GUX1_HYPJR
ID GUX1_HYPJR Reviewed; 514 AA.
AC A0A024RXP8;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Exoglucanase 1;
DE EC=3.2.1.91 {ECO:0000250|UniProtKB:P62694};
DE AltName: Full=1,4-beta-cellobiohydrolase;
DE AltName: Full=Cellobiohydrolase 7A;
DE Short=Cel7A;
DE AltName: Full=Exocellobiohydrolase I;
DE Short=CBHI;
DE AltName: Full=Exoglucanase I;
DE Flags: Precursor;
GN Name=cbh1; ORFNames=M419DRAFT_125125;
OS Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30)
OS (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1344414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX DOI=10.1089/ind.2013.0015;
RA Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.;
RT "Comparative genomics analysis of Trichoderma reesei strains.";
RL Ind. Biotechnol. 9:352-367(2013).
RN [2]
RP GLYCOSYLATION AT ASN-62; ASN-287 AND ASN-401.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=11270873; DOI=10.1016/s0378-4347(00)00373-x;
RA Hui J.P.M., Lanthier P., White T.C., McHugh S.G., Yaguchi M., Roy R.,
RA Thibault P.;
RT "Characterization of cellobiohydrolase I (Cel7A) glycoforms from extracts
RT of Trichoderma reesei using capillary isoelectric focusing and electrospray
RT mass spectrometry.";
RL J. Chromatogr. B 752:349-368(2001).
CC -!- FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of
CC 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide
CC cellobiose. The degradation of cellulose involves an interplay between
CC different cellulolytic enzymes. Hydrolysis starts with endoglucanases
CC (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to
CC reduce the polymerization degree of the substrate and create new chain
CC ends for exocellobiohydrolases (CBHs). The CBHs release the
CC disaccharide cellobiose from the non-reducing end of the cellulose
CC polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose
CC and other short cello-oligosaccharides into glucose units.
CC {ECO:0000250|UniProtKB:P62694}.
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:0000250|UniProtKB:P62694};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P62694}.
CC -!- DOMAIN: The enzyme consists of two functional domains, a catalytic core
CC joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-,
CC and proline-rich, highly glycosylated linker sequence.
CC {ECO:0000250|UniProtKB:P62694}.
CC -!- PTM: N-glycosylated. A high mannose glycan is attached to Asn-287
CC (predominantly Man(8)GlcNAc(2)) and single GlcNAc occupancy is observed
CC at Asn-62 and Asn-401 with some site heterogeneity depending on strains
CC and fermentation conditions. {ECO:0000269|PubMed:11270873}.
CC -!- PTM: O-glycosylated. Within the linker domain, all 8 threonines are
CC variably glycosylated with between at least one, and up to three,
CC mannose residues per site. All serines in this domain are at least
CC partially glycosylated with a single mannose residue. O-glycosylation
CC of the cellulase linker provides protection from proteolysis. Linker
CC glycans also contribute to binding affinity of cellobiohydrolases to
CC cellulose. {ECO:0000250|UniProtKB:P62694}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000305}.
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DR EMBL; KI911168; ETR97652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024RXP8; -.
DR SMR; A0A024RXP8; -.
DR iPTMnet; A0A024RXP8; -.
DR EnsemblFungi; ETR97652; ETR97652; M419DRAFT_125125.
DR KEGG; trr:M419DRAFT_125125; -.
DR HOGENOM; CLU_020817_3_2_1; -.
DR OrthoDB; 875234at2759; -.
DR BRENDA; 3.2.1.91; 6451.
DR Proteomes; UP000024376; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 CDD; cd07999; GH7_CBH_EG; 1.
DR Gene3D; 2.70.100.10; -; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001722; Glyco_hydro_7.
DR InterPro; IPR037019; Glyco_hydro_7_sf.
DR PANTHER; PTHR33753; PTHR33753; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..514
FT /note="Exoglucanase 1"
FT /id="PRO_5001533368"
FT DOMAIN 478..514
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 18..453
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT REGION 401..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..478
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT ACT_SITE 234
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT SITE 81
FT /note="Not glycosylated"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT MOD_RES 18
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:11270873"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:11270873"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:11270873"
FT CARBOHYD 462
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 463
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 464
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 465
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 470
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 471
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 472
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 474
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 475
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 479
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 481
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT CARBOHYD 492
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 21..89
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 36..42
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 67..88
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 78..84
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 155..414
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 189..227
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 193..226
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 247..273
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 255..260
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 278..348
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 486..503
FT /evidence="ECO:0000250|UniProtKB:P62694"
FT DISULFID 497..513
FT /evidence="ECO:0000250|UniProtKB:P62694"
SQ SEQUENCE 514 AA; 54111 MW; 9160A86350CA8424 CRC64;
MYRKLAVISA FLATARAQSA CTLQSETHPP LTWQKCSSGG TCTQQTGSVV IDANWRWTHA
TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG VTTSGNSLSI GFVTQSAQKN
VGARLYLMAS DTTYQEFTLL GNEFSFDVDV SQLPCGLNGA LYFVSMDADG GVSKYPTNTA
GAKYGTGYCD SQCPRDLKFI NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE
ALTPHPCTTV GQEICEGDGC GGTYSDNRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD
TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGSYSG NELNDDYCTA EEAEFGGSSF
SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT NETSSTPGAV RGSCSTSSGV
PAQVESQSPN AKVTFSNIKF GPIGSTGNPS GGNPPGGNPP GTTTTRRPAT TTGSSPGPTQ
SHYGQCGGIG YSGPTVCASG TTCQVLNPYY SQCL
