GUNB_PAELA
ID GUNB_PAELA Reviewed; 566 AA.
AC P23550;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 82.
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 Short=EG-B;
DE Flags: Precursor;
GN Name=celB;
OS Paenibacillus lautus (Bacillus lautus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1401;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PL236;
RX PubMed=2227426; DOI=10.1016/0378-1119(90)90135-e;
RA Joergensen P.L., Hansen C.K.;
RT "Multiple endo-beta-1,4-glucanase-encoding genes from Bacillus lautus PL236
RT and characterization of the celB gene.";
RL Gene 93:55-60(1990).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; M33762; AAA22408.1; -; Genomic_DNA.
DR PIR; JH0218; JH0218.
DR AlphaFoldDB; P23550; -.
DR SMR; P23550; -.
DR CAZy; CBM46; Carbohydrate-Binding Module Family 46.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR005102; Carbo-bd_X2.
DR InterPro; IPR040946; CBM46.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR016282; Glyco_hydro_5_endoGlcnase_B.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF18448; CBM46; 1.
DR Pfam; PF03442; CBM_X2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR PIRSF; PIRSF001043; Endoglucanase_B; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..30
FT CHAIN 31..566
FT /note="Endoglucanase B"
FT /id="PRO_0000007835"
FT ACT_SITE 177
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 299
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 566 AA; 62622 MW; 6426C8D8E29022C9 CRC64;
MKKRRSSKVI LSLAIVVALL AAVEPNAALA AAPPSAMQSY VEAMQPGWNL GNSLDAVGAD
ETLARGNPRI TKELIQNIAA QGYKSIRIPV TWDSHIGAAP NYQIEAAYLN RVQEVVQWAL
DANLYVMINV HHDSWLWISK MESQHDQVLA RYNAIWTQIA NKFKNSPSKL MFESVNEPRF
TDGGTTDEAK QQKMLDELNV SFFNIVRNSG GQNATRPLVL STLEASPTQE RMTALYNTMT
KLNDKNLIAT VHFYGFWPFS VNIAGYTKFD AETQNDIITT FDNVYNTFVA KGIPVVVGEY
GLLGFDKNTG VIEQGEKLKF FEFFAQYVKQ KSISTMLWDN GQHFNRTSFK WSDPDLFNMI
KASWTGRSST ASSDLIHVKQ GTAVKDTSVQ LNLNGNTLTS LSVNGTTLKS GTDYTLNSSR
LTFKASQLTK LTSLGKLGVN ATIVTKFNRG ADWKFNVVLY NTPKLSSTTG TTSSFAIPTA
FNGDQLATME AVYVNGGNAG PHNWTSFKEF ETTFSPAYSE GKIKLQQAFF NEVNDTTVTL
KFQFWSGEIV NYTIKKSGST VTGTAS