ID   GUNB_NEOPA              Reviewed;         473 AA.
AC   Q12647;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Endoglucanase B;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase B;
DE   AltName: Full=Endo-1,4-beta-glucanase B;
DE   Flags: Precursor;
GN   Name=CELB;
OS   Neocallimastix patriciarum (Rumen fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=4758;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8297343; DOI=10.1042/bj2970359;
RA   Zhou L., Xue G., Orpin C.G., Black G.W., Gilbert H.J., Hazlewood G.P.;
RT   "Intronless celB from the anaerobic fungus Neocallimastix patriciarum
RT   encodes a modular family A endoglucanase.";
RL   Biochem. J. 297:359-364(1994).
CC   -!- FUNCTION: Rate of hydrolysis of cellulo-oligosaccharides increased with
CC       increasing chain length from cellotriose to cellopentaose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; Z31364; CAA83238.1; -; mRNA.
DR   PIR; S40507; S40507.
DR   AlphaFoldDB; Q12647; -.
DR   SMR; Q12647; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   CLAE; EGL5B_NEOPA; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1220.10; -; 2.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR009034; Dockerin_dom_fun_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02013; CBM_10; 2.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF64571; SSF64571; 2.
DR   PROSITE; PS51763; CBM10; 2.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Repeat; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..473
FT                   /note="Endoglucanase B"
FT                   /id="PRO_0000007864"
FT   DOMAIN          391..427
FT                   /note="CBM10 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   DOMAIN          436..473
FT                   /note="CBM10 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   REGION          18..367
FT                   /note="Catalytic"
FT   REGION          365..387
FT                   /note="Linker"
FT   ACT_SITE        173
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        295
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   473 AA;  53070 MW;  B11D9F171EA33199 CRC64;
     MKFLNTFSLL SLAIIGSKAM KNISSKELVK DLTIGWSLGN TLDATCFETL DYNKNQIASE
     TCWGNVKTTQ ELYYKLSDLG FNTFRIPTTW SGHFGNAPDY KINDQWMKRV HEIVDYAINT
     GGYAILNIHH ETWNHAFQKN LESAKKILVA IWKQIAAEFA DYDEHLIFEG MNEPRKVGDP
     AEWNGGDYEG WNFVNEMNDL FVKTIRATGG NNALRHLMIP TYAACINDGA INNFKFPSGD
     DKVIVSLHSY SPYNFALNNG AGAISNFYDG SEIDWAMNTI NSKFISRGIP VIIGEFGAMN
     RNNEDDRERW AEYYIKKATS IGVPCVIWDN GYFEGEGERF GLINRSTLQV VYPKLVNGLI
     KGLGNSIKTR TTIRRTTTTT TSQSQPTNND SCFSVNLGYS CCNGCEVEYT DSDGEWGVEN
     GNWCGIKSSC SNTSRICWSE KLGYPCCQNT SSVVYTDNDG KWGVENGNWC GIY