ID A0A0A0BYA2_9CELL Unreviewed; 456 AA.
AC A0A0A0BYA2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=N869_00990 {ECO:0000313|EMBL:KGM12901.1};
OS Cellulomonas bogoriensis 69B4 = DSM 16987.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM12901.1, ECO:0000313|Proteomes:UP000054314};
RN [1] {ECO:0000313|EMBL:KGM12901.1, ECO:0000313|Proteomes:UP000054314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=69B4 {ECO:0000313|EMBL:KGM12901.1,
RC ECO:0000313|Proteomes:UP000054314};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL Submitted (AUG-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|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:KGM12901.1}.
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DR EMBL; AXCZ01000084; KGM12901.1; -; Genomic_DNA.
DR RefSeq; WP_035060477.1; NZ_AXCZ01000084.1.
DR AlphaFoldDB; A0A0A0BYA2; -.
DR OrthoDB; 9801198at2; -.
DR Proteomes; UP000054314; 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; 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; 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.
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:UP000054314};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..456
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001960120"
FT DOMAIN 355..456
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 331..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 47936 MW; 28714FC76B95CAAB CRC64;
MRTKHWLAGL AAVALALPVA ASPAAAAEPP GFRIDDGRLV ESDGSPFVMR GVNHAHTWYT
DRTESFAGIS SLGANAVRTV LSSGHRWTRN DVDDVREVIE LAKQARLVSV LEVHDTTGYG
EEGAAASLAQ AVEYWISVKP ALDGQEDYVL LNIGNEPFGN DATANQRYVT DTISAIQTLR
RAGFAHTIVV DAPNWGQDWQ HIMRDNAQRI FDADPDANVL FSIHMYGVYA QGSTVRSYFD
AFERAGLPLI VGEFGNTHSD GEVDEDTILA EAQARGIGWL GWSWSGNSGG VEYLDLTHDF
DASSLTPWGE RLFHGPDGIA RTAQRAAVFA GTTPTPTPTP TTPTPTPTTP APTPTPTPAE
GCTAELAVIG SWSGGFQAEV RVTAGTAAIE GWSTSFTLPA GTTIQNLWGG SATGSAGEVT
VVNAAWNGGL SAGQGASFGF IGAGPAPSGP VTCAAR
//
