ID   GUB_ORPSP               Reviewed;         245 AA.
AC   O14412;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Beta-glucanase;
DE            EC=3.2.1.73;
DE   AltName: Full=1,3-1,4-beta-D-glucan 4-glucanohydrolase;
DE   AltName: Full=Endo-beta-1,3-1,4 glucanase;
DE   AltName: Full=Lichenase;
DE   Flags: Precursor;
GN   Name=licA;
OS   Orpinomyces sp. (strain PC-2).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Orpinomyces; unclassified Orpinomyces.
OX   NCBI_TaxID=50059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 30-41.
RX   PubMed=9324248; DOI=10.1128/jb.179.19.6028-6034.1997;
RA   Chen H., Li X.-L., Ljungdahl L.G.;
RT   "Sequencing of a 1,3-1,4-beta-D-glucanase (lichenase) from the anaerobic
RT   fungus Orpinomyces strain PC-2: properties of the enzyme expressed in
RT   Escherichia coli and evidence that the gene has a bacterial origin.";
RL   J. Bacteriol. 179:6028-6034(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-
CC         glucans containing (1->3)- and (1->4)-bonds.; EC=3.2.1.73;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.8-6.2.;
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR   EMBL; U63813; AAD04192.1; -; mRNA.
DR   AlphaFoldDB; O14412; -.
DR   SMR; O14412; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   CLAE; LIC16A_ORPSP; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042972; F:licheninase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR044791; Beta-glucanase/XTH.
DR   InterPro; IPR008264; Beta_glucanase.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   PANTHER; PTHR31062; PTHR31062; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   PRINTS; PR00737; GLHYDRLASE16.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:9324248"
FT   CHAIN           30..245
FT                   /note="Beta-glucanase"
FT                   /id="PRO_0000011795"
FT   DOMAIN          30..245
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        134
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        138
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        63..90
FT                   /evidence="ECO:0000250"
FT   CONFLICT        36
FT                   /note="S -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   245 AA;  27929 MW;  08B5DF57D89F2DCC CRC64;
     MKSIISIAAL SVLGLISKTM AAPAPAPVPG TAWNGSHDVM DFNYHESNRF EMSNWPNGEM
     FNCRWTPNND KFENGKLKLT IDRDGSGYTC GEYRTKNYYG YGMFQVNMKP IKNPGVVSSF
     FTYTGPSDGT KWDEIDIEFL GYDTTKVQFN YYTNGQGHHE HIHYLGFDAS QGFHTYGFFW
     ARNSITWYVD GTAVYTAYDN IPDTPGKIMM NAWNGIGVDD WLRPFNGRTN ISAYYDWVSY
     DAPRN