GUNA_THEBI
ID GUNA_THEBI Reviewed; 456 AA.
AC P26414;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Endoglucanase A;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase A;
DE AltName: Full=Endo-1,4-beta-glucanase A;
DE Flags: Precursor;
GN Name=celA;
OS Thermobispora bispora (Microbispora bispora).
OC Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae;
OC Thermobispora.
OX NCBI_TaxID=2006;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yablonsky M.D., Elliston K.O., Eveleigh D.E.;
RL (In) Coughlan M.P. (eds.);
RL Production, characterization and application of cellulose, hemicellulose
RL and lignin enzyme degrading systems, pp.77-83, Elsevier, London (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 6 (cellulase B) family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P26414; -.
DR SMR; P26414; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
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; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
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; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51989; SSF51989; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..456
FT /note="Endoglucanase A"
FT /id="PRO_0000007905"
FT DOMAIN 353..456
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 31..322
FT /note="Catalytic"
FT REGION 255..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..355
FT /note="Linker ('hinge') (Pro-Ser box)"
FT COMPBIAS 325..354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 300
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT DISULFID 114..159
FT /evidence="ECO:0000250"
FT DISULFID 267..302
FT /evidence="ECO:0000250"
FT DISULFID 360..453
FT /evidence="ECO:0000250"
SQ SEQUENCE 456 AA; 47011 MW; B06D8595E322848F CRC64;
MSRIRRFLAT ALAAATAGVG AIVTAIASAG PAHAYDSPFY VDPQSNAAKW VAANPNDPRT
PVIRDRIAAV PTGRWFANYN PSTVRAEVDA YVGAAAAAGK IPIMVVYAMP NRDCGGPSAG
GAPNHTAYRA WIDEIAAGLR NRPAVIILEP DALPIMTNCM SPSEQAEVQA SAVGAGKKFK
AASSQAKVYF DAGHDAWVPA DEMASRLRGA DIANSADGIA LNVSNYRYTS GLISYAKSVL
SAIGASHLRA VIDTSRNGNG PLGSEWCDPP GRATGTWSTT DTGDPAIDAF LWIKPPGEAD
GCIATPGVFV PDRAYELAMN AAPPTYSPSP TPSTPSPSPS QSDPGSPSPS PSQPPAGRAC
EATYALVNQW PGGFQAEVTV KNTGSSPING WTVQWTLPSG QSITQLWNGD LSTSGSNVTV
RNVSWNGNVP AGGSTSFGFL GSGTGQLSSS ITCSAS
