ID   GUNB_CALSA              Reviewed;        1039 AA.
AC   P10474;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   24-JAN-2024, entry version 120.
DE   RecName: Full=Endoglucanase/exoglucanase B;
DE   Includes:
DE     RecName: Full=Endoglucanase;
DE              EC=3.2.1.4;
DE     AltName: Full=Cellobiohydrolase;
DE     AltName: Full=Cellulase;
DE     AltName: Full=Endo-1,4-beta-glucanase;
DE   Includes:
DE     RecName: Full=Exoglucanase;
DE              EC=3.2.1.91;
DE     AltName: Full=1,4-beta-cellobiohydrolase;
DE     AltName: Full=Exocellobiohydrolase;
DE   Flags: Precursor;
GN   Name=celB;
OS   Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum).
OC   Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC   Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX   NCBI_TaxID=44001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2789517; DOI=10.1093/nar/17.1.439;
RA   Saul D.J., Williams L.C., Love D.R., Chamley L.W., Bergquist P.L.;
RT   "Nucleotide sequence of a gene from Caldocellum saccharolyticum encoding
RT   for exocellulase and endocellulase activity.";
RL   Nucleic Acids Res. 17:439-439(1989).
CC   -!- FUNCTION: This protein is made up of two domains: the N-terminal domain
CC       has exoglucanase activity while the C-terminal domain is an
CC       endoglucanase.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC         and cellotetraose, releasing cellobiose from the non-reducing ends of
CC         the chains.; EC=3.2.1.91;
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glycosyl
CC       hydrolase 10 (cellulase F) family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC       hydrolase 5 (cellulase A) family. {ECO:0000305}.
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DR   EMBL; X13602; CAA31936.1; -; Genomic_DNA.
DR   PIR; S02711; S02711.
DR   AlphaFoldDB; P10474; -.
DR   SMR; P10474; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   BRENDA; 3.2.1.4; 1055.
DR   BRENDA; 3.2.1.91; 1055.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM01067; CBM_3; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   PROSITE; PS51172; CBM3; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Multifunctional enzyme; Polysaccharide degradation; Repeat; Signal.
FT   SIGNAL          1..28
FT   CHAIN           29..1039
FT                   /note="Endoglucanase/exoglucanase B"
FT                   /id="PRO_0000007983"
FT   DOMAIN          39..372
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   DOMAIN          418..571
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   REGION          375..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..413
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..616
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        177
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        285
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   ACT_SITE        792
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1039 AA;  117641 MW;  0E0378171594DDAE CRC64;
     MKRNLFRIVS RVVLIAFIAS ISLVGAMSYF PVETQAAPDW SIPSLCESYK DDFMIGVAIP
     ARCLSNDTDK RMVLKHFNSI TAENEMKPES LLAGQTSTGL SYRFSTADAF VDFASTNKIG
     IRGHTLVWHN QTPDWFFKDS NGQRLSKDAL LARLKQYIYD VVGRYKGKVY AWDVVNEAID
     ENQPDSYRRS TWYEICGPEY IEKAFIWAHE ADPNAKLFYN DYNTEISKKR DFIYNMVKNL
     KSKGIPIHGI GMQCHINVNW PSVSEIENSI KLFSSIPGIE IHITELDMSL YNYGSSENYS
     TPPQDLLQKQ SQKYKEIFTM LKKYKNVVKS VTFWGLKDDY SWLRSFYGKN DWPLLFFEDY
     SAKPAYWAVI EASGVTTSSP TPTPTPTVTV TPTPTPTPTP TVTATPTPTP TPVSTPATGG
     QIKVLYANKE TNSTTNTIRP WLKVVNSGSS SIDLSRVTIR YWYTVDGERA QSAVSDWAQI
     GASNVTFKFV KLSSSVSGAD YYLEIGFKSG AGQLQPGKDT GEIQIRFNKS DWSNYNQGND
     WSWLQSMTSY GENEKVTAYI DGVLVWGQEP SGATPAPTMT VAPTATPTPT LSPTVTPTPA
     PTQTAIPTPT LTPNPTPTSS IPDDTNDDWL YVSGNKIVDK DGRPVWLTGI NWFGYNTGTN
     VFDGVWSCNL KDTLAEIANR GFNLLRVPIS AELILNWSQG IYPKPNINYY VNPELEGKNS
     LEVFDIVVQT CKEVGLKIML DIHSIKTDAM GHIYPVWYDE KFTPEDFYKA CEWITNRYKN
     DDTIIAFDLK NEPHGKPWQD TTFAKWDNST DINNWKYAAE TCAKRILNIN PNLLIVIEGI
     EAYPKDDVTW TSKSSSDYYS TWWGGNLRGV RKYPINLGKY QNKVVYSPHD YGPSVYQQPW
     FYPGFTKESL LQDCWRPNWA YIMEENIAPL LIGEWGGHLD GADNEKWMKY LRDYIIENHI
     HHTFWCFNAN SGDTGGLVGY DFTTWDEKKY SFLKPALWQD SQGRFVGLDH KRPLGTNGKN
     INITTYYNNN EPEPVPASK
//