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
//
