ID   GUN_CELUD               Reviewed;         359 AA.
AC   P18336;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
OS   Cellulomonas uda.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=1714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-37.
RC   STRAIN=CB4;
RA   Nakamura K., Misawa N., Kitamura K.;
RT   "Sequence of a cellulase gene of Cellulomonas uda CB4.";
RL   J. Biotechnol. 4:247-254(1986).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC       {ECO:0000305}.
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DR   EMBL; M36503; AAA23090.1; -; Genomic_DNA.
DR   PIR; I40696; I40696.
DR   AlphaFoldDB; P18336; -.
DR   SMR; P18336; -.
DR   CAZy; GH8; Glycoside Hydrolase Family 8.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR002037; Glyco_hydro_8.
DR   InterPro; IPR019834; Glyco_hydro_8_CS.
DR   Pfam; PF01270; Glyco_hydro_8; 1.
DR   PRINTS; PR00735; GLHYDRLASE8.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|Ref.1"
FT   CHAIN           24..359
FT                   /note="Endoglucanase"
FT                   /id="PRO_0000007933"
FT   ACT_SITE        53
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        110
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10058"
SQ   SEQUENCE   359 AA;  40690 MW;  0445D7571B683148 CRC64;
     MPLRALVAVI VTTAVMLVPR AWAQTAWERY KARFMMPDAR IIDTANGNVS HTEGQGFAML
     LAVANNDRPA FDKLWQWTDS TLRDKSNGLF YWRYNPVAPD PIADKNNATD GDTLIAWALL
     RAQKQWQDKR YATASDAITA SLLKYTVVTF AGRQVMLPGV KGFNRNDHLN LNPSYFIFPA
     WRAFAERTHL TAWRTLQSDG QALLGQMGWG KSHLPSDWVA LRADGKMLPA KEWPPRMSFD
     AIRIPLYISW VDPHSALLAP WKAWMQSYPR LQTPAWINVS TNEVAPWNMA GGLLAVRDLT
     LGEPLERRRL TTRMIITPPA SSCWSGWRNR ISASAVMALQ VSQPVCLRAE RKEQERLTM