ID   GUN1_STRRE              Reviewed;         746 AA.
AC   Q05156;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Cellulase 1;
DE            EC=3.2.1.4;
DE   AltName: Full=Avicelase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   AltName: Full=Endoglucanase;
DE   Flags: Precursor;
GN   Name=cel1;
OS   Streptomyces reticuli.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-41 AND
RP   379-391.
RC   STRAIN=Tu45;
RX   PubMed=1282194; DOI=10.1111/j.1365-2958.1992.tb01797.x;
RA   Schlochtermeier A., Walter S., Schroeder J., Moorman M., Schrempf H.;
RT   "The gene encoding the cellulase (Avicelase) Cel1 from Streptomyces
RT   reticuli and analysis of protein domains.";
RL   Mol. Microbiol. 6:3611-3621(1992).
CC   -!- FUNCTION: This endoglucanase acts only on crystalline cellulose.
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   -!- SUBCELLULAR LOCATION: Note=Exists in both mycelium-associated and
CC       extracellular forms.
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; X65616; CAA46570.1; -; Genomic_DNA.
DR   PIR; S27985; S27985.
DR   AlphaFoldDB; Q05156; -.
DR   SMR; Q05156; -.
DR   CAZy; CBM4; Carbohydrate-Binding Module Family 4.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02850; E_set_Cellulase_N; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_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   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS60032; GH9_1; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:1282194"
FT   CHAIN           30..746
FT                   /note="Cellulase 1"
FT                   /id="PRO_0000007958"
FT   DOMAIN          45..170
FT                   /note="CBM-cenC"
FT   REGION          171..211
FT                   /note="Linker"
FT   REGION          212..746
FT                   /note="Catalytic"
FT   ACT_SITE        342
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT   ACT_SITE        669
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        717
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        726
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   746 AA;  80000 MW;  FDF1ADB4714A35FD CRC64;
     MKRRTTAVLT LTALLGTALT ALPVQQAGAE EVEQVRNGTF DTTTDPWWTS NVTAGLSDGR
     LCADVPGGTT NRWDSAIGQN DITLVKGETY RFSFHASGIP EGHVVRAVVG LAVSPYDTWQ
     EASPVLTEAD GSYSYTFTAP VDTTQGQVAF QVGGSTDAWR FCVDDVSLLG GVPPEVYEPD
     TGPRVRVNQV AYLPAGPKNA TLVTDATARL PWQLRNAQGT TVARGLTVPR GVDASSGQNV
     HSIDFGSYRG RGTGYTLVAD GETSHPFDID AAAYRPLRLD SVKYYYTQRS GIAIRDDLRP
     GYGRAAGHLN VAPNQGDANV PCQPGVCDYT LDVTGGWYDA GDHGKYVVNG GIATWELLST
     YERSLTARTG HPAALGDGTL ALPESGNKVP DVLDEARWEL EFLLKMQVPA GQPLAGMAHH
     KLHDEQWTGL PLLPDQDPQK RELHPPTTAA TLNLAATAAQ AARLYRPFDK AFAARALTAA
     RTAWQAALAH PDLLADPNDG TGGGAYNDDD VTDEFYWAAA ELYLTTGERQ FADHVLDSPV
     HTADIFGPTG FDWGHTAAAG RLDLALVPSR LPGRDQVRRS VIKAADTYLA TLTAHPYGMP
     YAPAGNRYDW GSSHQVLNNG VVLASAYDLT GAAKYRDGAL QGMDYVLGRN ALNMSYVTGY
     GEVSSHNQHS RWYAHQLDPT LPNPPSGTLA GGPNSSIQDP YAQSKLTGCV GQFCYIDDIQ
     SWSTNETAIN WNAALARMAS FAADQG
//