ID   XYN2_RHIOR              Reviewed;         216 AA.
AC   W0HJ53;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Endo-1,4-beta-xylanase 2;
DE            Short=Xylanase 2;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 2;
DE   Flags: Precursor;
GN   Name=xyn2;
OS   Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=64495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-36, SUBCELLULAR
RP   LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=24760228; DOI=10.1007/s00253-014-5741-4;
RA   Xiao Z., Grosse S., Bergeron H., Lau P.C.;
RT   "Cloning and characterization of the first GH10 and GH11 xylanases from
RT   Rhizopus oryzae.";
RL   Appl. Microbiol. Biotechnol. 98:8211-8222(2014).
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. {ECO:0000269|PubMed:24760228}.
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:24760228};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.2 mg/ml for birchwood xylan {ECO:0000269|PubMed:24760228};
CC       pH dependence:
CC         Optimum pH is 5.0-6.0. {ECO:0000269|PubMed:24760228};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.
CC         {ECO:0000269|PubMed:24760228};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24760228}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; KF640267; AHF72524.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0HJ53; -.
DR   SMR; W0HJ53; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11A_RHIOR; -.
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   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 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; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:24760228"
FT   CHAIN           28..216
FT                   /note="Endo-1,4-beta-xylanase 2"
FT                   /id="PRO_0000429748"
FT   DOMAIN          28..216
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        112
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   216 AA;  23261 MW;  D03734950C4B2116 CRC64;
     MVSFSSLFVA ACAAVTAFAL PNELEKRAIT SNEQGTNNGY FYSFWTNGGG SVSYNNGAAG
     QYSVNWKDCG SFTSGKGWAT GSARNINFSG SFNPSGNAYL AVYGWTTSPL VEYYIMENYG
     EYNPGSSMAH KGTVTSDGSV YDIYAHQQVN QPSIVGTATF NQYWSIRRNK RSSGTVTTAN
     HFNAWSRLGM GLGSHNYQIV NTEGYQSSGS ASITVS