ID XYNA_SCHCO Reviewed; 197 AA.
AC P35809;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 24-JAN-2024, entry version 102.
DE RecName: Full=Endo-1,4-beta-xylanase A;
DE Short=Xylanase A;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
GN Name=XYNA;
OS Schizophyllum commune (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=5334;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 38548 / Delmar / 13 / IHEM 5263;
RA Yaguchi M., Roy C., Ujiie M., Watson D.C., Wakarchuk W.;
RL (In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J.
RL (eds.);
RL Xylans and xylanases, pp.149-154, Elsevier, Amsterdam (1992).
RN [2]
RP PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RC STRAIN=ATCC 38548 / Delmar / 13 / IHEM 5263;
RX PubMed=8243636; DOI=10.1016/0014-5793(93)80698-t;
RA Oku T., Roy C., Watson D.C., Wakarchuk W., Campbell R., Yaguchi M.,
RA Jurasek L., Paice M.G.;
RT "Amino acid sequence and thermostability of xylanase A from Schizophyllum
RT commune.";
RL FEBS Lett. 334:296-300(1993).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND ACTIVE SITE GLU-87.
RC STRAIN=ATCC 38548 / Delmar / 13 / IHEM 5263;
RX PubMed=7906649; DOI=10.1111/j.1432-1033.1994.tb18563.x;
RA Bray M.R., Clarke A.J.;
RT "Identification of a glutamate residue at the active site of xylanase A
RT from Schizophyllum commune.";
RL Eur. J. Biochem. 219:821-827(1994).
CC -!- FUNCTION: Hydrolyzes xylans into xylobiose and xylose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active over a very broad pH range.;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR PIR; A44597; A44597.
DR AlphaFoldDB; P35809; -.
DR SMR; P35809; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11A_SCHCO; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02612721; -.
DR BRENDA; 3.2.1.8; 5611.
DR UniPathway; UPA00114; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033119; GH11_AS_2.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS00777; GH11_2; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW Xylan degradation.
FT CHAIN 1..197
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000184071"
FT DOMAIN 1..197
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:7906649"
FT ACT_SITE 184
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT DISULFID 111..160
FT /evidence="ECO:0000269|PubMed:8243636"
SQ SEQUENCE 197 AA; 20979 MW; 42C8074E67C1FBE9 CRC64;
SGTPSSTGTD GGYYYSWWTD GAGDATYQNN GGGSYTLTWS GNNGNLVGGK GWNPGAASRS
ISYSGTYQPN GNSYLSVYGW TRSSLIEYYI VESYGSYDPS SAASHKGSVT CNGATYDILS
TWRYNAPSID GTQTFEQFWS VRNPKKAPGG SISGTVDVQC HFDAWKGLGM NLGSEHNYQI
VATEGYQSSG TATITVT
//
