ID U3RAX8_BACPU Unreviewed; 465 AA.
AC U3RAX8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
DE Flags: Fragment;
OS Bacillus pumilus (Bacillus mesentericus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1408 {ECO:0000313|EMBL:AGW99982.1};
RN [1] {ECO:0000313|EMBL:AGW99982.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IARI-SP-5 {ECO:0000313|EMBL:AGW99982.1};
RA Pandey S., Tiwari R., Nain L., Saxena A.K.;
RT "Diversity of endoglucanase gene in Bacillus species.";
RL Submitted (JUN-2013) 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|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; KF240852; AGW99982.1; -; Genomic_DNA.
DR AlphaFoldDB; U3RAX8; -.
DR SMR; U3RAX8; -.
DR GO; GO:0008810; F:cellulase 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; 2.60.40.710; Endoglucanase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_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; PF00942; CBM_3; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51172; CBM3; 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:AGW99982.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361153}.
FT DOMAIN 332..465
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT NON_TER 465
FT /evidence="ECO:0000313|EMBL:AGW99982.1"
SQ SEQUENCE 465 AA; 51549 MW; CE525F76DC3BD910 CRC64;
MGGMIASPAS AAGTKTPVAK NGQLSIKGTQ LVNRDGKAVQ LKGISSHGLQ WYGEYVNKDS
LKWLRDDWGI TVFRAAMYTA DGRNRYNPSV KNKVKEAVEA AKELGIYVII DWHILNDGNP
NQNKEKAKEF FKEMSSLYGN TPNVIYEIAN EPNGDVNWKR DIKPYAEEVI SVIRKNDPDN
IIIVGTGTWS QDVNDAADDQ LKDANVMYAL HFYAGTHGQF LRDKANYALS KGAPIFVTEW
GTSDASGNGG VFLDQSREWL KYLDSKTISW VNWNLSDKQE SSSALKPGAS KTGGWRLSDL
SASGTFVREN ILGTKDSTKD IPETPSKDKP TQENGISVQY RAGDGSMNSN QIRPQLQIKN
NGNTTVDLKD VTARYWYKAK NKGQNFDCDY AQIGCGNVTH KFVTLHKPKQ GADTYLELGF
KNGTLAPGAS TGNIQLRLHN DDWSNYAQSG DYSFFKSNTF KTTKK
//
