GUNB_CELFI
ID GUNB_CELFI Reviewed; 1045 AA.
AC P26225;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=cenB;
OS Cellulomonas fimi.
OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; Cellulomonas.
OX NCBI_TaxID=1708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1987122; DOI=10.1128/jb.173.1.308-314.1991;
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 from
RT Cellulomonas fimi.";
RL J. Bacteriol. 173:308-314(1991).
RN [2]
RP DOMAINS.
RX PubMed=1938913; DOI=10.1128/jb.173.22.7126-7135.1991;
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 generally
CC requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC cut the disaccharide cellobiose from the non-reducing end of the
CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC cellobiose and other short cello-oligosaccharides to glucose.
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 -!- DOMAIN: The linker region (also termed 'hinge') may be a potential site
CC for proteolysis. {ECO:0000269|PubMed:1938913}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
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DR EMBL; M64644; AAA23086.1; -; Genomic_DNA.
DR PIR; A39199; A39199.
DR RefSeq; WP_013769201.1; NZ_LR134387.1.
DR AlphaFoldDB; P26225; -.
DR SMR; P26225; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR OMA; RWLDYWT; -.
DR GO; GO:0008810; F:cellulase 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 CDD; cd00063; FN3; 3.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.40.710; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR013783; Ig-like_fold.
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 SMART; SM00637; CBD_II; 1.
DR SMART; SM01067; CBM_3; 1.
DR SMART; SM00060; FN3; 3.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF49384; SSF49384; 2.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS51172; CBM3; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Repeat; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1045
FT /note="Endoglucanase B"
FT /id="PRO_0000007945"
FT DOMAIN 493..642
FT /note="CBM3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT DOMAIN 653..743
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 751..840
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 849..940
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 939..1045
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 34..492
FT /note="Catalytic"
FT REGION 644..650
FT /note="Linker ('hinge') (Pro-Thr box)"
FT REGION 734..748
FT /note="Linker ('hinge') (Pro-Thr box)"
FT REGION 831..846
FT /note="Linker ('hinge') (Pro-Thr box)"
FT REGION 931..944
FT /note="Linker ('hinge') (Pro-Thr box)"
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT DISULFID 946..1044
FT /evidence="ECO:0000250"
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
