ID A0A1I0CHR3_9FIRM Unreviewed; 662 AA.
AC A0A1I0CHR3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN ORFNames=SAMN04487772_11016 {ECO:0000313|EMBL:SET19069.1};
OS [Clostridium] polysaccharolyticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=29364 {ECO:0000313|EMBL:SET19069.1, ECO:0000313|Proteomes:UP000199800};
RN [1] {ECO:0000313|EMBL:SET19069.1, ECO:0000313|Proteomes:UP000199800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1801 {ECO:0000313|EMBL:SET19069.1,
RC ECO:0000313|Proteomes:UP000199800};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000966};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOHN01000010; SET19069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0CHR3; -.
DR STRING; 29364.SAMN04487772_11016; -.
DR OrthoDB; 9800475at2; -.
DR Proteomes; UP000199800; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000199800};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..662
FT /note="cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011772497"
FT DOMAIN 31..145
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 143..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 73456 MW; E0CC2F6C0D3AAE9D CRC64;
MKAMSKKRNF NALVSFVMIL ALSLSFLLPN AAFAAAAKTD AVELKTEGSS WNGGFSVNVY
VNNTGTQTIT DWKVVIEKNG FTLSSIWCAD SKASSDTYVV TPNDWAKSIS AGSSVNFGFC
GTGKMPEDTQ YTVVYKINGK EYSTGDVVPD TEPSTAPSVV PSTEPSVKPS AKPSVEPSIK
PSVEPSIKPS AKPSTEPSAK PSVEPSIKPS VKPSIKPSTA PAGDAKSGDD WLHVEGTNIC
DKYGNKVWLT GANWFGFNCR ERMLLDSYHS NIIADIEQVA DKGINVVRIP IATDLLYSWS
KGIYPASTDT SYNNKALAGL NSFELFNFML ENFKRVGIKV ILDVHGAETD NQGHNYPVWY
KGSITEEVFK AAWVWAADQY KNDDTIIGFD LKNEPHTNTG DIKIKAQSAI WDDSSLANNW
KRVAQETALA ILDVHPHALI FVEGVEIYPK DSIWDDESIN TSAWGGTNDY YCTWWGGNLR
GVKDYPINLG KYQSQLVYSP HDYGPIVFNQ SWFQGDFESA SDKEAFDIMY SQCWHDNWGY
IMEDGIAPLL VGEWGGITEG NHPLLDQNQK YLRCMRDYII QNKYSLHHTF WCINIDSADT
NGLLTRDEGT PFEGGRDLKW NDYKYDNYLK PALWQTADGT FIGLDHEIPL GHNGIALGTT
QY
//
