ID D6Y754_THEBD Unreviewed; 460 AA.
AC D6Y754;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN OrderedLocusNames=Tbis_0925 {ECO:0000313|EMBL:ADG87649.1};
OS Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM
OS 10125 / KCTC 9307 / NBRC 14880 / R51).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Thermobispora.
OX NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG87649.1, ECO:0000313|Proteomes:UP000006640};
RN [1] {ECO:0000313|EMBL:ADG87649.1, ECO:0000313|Proteomes:UP000006640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 /
RC NBRC 14880 / R51 {ECO:0000313|Proteomes:UP000006640};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermobispora bispora DSM 43833.";
RL Submitted (JAN-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; CP001874; ADG87649.1; -; Genomic_DNA.
DR RefSeq; WP_013131182.1; NC_014165.1.
DR AlphaFoldDB; D6Y754; -.
DR STRING; 469371.Tbis_0925; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR KEGG; tbi:Tbis_0925; -.
DR eggNOG; COG2730; Bacteria.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_018488_0_0_11; -.
DR OrthoDB; 9801198at2; -.
DR Proteomes; UP000006640; 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|RuleBase:RU361153};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000006640};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..460
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003091057"
FT DOMAIN 356..460
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 325..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 49066 MW; DC0CD31BD2642BA8 CRC64;
MRTRLGVAVA ALFALAWSLI VWSPPAQAAV GLRVGDGKIY EANGAEFIMR GTSHPHAWYP
NQTGSFADIK SLGANTVRVV LSGGRWTPNS PSDVANVIRL CKENRLICVL ENHDTTGYGE
QSGAYPLDQA VDYWISLKSV LTGEENYIVI NIGNEPYGNN NPSAWTAATI NAIQRMRDAG
FQHLLMVDAP NWGQDWAFVM RDNAATVFDS DPLKNTVFSI HMYGVFDTAN EITSYLQAFQ
SARLPLVIGE FGHLHSDGDP DEDTIMAEAE ARGIGYIGWS WSGNGGGVEY LDQVENFDPA
RLTPWGQRLF NGPNGIKATA KEATVYGGTA SPPPSSPPAS PPVSPPVSPP VSPSPSPSGS
KGCTASYRIV NEWNGGFQGE VTVTAGDSAI SGWTVSWTFP DGQAVTQAWN ATITSNGPSV
TAKNMSYNGD LGPGAGTTFG FLGSWQGQNR VPPEVICTAS
//
