GUX2_THES1
ID GUX2_THES1 Reviewed; 914 AA.
AC P50900; L7VQ95;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Exoglucanase-2;
DE EC=3.2.1.91;
DE AltName: Full=1,4-beta-cellobiohydrolase II;
DE AltName: Full=Avicelase II;
DE AltName: Full=Exocellobiohydrolase II;
DE AltName: Full=Exoglucanase II;
DE Flags: Precursor;
GN Name=celY; OrderedLocusNames=Cst_c18970;
OS Thermoclostridium stercorarium (strain ATCC 35414 / DSM 8532 / NCIMB 11754)
OS (Clostridium stercorarium).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Thermoclostridium.
OX NCBI_TaxID=1121335;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35414 / DSM 8532 / NCIMB 11754;
RA Bronnenmeier K., Kundt K., Riedel K., Schwarz W.H., Staudenbauer W.L.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35414 / DSM 8532 / NCIMB 11754;
RX PubMed=23516204; DOI=10.1128/genomea.00073-13;
RA Poehlein A., Zverlov V.V., Daniel R., Schwarz W.H., Liebl W.;
RT "Complete genome sequence of Clostridium stercorarium subsp. stercorarium
RT strain DSM 8532, a thermophilic degrader of plant cell wall fibers.";
RL Genome Announc. 1:E0007313-E0007313(2013).
RN [3]
RP CHARACTERIZATION.
RC STRAIN=ATCC 35414 / DSM 8532 / NCIMB 11754;
RX PubMed=1909625; DOI=10.1111/j.1432-1033.1991.tb16195.x;
RA Bronnenmeier K., Ruecknagel K.P., Staudenbauer W.L.;
RT "Purification and properties of a novel type of exo-1,4-beta-glucanase
RT (avicelase II) from the cellulolytic thermophile Clostridium
RT stercorarium.";
RL Eur. J. Biochem. 200:379-385(1991).
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;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 48 (cellulase L) family.
CC {ECO:0000305}.
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DR EMBL; Z69359; CAA93280.1; -; Genomic_DNA.
DR EMBL; CP004044; AGC68874.1; -; Genomic_DNA.
DR RefSeq; WP_015359554.1; NC_020887.2.
DR AlphaFoldDB; P50900; -.
DR SMR; P50900; -.
DR STRING; 1121335.Clst_1824; -.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR CAZy; GH48; Glycoside Hydrolase Family 48.
DR EnsemblBacteria; AGC68874; AGC68874; Cst_c18970.
DR KEGG; css:Cst_c18970; -.
DR PATRIC; fig|1121335.3.peg.1896; -.
DR eggNOG; COG4447; Bacteria.
DR eggNOG; COG5297; Bacteria.
DR BRENDA; 3.2.1.176; 1520.
DR BRENDA; 3.2.1.91; 1520.
DR Proteomes; UP000011220; Chromosome.
DR GO; GO:0008810; F:cellulase activity; 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 Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.170.160.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.710; -; 1.
DR Gene3D; 4.10.870.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR005102; Carbo-bd_X2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR023309; Endo-1-4-beta-glucanase_dom2.
DR InterPro; IPR027390; Endoglucanase_F_dom3.
DR InterPro; IPR000556; Glyco_hydro_48F.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF03442; CBM_X2; 1.
DR Pfam; PF02011; Glyco_hydro_48; 1.
DR PRINTS; PR00844; GLHYDRLASE48.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51172; CBM3; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..914
FT /note="Exoglucanase-2"
FT /id="PRO_0000008030"
FT DOMAIN 763..914
FT /note="CBM3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT CONFLICT 520
FT /note="G -> R (in Ref. 1; CAA93280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 914 AA; 102921 MW; B24CFC80F3AF4C7C CRC64;
MKRRLMKGIS LLTLVFLIGI MLQLSLKSEL TAYASSDDPY KQRFLELWEE LHDPSNGYFS
SHGIPYHAVE TLIVEAPDYG HLTTSEAMSY YLWLEALYGK FTGDFSYFMK AWETIEKYMI
PTEQDQPNRS MAGYNPAKPA TYAPEWEEPS MYPSQLDFSA PVGIDPIYNE LVSTYGTNTI
YGMHWLLDVD NWYGFGRRAD RISSPAYINT FQRGSQESVW ETIPQPCWDD LTIGGRNGFL
DLFVGDSQYS AQFKYTNAPD ADARAIQATY WANQWAKEHG VNLSQYVKKA SRMGDYLRYA
MFDKYFRKIG DSKQAGTGYD AAHYLLSWYY AWGGGITADW AWIIGCSHVH AGYQNPMTAW
ILANDPEFKP ESPNGANDWA KSLERQLEFY QWLQSAEGAI AGGATNSYKG RYETLPAGIS
TFYGMAYEEH PVYLDPGSNT WFGFQAWTMQ RVAEYYYLTG DTRAEQLLDK WVDWIKSVVR
LNSDGTFEIP GNLEWSGQPD TWTGTYTGNP NLHVSVVSYG TDLGAAGSLA NALLYYAKTS
GDDEARNLAK ELLDRMWNLY RDDKGLSAPE TREDYVRFFE QEVYVPQGWS GTMPNGDRIE
PGVTFLDIRS KYLNDPDYPK LQQAYNEGKA PVFNYHRFWA QCDIAIANGL YSILFGSEQA
NDSFITPTSA TFDKNNQEDI SVTVTYNGNT LLGIKSGSSY LIEGVDYIVN GDVIIIKKEF
LAGQATGSIS LLFDFSAGLD RTLTIDIIDT GGGEEPVEPV EPVEGVLIIQ SFNANTQEIS
NSIMPRFRIY NSGNTSIPLS EVKLRYYYTV DGDKPQNFWC DWASIGSSNV TGTFVKMDGA
TTGADYYLEI GFTPQAGTLE PGASIEVQGR FSKIDWTDYT QTNDYSFNPT ASSYVDFNKI
TAYISGNLVY GIEP
