKPAYYGI LAGLQSGSGS SSSTSSTTLI TTTTPTASSS
TTSATTTSAT SGAAHWGQCG GIGWSGPTIC VSPYTCQVLN PYYSQCL
