ID A0A0N0T8K4_9NOCA Unreviewed; 859 AA.
AC A0A0N0T8K4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=ADL03_21800 {ECO:0000313|EMBL:KOV83178.1};
OS Nocardia sp. NRRL S-836.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV83178.1, ECO:0000313|Proteomes:UP000037746};
RN [1] {ECO:0000313|Proteomes:UP000037746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-836 {ECO:0000313|Proteomes:UP000037746};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
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|RuleBase:RU361166};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|PROSITE-ProRule:PRU10060, ECO:0000256|RuleBase:RU361166}.
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:KOV83178.1}.
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DR EMBL; LGDY01000102; KOV83178.1; -; Genomic_DNA.
DR RefSeq; WP_053735329.1; NZ_LGDY01000102.1.
DR AlphaFoldDB; A0A0N0T8K4; -.
DR STRING; 1519492.ADL03_21800; -.
DR PATRIC; fig|1519492.3.peg.4683; -.
DR OrthoDB; 9808897at2; -.
DR Proteomes; UP000037746; 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 CDD; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR004197; Cellulase_Ig-like.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Reference proteome {ECO:0000313|Proteomes:UP000037746};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 31..859
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5005732772"
FT DOMAIN 752..859
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT ACT_SITE 720
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 729
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 859 AA; 90085 MW; 06FC3E9220A84503 CRC64;
MRSQPPRLLA AALLTALAAT AIPAAGTAEA AEYERVLNGK FDSGSADPWW SSAGVTNRIT
GGELCASVTG GTTNPWDALV GQNGVPFESG QSYTLSFDAH ATTAQPVAAA AGESVSPYRG
IARQEFAVTP TKQHFTFSFT STLDFPDAGN GQVAFQLGGQ TADNTICVDN VSLVGGVKPP
GGVVPNPTRK VQVDQVGYVP GLPKRATLVS TATTPQTWTL KNSAGATVAS GQSTPKGADA
TSGDSVHSID FSSFDTPGTG YTLVVGTDSS FPFDISADVV KKLRYDALAF FYHQRSGTPI
EAQYVGDQYA RPAGHINVAP NQGDNNVPCR ADLACGYTLD VRGGWYDAGD HGKYVVNGGI
SAWQLLNSYE RAARIGDASA FRDGTLAIPE KANGVPDLLD EARWEVDFLL KMQAPDGMAH
HKVHDANWTA LPTRPELDDQ PRRLSATSTA ATLNLAAVAA QASRLWKSVD ATYSAKLLTA
ARKAYAAAKA NPNKIADPND GTGGGAYSDN TVSDEFYWAA AELYATTGES AYGTDVTSSP
HYKAASLTRA GFYWGGTAPL GDITLALVPT GLPAADVTAI KTAFATVADQ HLAAMAQMGY
ATPYDNSVDG YVWGSNSAVL NNAQVLALAH DFTGADKYRD GVFEALHYLL GRNPLSTSYV
AGYGEQAVQN VHHRFWAKQN DPTLPIAPPG SLSGGPNSGL QDPIVQRLLP GCPQQKCWVD
DIGAYSVNEV AVNWNSALAW VSGWAAEKSG KPPVPVADCE VTFTANRWSS GLSANVAVKN
TGTTAWTSWK LGFALPGTQQ VTAGWSANWS QTGRDVTATN MSWNGKVEAG KSVYIGFNAS
GAGGDPTAFT INGKSCKTG
//
