ID   XYN1_RHIOR              Reviewed;         331 AA.
AC   W0HFK8;
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 1;
DE            Short=Xylanase 1;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 1;
DE   Flags: Precursor;
GN   Name=xyn1;
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 147-158; 195-206 AND
RP   218-229, SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND
RP   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=11 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 40 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 10 (cellulase F) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KF640266; AHF72523.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0HFK8; -.
DR   SMR; W0HFK8; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10A_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   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; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 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   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..331
FT                   /note="Endo-1,4-beta-xylanase 1"
FT                   /id="PRO_0000429747"
FT   DOMAIN          50..330
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        161
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        267
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   DISULFID        285..291
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  35472 MW;  7DB6ABF17AB4C63E CRC64;
     MIPNITQLKT AALVMLFAGQ ALSGPVESRQ ASESIDAKFK AHGKKYLGNI ADQGTLNGNP
     KTPAIIKANF GQLSPENSMK WDATEPSQGQ FSFAGSDYFV EFAETNGKLI RGHTLVWHSQ
     LPSWVSSITD KTTLTDVMKN HITTVMKQYK GKVYAWDVVN EIFEEDGTLR DSVFSRVLGE
     DFVRIAFETA READPEAKLY INDYNLDSAT SAKLQGMVSH VKKWIAAGVP IDGIGSQTHL
     GAGAGAAASG SLNALASAGT EEVAVTELDI AGASSTDYVD VVNACLDQPK CVGITVWGVA
     DPDSWRADES PLLFDASYNP KEAYNAIAAA L