GUN6_HUMIN
ID GUN6_HUMIN Reviewed; 348 AA.
AC Q7SIG5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Endoglucanase-6B;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase 6B;
DE AltName: Full=Endo-1,4-beta-glucanase 6B;
GN Name=cel6B {ECO:0000303|PubMed:10794732};
OS Humicola insolens (Soft-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Humicola.
OX NCBI_TaxID=34413;
RN [1] {ECO:0000305}
RP CATALYTIC ACTIVITY.
RX PubMed=9335167; DOI=10.1016/s0168-1656(97)00090-4;
RA Schuelein M.;
RT "Enzymatic properties of cellulases from Humicola insolens.";
RL J. Biotechnol. 57:71-81(1997).
RN [2] {ECO:0000312|PDB:1DYS}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=10794732; DOI=10.1042/bj3480201;
RA Davies G.J., Brzozowski A.M., Dauter M., Varrot A., Schuelein M.;
RT "Structure and function of Humicola insolens family 6 cellulases: structure
RT of the endoglucanase, Cel6B, at 1.6 A resolution.";
RL Biochem. J. 348:201-207(2000).
CC -!- FUNCTION: Plays a central role in the recycling of plant biomass. The
CC biological conversion of cellulose to glucose generally requires three
CC types of hydrolytic enzymes: (1) Endoglucanases which cut internal
CC beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the
CC disaccharide cellobiose from the non-reducing end of the cellulose
CC polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose
CC 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 Evidence={ECO:0000269|PubMed:9335167};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10794732}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC {ECO:0000255}.
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DR PDB; 1DYS; X-ray; 1.60 A; A/B=1-348.
DR PDBsum; 1DYS; -.
DR AlphaFoldDB; Q7SIG5; -.
DR SMR; Q7SIG5; -.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR CLAE; EGL6B_HUMIN; -.
DR BioCyc; MetaCyc:MON-17625; -.
DR EvolutionaryTrace; Q7SIG5; -.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SUPFAM; SSF51989; SSF51989; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase;
KW Hydrolase; Polysaccharide degradation.
FT CHAIN 1..348
FT /note="Endoglucanase-6B"
FT /id="PRO_0000248842"
FT REGION 222..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057,
FT ECO:0000303|PubMed:10794732"
FT ACT_SITE 139
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057,
FT ECO:0000269|PubMed:10794732"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT TURN 5..8
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:1DYS"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 150..169
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 193..207
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:1DYS"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:1DYS"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:1DYS"
FT HELIX 332..340
FT /evidence="ECO:0007829|PDB:1DYS"
SQ SEQUENCE 348 AA; 37753 MW; 5F1E4A4367402E54 CRC64;
QSGNPFSGRT LLVNSDYSSK LDQTRQAFLS RGDQTNAAKV KYVQEKVGTF YWISNIFLLR
DIDVAIQNAR AAKARGENPI VGLVLYNLPD RDCSAGESSG ELKLSQNGLN RYKNEYVNPF
AQKLKAASDV QFAVILEPDA IGNMVTGTSA FCRNARGPQQ EAIGYAISQL QASHIHLYLD
VANGGWLGWA DKLEPTAQEV ATILQKAGNN AKIRGFSSNV SNYNPYSTSN PPPYTSGSPS
PDESRYATNI ANAMRQRGLP TQFIIDQSRV ALSGARSEWG QWCNVNPAGF GQPFTTNTNN
PNVDAIVWVK PGGESDGQCG MGGAPAAGMW FDAYAQMLTQ NAHDEIAR
