ID A0A428XN24_9ACTN Unreviewed; 510 AA.
AC A0A428XN24;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=DMB66_33300 {ECO:0000313|EMBL:RSM56727.1};
OS Actinoplanes sp. ATCC 53533.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1288362 {ECO:0000313|EMBL:RSM56727.1, ECO:0000313|Proteomes:UP000287606};
RN [1] {ECO:0000313|EMBL:RSM56727.1, ECO:0000313|Proteomes:UP000287606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53533 {ECO:0000313|EMBL:RSM56727.1,
RC ECO:0000313|Proteomes:UP000287606};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) 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:RSM56727.1}.
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DR EMBL; QHHV01000114; RSM56727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428XN24; -.
DR OrthoDB; 9800955at2; -.
DR Proteomes; UP000287606; 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; PTHR31297:SF17; ENDOGLUCANASE; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 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, ECO:0000313|EMBL:RSM56727.1};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000287606};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..510
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019541456"
FT DOMAIN 410..510
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 396..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 54233 MW; 096A1870292C8B51 CRC64;
MGSRVRKAGF AFLAAMLAFT GSVSGVANPA SAGVVAQLTA SQLVADMGAG WNLGNSLEAN
ANGIPSETAW NNPTVTQALI DRVQAAGFKT IRIPVAYLGH IGSGPDYTVN PAWLNRIQEV
VNYAYSRGLY VLINMHGDGY KSVTGSWLIC DSSAQATIRD KYQKVWQQVA TRFQSYNEHL
IFESMNENFD GQYGNPTQPC YSNINTYNQI FVDAVRRAGG NNTSRWLLVP GWNTNIDYTA
GNYGFVLPTD QYRSPAIPGN EQRIMISVHY YDPWDFAGTE DGAITQWGSD ATNPAKTSTW
GQEDFLDAQF KKMYDTFVVR GYPVFIGEYG AVDKTSFDSS NNRYRANFAR TVVATAKKYG
AATAYWDNGF NGQYGLGIFN RSSATVTQQG IIDAIMGASP PPSSPPPSSP PPGATGCTAT
ISTNAWTGGF VATVKVTAGA AALISWSVSI TLPAGTAVTS SWNSQAAGTT GTVRFANASY
NGSVPAGGST EFGFQGTGGP PTGAPTCTAS
//
