ID A0A0M9X607_9ACTN Unreviewed; 461 AA.
AC A0A0M9X607;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=ADK41_33945 {ECO:0000313|EMBL:KOT29558.1};
OS Streptomyces caelestis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT29558.1, ECO:0000313|Proteomes:UP000037773};
RN [1] {ECO:0000313|EMBL:KOT29558.1, ECO:0000313|Proteomes:UP000037773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT29558.1,
RC ECO:0000313|Proteomes:UP000037773};
RA Noorani M.;
RL Submitted (JUL-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOT29558.1}.
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DR EMBL; LGCN01000248; KOT29558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9X607; -.
DR PATRIC; fig|36816.3.peg.7388; -.
DR Proteomes; UP000037773; 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; IPR018366; CBM2_CS.
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; PS00561; CBM2_A; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000037773};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..461
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038784541"
FT DOMAIN 29..139
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
SQ SEQUENCE 461 AA; 48763 MW; 0B4EE8F05820E594 CRC64;
MRRNAVKRFL ALLATCATVL GLTALTGPQA AAAAGCRVDY TVAGQWQGGF QAGVRITNLG
APVSGWTLGF TMPDAGQKIV QGWNATWSQS GATVTAAAVD WNRTLATGAT VDLGFTGSFT
GANPRPTAFT LNGVACTGSV EEPPPAPDDG TPVDVNGQLH VCGVNLCNQY DRPVQLRGMS
THGLQWFSRC YDTASLDALA QDWKSDLLRI AMYVQEDGYE TDPAGFTGRV NSLVDMAEAR
GMYAVIDFHT LTPGDPNFNL DRAKTFFASV AARNAGKKNV IYEIANEPNG VSWAAVKSYA
EQVIPVIRAA DPDAVVIVGT RGWSSLGVSD GSNENEVVDN PVNATNIMYA FHFYAASHKD
AYRATVSRAA SRLPLFVSEF GTVSATGGGA VDRASSTAWL DLLDQLKISY ANWTYSDADE
GSAAFRPGTC GGTDYSGSGV LTESGALLKS RISTPDTFPT R
//
