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Database: UniProt
Entry: V9XSU0_BACIU
LinkDB: V9XSU0_BACIU
Original site: V9XSU0_BACIU 
ID   V9XSU0_BACIU            Unreviewed;       335 AA.
AC   V9XSU0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
DE   Flags: Fragment;
OS   Bacillus subtilis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423 {ECO:0000313|EMBL:AHD24509.1};
RN   [1] {ECO:0000313|EMBL:AHD24509.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H13h {ECO:0000313|EMBL:AHD24509.1};
RA   Dahpahlevan S., Hashemi M., Mousivand M., Khara J.;
RT   "Purification and properties of the endo-1, 4-beta-glucanase from Bacillus
RT   subtilis.";
RL   Submitted (OCT-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; KF715636; AHD24509.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9XSU0; -.
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; 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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361153};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:AHD24509.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361153}.
FT   DOMAIN          194..335
FT                   /note="CBM3"
FT                   /evidence="ECO:0000259|PROSITE:PS51172"
FT   REGION          177..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AHD24509.1"
FT   NON_TER         335
FT                   /evidence="ECO:0000313|EMBL:AHD24509.1"
SQ   SEQUENCE   335 AA;  36402 MW;  BF67811203494F62 CRC64;
     GNTPNVIKEI ANEPNRDVNL KRDIKPYAEE VISVIRKKDP DNIIIVGTGT WGQDVKDAAE
     DQLKDANVMY ALHFYAGTHG QSFREKANYA LRKGAPIFVT EWGTSDASGN GGVFLDQSRE
     RVDYLDSKNI SWVDWNFLEK PESSLALKPG ALKTGGWPLT DLTGSGTFVR ENLCGNKDLT
     KDAPETPAQE NSAPEKGLSV QYKAGGGGGD SNQIPPQLPI KKNGNAAGDL KDVPARFWLN
     AKNKGPKYGC GYAPIGCGNL IPKFVALQKP KQGADTYLEM GLKTGTLSPG ASPGNIQVCF
     PKEDWGNYAQ SGGYSFFQSN TLKKTKKITL YHQEN
//
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