ID D4MIK7_9FIRM Unreviewed; 585 AA.
AC D4MIK7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=ES1_04480 {ECO:0000313|EMBL:CBL33590.1};
OS [Eubacterium] siraeum V10Sc8a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=717961 {ECO:0000313|EMBL:CBL33590.1, ECO:0000313|Proteomes:UP000007050};
RN [1] {ECO:0000313|EMBL:CBL33590.1, ECO:0000313|Proteomes:UP000007050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL33590.1,
RC ECO:0000313|Proteomes:UP000007050};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Eubacterium siraeum V10Sc8a.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL33590.1, ECO:0000313|Proteomes:UP000007050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL33590.1,
RC ECO:0000313|Proteomes:UP000007050};
RA Pajon A.;
RL Submitted (MAR-2010) 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 ECO:0000256|RuleBase:RU361153};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|RuleBase:RU361153}.
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DR EMBL; FP929059; CBL33590.1; -; Genomic_DNA.
DR AlphaFoldDB; D4MIK7; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR KEGG; esr:ES1_04480; -.
DR PATRIC; fig|717961.3.peg.470; -.
DR HOGENOM; CLU_012932_2_0_9; -.
DR BioCyc; ESIR717961:G136L-356-MONOMER; -.
DR Proteomes; UP000007050; Chromosome.
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; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 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 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361153};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:CBL33590.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361153}.
FT DOMAIN 135..247
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 50..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 63699 MW; B1491C4E475218D6 CRC64;
MTALIREGCF NITTERGNMK KSIIRRAIAV FIAAAMLAGC AAQDSGVLSS VGNNSATESN
ESYVEDTSSV DENSEVTSVD NSVTESDTSS DTSEQEESNA SKQENTSKSD NTEKPADTTK
VQATADTKNN SQSKPASSAS NFTVQWKKSS SWEEGGKKCG GYEIVITNNG DTVNSWTAKV
TVPGNTKLMS QWNGIFSISG NTMTVKNESY NGTIEKGKSV SFGFNYSADA YINEGKVTVN
GSTAGTSAGN NSNNNNNNNN NTSTTKKPAA TVPPAPSDPK GTTPVSQHGQ LSVKNGQLVD
KSGKGYQLRG MSTHGLTWFP EFVNESAFKT LRDDWNTNVV RLAMYVDEWG NGQCYMGNKS
GSLELLEKGV DICVKLDMYV IIDWHVLNPG DPSKYTNEAK SFFETVSKRY AKYPNVIYEI
CNEPNGGASW SGNIKPYAEK IIPVIRKNAP NSVIIVGTPT WSQEIDKPLS DPLSYKNVMY
AFHFYAATHA GLRSNVENCV AQGLPVFVSE FGTCDASGGG ANDFNETQKW LSYFDKQGIS
YCNWSICNKD ETCSVLRPGT SANGNWSESD LTENGKWMRN WFRKH
//
