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Database: UniProt
Entry: P10474
LinkDB: P10474
Original site: P10474 
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   23-MAY-2018, entry version 108.
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;
OC   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
RT   encoding 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
CC       domain has exoglucanase activity while the C-terminal domain is an
CC       endoglucanase.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-D-glucosidic
CC       linkages in cellulose and cellotetraose, releasing cellobiose from
CC       the non-reducing ends of the chains.
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}.
DR   EMBL; X13602; CAA31936.1; -; Genomic_DNA.
DR   PIR; S02711; S02711.
DR   ProteinModelPortal; 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   PRIDE; P10474; -.
DR   eggNOG; ENOG4105CYP; Bacteria.
DR   eggNOG; COG2730; LUCA.
DR   eggNOG; COG3693; LUCA.
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; IPR001000; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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;
KW   Hydrolase; Multifunctional enzyme; Polysaccharide degradation; Repeat;
KW   Signal.
FT   SIGNAL        1     28
FT   CHAIN        29   1039       Endoglucanase/exoglucanase B.
FT                                /FTId=PRO_0000007983.
FT   DOMAIN       39    372       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   DOMAIN      418    571       CBM3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00513}.
FT   COMPBIAS    376    416       Pro/Thr-rich.
FT   COMPBIAS    574    618       Pro/Thr-rich.
FT   ACT_SITE    177    177       Proton donor. {ECO:0000255}.
FT   ACT_SITE    285    285       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10061}.
FT   ACT_SITE    792    792       {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
//
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