GUNB_CALSA
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 25-MAY-2022, entry version 116.
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; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; 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; -; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR044846; GH10.
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; PTHR31490; PTHR31490; 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; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51445; SSF51445; 2.
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
