ID A0A1C4UE94_MICEC Unreviewed; 462 AA.
AC A0A1C4UE94;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=GA0070618_0252 {ECO:0000313|EMBL:SCE69983.1};
OS Micromonospora echinospora (Micromonospora purpurea).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1877 {ECO:0000313|EMBL:SCE69983.1, ECO:0000313|Proteomes:UP000198253};
RN [1] {ECO:0000313|EMBL:SCE69983.1, ECO:0000313|Proteomes:UP000198253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43816 {ECO:0000313|EMBL:SCE69983.1,
RC ECO:0000313|Proteomes:UP000198253};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; LT607413; SCE69983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4UE94; -.
DR InParanoid; A0A1C4UE94; -.
DR OrthoDB; 9801198at2; -.
DR Proteomes; UP000198253; Chromosome i.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..462
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008704759"
FT DOMAIN 359..462
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 327..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..364
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 48408 MW; E0B9B4FF4F45477D CRC64;
MKTRLSVVAA TLLAFVVSLV AFGGQPAHAA TGFTVANGKL YDANGAEFVM RGVNHAHTWY
THQTSSFANI KALGANTVRV VLSSGQRWTK NETADVANVI SLCKQNRLIC VLEVHDTTGY
GEQAGAATLA QAVDYWISVQ SALTGQEKYV IVNIGNEPYG NQNYSGWATD TANAIKRLRT
AGFAHTIMVD GPNWGQDWTY TMRDNAASVF AADPAKNTVF SIHMYGVFNT AAKISDYLGR
FRTAGLPIVV GEFGHNHSDG DPDEDAILSY SQANGIGYLG WSWSGNGGGV EYLDMAINFD
PANLSSWGQR IFNGANGIKQ TAKEATVFGS TPPTTPPPTT PPPTTPPPTT PPPTTPPPTT
PPPGGCTATY TVTGSWQGGF QGEVKVTAGS AAIRGWTVNW TFANGQTVTQ SWNATVTSSG
SAVTARNVAY NGNLGAGAST TFGFIGATSG GNTAPTPTCT AA
//
