GUX6_HUMIN
ID GUX6_HUMIN Reviewed; 476 AA.
AC Q9C1S9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Exoglucanase-6A;
DE EC=3.2.1.91;
DE AltName: Full=1,4-beta-cellobiohydrolase 6A;
DE AltName: Full=Avicelase 2;
DE AltName: Full=Beta-glucancellobiohydrolase 6A;
DE AltName: Full=Exocellobiohydrolase 6A;
DE Flags: Precursor;
GN Name=cel6A {ECO:0000303|PubMed:10413461, ECO:0000303|PubMed:12842048,
GN ECO:0000303|PubMed:9335167, ECO:0000303|PubMed:9882628};
GN Synonyms=avi2 {ECO:0000312|EMBL:BAB39154.1};
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:0000312|EMBL:BAB39154.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FERM BP-5977;
RX PubMed=12843680; DOI=10.1271/bbb.67.1434;
RA Moriya T., Watanabe M., Sumida N., Okakura K., Murakami T.;
RT "Cloning and overexpression of the avi2 gene encoding a major cellulase
RT produced by Humicola insolens FERM BP-5977.";
RL Biosci. Biotechnol. Biochem. 67:1434-1437(2003).
RN [2] {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 [3] {ECO:0000305, ECO:0000312|PDB:2BVW}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 115-476 IN COMPLEX WITH GLUCOSE
RP AND CELLOTETRAOSE, ACTIVE SITE, AND GLYCOSYLATION AT ASN-167.
RX PubMed=10413461; DOI=10.1021/bi9903998;
RA Varrot A., Schuelein M., Davies G.J.;
RT "Structural changes of the active site tunnel of Humicola insolens
RT cellobiohydrolase, Cel6A, upon oligosaccharide binding.";
RL Biochemistry 38:8884-8891(1999).
RN [4] {ECO:0000305, ECO:0000312|PDB:1GZ1}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 115-476 OF MUTANT ALA-416 IN
RP COMPLEX WITH SUBSTRATE ANALOG, AND GLYCOSYLATION AT ASN-167.
RX PubMed=12454501; DOI=10.1107/s0907444902017006;
RA Varrot A., Frandsen T.P., Driguez H., Davies G.J.;
RT "Structure of the Humicola insolens cellobiohydrolase Cel6A D416A mutant in
RT complex with a non-hydrolysable substrate analogue, methyl cellobiosyl-4-
RT thio-beta-cellobioside, at 1.9 A.";
RL Acta Crystallogr. D 58:2201-2204(2002).
RN [5] {ECO:0000305, ECO:0000312|PDB:1OC7}
RP X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 113-476 OF MUTANT ASN-431 IN
RP COMPLEX WITH SUBSTRATE ANALOGS, AND GLYCOSYLATION AT ASN-167.
RX PubMed=12842048; DOI=10.1016/s0969-2126(03)00124-2;
RA Varrot A., Frandsen T.P., von Ossowski I., Boyer V., Cottaz S., Driguez H.,
RA Schuelein M., Davies G.J.;
RT "Structural basis for ligand binding and processivity in cellobiohydrolase
RT Cel6A from Humicola insolens.";
RL Structure 11:855-864(2003).
RN [6] {ECO:0000305, ECO:0000312|PDB:1BVW}
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-476, FUNCTION, SUBUNIT, AND
RP GLYCOSYLATION AT THR-144; SER-153 AND ASN-167.
RX PubMed=9882628; DOI=10.1042/bj3370297;
RA Varrot A., Hastrup S., Schuelein M., Davies G.J.;
RT "Crystal structure of the catalytic core domain of the family 6
RT cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A
RT resolution.";
RL Biochem. J. 337:297-304(1999).
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 {ECO:0000269|PubMed:9882628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC and cellotetraose, releasing cellobiose from the non-reducing ends of
CC the chains.; EC=3.2.1.91; Evidence={ECO:0000269|PubMed:9335167};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10413461,
CC ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048,
CC ECO:0000269|PubMed:9882628}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase A) family.
CC {ECO:0000255}.
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DR EMBL; AB048710; BAB39154.1; -; Genomic_DNA.
DR PDB; 1BVW; X-ray; 1.92 A; A=117-476.
DR PDB; 1GZ1; X-ray; 1.90 A; A=115-476.
DR PDB; 1OC5; X-ray; 1.70 A; A=113-476.
DR PDB; 1OC6; X-ray; 1.50 A; A=113-476.
DR PDB; 1OC7; X-ray; 1.11 A; A=113-476.
DR PDB; 1OCB; X-ray; 1.75 A; A/B=115-476.
DR PDB; 1OCJ; X-ray; 1.30 A; A=115-476.
DR PDB; 1OCN; X-ray; 1.31 A; A=115-476.
DR PDB; 2BVW; X-ray; 1.70 A; A/B=115-476.
DR PDB; 4I5R; X-ray; 1.50 A; A=117-161.
DR PDB; 4I5U; X-ray; 1.22 A; A=117-161.
DR PDBsum; 1BVW; -.
DR PDBsum; 1GZ1; -.
DR PDBsum; 1OC5; -.
DR PDBsum; 1OC6; -.
DR PDBsum; 1OC7; -.
DR PDBsum; 1OCB; -.
DR PDBsum; 1OCJ; -.
DR PDBsum; 1OCN; -.
DR PDBsum; 2BVW; -.
DR PDBsum; 4I5R; -.
DR PDBsum; 4I5U; -.
DR AlphaFoldDB; Q9C1S9; -.
DR SMR; Q9C1S9; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR CLAE; CBH6A_HUMIN; -.
DR iPTMnet; Q9C1S9; -.
DR BRENDA; 3.2.1.91; 2710.
DR EvolutionaryTrace; Q9C1S9; -.
DR PRO; PR:Q9C1S9; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR DisProt; DP01080; -.
DR Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51989; SSF51989; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..476
FT /note="Exoglucanase-6A"
FT /id="PRO_0000248843"
FT DOMAIN 33..60
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 67..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..222
FT /note="Substrate binding loop 1"
FT /evidence="ECO:0000269|PubMed:10413461,
FT ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"
FT REGION 423..461
FT /note="Substrate binding loop 2"
FT /evidence="ECO:0000269|PubMed:10413461,
FT ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"
FT ACT_SITE 252
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057,
FT ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12842048"
FT ACT_SITE 431
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056,
FT ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501,
FT ECO:0000269|PubMed:12842048"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10413461,
FT ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10413461,
FT ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10413461,
FT ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10413461,
FT ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10413461,
FT ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10413461,
FT ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10413461,
FT ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10413461,
FT ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"
FT CARBOHYD 144
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:9882628"
FT CARBOHYD 153
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:9882628"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10413461,
FT ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048,
FT ECO:0000269|PubMed:9882628"
FT DISULFID 33..50
FT /evidence="ECO:0000255"
FT DISULFID 44..60
FT /evidence="ECO:0000255"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:1OC7"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2BVW"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:1OC7"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1OC7"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 173..186
FT /evidence="ECO:0007829|PDB:1OC7"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:1OC7"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 222..239
FT /evidence="ECO:0007829|PDB:1OC7"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:1OC7"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 264..283
FT /evidence="ECO:0007829|PDB:1OC7"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:1OC7"
FT TURN 298..302
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 304..320
FT /evidence="ECO:0007829|PDB:1OC7"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 357..370
FT /evidence="ECO:0007829|PDB:1OC7"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:1OC7"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:1OC7"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:1OC7"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:1OC7"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:1OC7"
SQ SEQUENCE 476 AA; 51276 MW; D2B0054F1381E653 CRC64;
MAKFFLTAAF AAAALAAPVV EERQNCAPTW GQCGGIGFNG PTCCQSGSTC VKQNDWYSQC
LPGSQVTTTS TTSTSSSSTT SRATSTTRTG GVTSITTAPT RTVTIPGGAT TTASYNGNPF
EGVQLWANNY YRSEVHTLAI PQITDPALRA AASAVAEVPS FQWLDRNVTV DTLLVETLSE
IRAANQAGAN PPYAAQIVVY DLPDRDCAAA ASNGEWAIAN NGANNYKGYI NRIREILISF
SDVRTILVIE PDSLANMVTN MNVAKCSGAA STYRELTIYA LKQLDLPHVA MYMDAGHAGW
LGWPANIQPA AELFAKIYED AGKPRAVRGL ATNVANYNAW SISSPPPYTS PNPNYDEKHY
IEAFRPLLEA RGFPAQFIVD QGRSGKQPTG QKEWGHWCNA IGTGFGMRPT ANTGHQYVDA
FVWVKPGGEC DGTSDTTAAR YDYHCGLEDA LKPAPEAGQW FQAYFEQLLR NANPPF
