ID   GUNB_CELFI     STANDARD;      PRT;  1045 AA.
AC   P26225;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   21-MAR-2006, entry version 53.
DE   Endoglucanase B precursor (EC 3.2.1.4) (Endo-1,4-beta-glucanase B)
DE   (Cellulase B).
GN   Name=cenB;
OS   Cellulomonas fimi.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=1708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91100298; PubMed=1987122;
RA   Meinke A., Braun C., Gilkes N.R., Kilburn D.G., Miller R.C. Jr.,
RA   Warren R.A.J.;
RT   "Unusual sequence organization in CenB, an inverting endoglucanase
RT   from Cellulomonas fimi.";
RL   J. Bacteriol. 173:308-314(1991).
RN   [2]
RP   DOMAINS.
RX   MEDLINE=92041609; PubMed=1938913;
RA   Meinke A., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.;
RT   "Multiple domains in endoglucanase B (CenB) from Cellulomonas fimi:
RT   functions and relatedness to domains in other polypeptides.";
RL   J. Bacteriol. 173:7126-7135(1991).
CC   -!- FUNCTION: The biological conversion of cellulose to glucose
CC       generally requires three types of hydrolytic enzymes: (1)
CC       Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2)
CC       Exocellobiohydrolases that cut the dissaccharide cellobiose from
CC       the nonreducing end of the cellulose polymer chain; (3)
CC       Beta-1,4-glucosidases which hydrolyze the cellobiose and other
CC       short cello-oligosaccharides to glucose.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC   -!- DOMAIN: The linker region (also termed "hinge") may be a potential
CC       site for proteolysis.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E)
CC       family.
CC   -!- SIMILARITY: Contains 1 CBM2 (carbohydrate binding type-2) domain.
CC   -!- SIMILARITY: Contains 1 CBM3 (carbohydrate binding type-3) domain.
CC   -!- SIMILARITY: Contains 3 fibronectin type-III domains.
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DR   EMBL; M64644; AAA23086.1; -; Genomic_DNA.
DR   PIR; A39199; A39199.
DR   HSSP; P26221; 1TF4.
DR   InterPro; IPR008928; 6hp_glycosidase.
DR   InterPro; IPR008965; Carb_bd.
DR   InterPro; IPR001956; CBD_3.
DR   InterPro; IPR001919; CBD_bac.
DR   InterPro; IPR012291; CBD_carb_bd.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR008957; FN_III-like.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR012343; Glyco_trans_sub.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   ProDom; PD001947; CBD_3; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00060; FN3; 3.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS51172; CBM3; 1.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS00592; GLYCOSYL_HYDROL_F9_1; 1.
DR   PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2; 1.
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Repeat; Signal.
FT   SIGNAL        1     33       Potential.
FT   CHAIN        34   1045       Endoglucanase B.
FT                                /FTId=PRO_0000007945.
FT   DOMAIN      493    642       CBM3.
FT   DOMAIN      650    740       Fibronectin type-III 1.
FT   DOMAIN      748    837       Fibronectin type-III 2.
FT   DOMAIN      847    937       Fibronectin type-III 3.
FT   DOMAIN      939   1045       CBM2.
FT   REGION       34    643       Catalytic.
FT   REGION      644    650       Linker ("hinge") (Pro-Thr box).
FT   REGION      734    748       Linker ("hinge") (Pro-Thr box).
FT   REGION      831    846       Linker ("hinge") (Pro-Thr box).
FT   REGION      931    944       Linker ("hinge") (Pro-Thr box).
FT   ACT_SITE    410    410       By similarity.
FT   ACT_SITE    449    449       By similarity.
FT   ACT_SITE    458    458       By similarity.
FT   DISULFID    946   1044       By similarity.
SQ   SEQUENCE   1045 AA;  108991 MW;  AC2F7B84E4E3C4F0 CRC64;
     MLRQVPRTLV AGGSALAVAV GVLVAPLATG AAAAPTYNYA EALQKSMFFY QAQRSGDLPA
     DFPVSWRGDS GLTDGADVGK DLTGGWYDAG DHVKFGFPMA FSATMLAWGA IESPTGYSKA
     GSLDELKDNL RFVSDYFVKA HTAPNELYVQ VGDGEADHKW WGPAEVMTMA RPSHKISASC
     PGSDVAAETA AALASSAIVL KGDDPAYAAT LVSHAKQLYT FADTYRGAYS DCVTAASAYY
     KSWSGYQDEL VWGAYWLYKA TGDATYLAKA EAEYDKLGTE NQSTTRSYKW TIAWDNKQFG
     TYALLAMETG KQKYVDDANR WLDYWTVGVN GQKVPYSPGG QAVLDSWGAL RYAANTSFVA
     LVYSDWMTDA TRKARYHDFG VRQINYALGD NPRSSSYVVG FGANPPTAPH HRTAHGSWLD
     SITTPAQSRH VLYGALVGGP GSPNDAYTDS RQDYVANEVA TDYNAGFTSA LARLVEEYGG
     TPLASFPTPE QPDGDQLFVE AMLNQPPSGT FTEVKAMIRN QSAFPARSLK NAKVRYWFTT
     DGFAASDVTL SANYSECGAQ SGKGVSAGGT LGYVELSCVG QDIHPGGQSQ HRREIQFRLT
     GPAGWNPAND PSYTGLTQTA LAKASAITLY DGSTLVWGKE PTGTTTDTTP PTTPGTPVAT
     GVTTVGASLS WAASTDAGSG VAGYELYRVQ GTTQTLVGTT TAAAYILRDL TPGTAYSYVV
     KAKDVAGNVS AASAAVTFTT DTTGETEPPT TPGTPVASAV TSTGATLAWA PSTGDPAVSG
     YDVLRVQGTT TTVVAQTTVP TVTLSGLTPS TAYTYAVRAK NVAGDVSALS APVTFTTAAP
     PVDTVAPTVP GTPVASNVAT TGATLTWTAS TDSGGSGLAG YEVLRVSGTT QTLVASPTTA
     TVALAGLTPA TAYSYVVRAK DGAGNVSAVS SPVTFTTLPV TSTPSCTVVY STNSWNVGFT
     GSVKITNTGT TPLTWTLGFA FPSGQQVTQG WSATWSQTGT TVTATGLSWN ATLQPGQSTD
     IGFNGSHPGT NTNPASFTVN GEVCG
//