ID   GUN1_BUTFI              Reviewed;         547 AA.
AC   P20847;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-MAY-2023, entry version 102.
DE   RecName: Full=Endoglucanase 1;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase 1;
DE   AltName: Full=Endo-1,4-beta-glucanase 1;
GN   Name=end1;
OS   Butyrivibrio fibrisolvens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H17C;
RX   PubMed=2615759; DOI=10.1007/bf00261176;
RA   Berger E., Jones W.A., Jones D.T., Woods D.R.;
RT   "Cloning and sequencing of an endoglucanase (end1) gene from Butyrivibrio
RT   fibrisolvens H17c.";
RL   Mol. Gen. Genet. 219:193-198(1989).
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; X17538; CAA35574.1; -; Genomic_DNA.
DR   PIR; JQ0356; JQ0356.
DR   AlphaFoldDB; P20847; -.
DR   SMR; P20847; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31297:SF41; ENDOGLUCANASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G01830)-RELATED; 1.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..547
FT                   /note="Endoglucanase 1"
FT                   /id="PRO_0000184046"
FT   DOMAIN          448..547
FT                   /note="CBM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT   REGION          398..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..448
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        189
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        321
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   547 AA;  61078 MW;  C62EE40E6442ECF9 CRC64;
     MHKSKCIKRV FTFLLALFVF VMAIPATKVS AAGGTDRSAT QVVSDMRVGW NIGNSLDSFG
     QSYNFPYTSL NETYWGNPAT TKALIDEVAK AGFNTIRIPV SWGQYTTGSD YQIPDFVMNR
     VKEVVDYCIV NDMYVILNSH HDINSDYCFY VPNNANKDRS EKYFKSIWTQ IAKEFKNYDY
     HLVFETMNEP RLVGHGEEWW FPRNNPSNDI REAVACINDY NQVALDAIRA TGGNNATRCV
     MVPGYDASIE GCMTDGFKMP NDTASGRLIL SVHAYIPYYF ALASDTYVTR FDDNLKYDID
     SFFNDLNSKF LSRNIPVVVG ETSATNRNNT AERVKWADYY WGRAARYSNV AMVLWDNNIY
     QNNSAGSDGE CHMYIDRNSL QWKDPEIIST IMKHVDGTPA TINGKEIPST EQPDPTPVDP
     DPTPVDPDPT PVDPDPTPVD PDPQPVDPTP VSGALKAEYT INNWGSGYQV LIKVKNDSAS
     RVDGWTLKIS KSEVKIDSSW CVNIAEEGGY YVITPMSWNS SLEPSASVDF GIQGSGSIGT
     SVNISVQ
//