ID A0A269WBU1_9BACL Unreviewed; 912 AA.
AC A0A269WBU1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=CHH75_05945 {ECO:0000313|EMBL:PAK54890.1};
OS Paenibacillus sp. 7541.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2026236 {ECO:0000313|EMBL:PAK54890.1, ECO:0000313|Proteomes:UP000215741};
RN [1] {ECO:0000313|EMBL:PAK54890.1, ECO:0000313|Proteomes:UP000215741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7541 {ECO:0000313|EMBL:PAK54890.1,
RC ECO:0000313|Proteomes:UP000215741};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (AUG-2017) 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:PRU10059, 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:PAK54890.1}.
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DR EMBL; NQLZ01000008; PAK54890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A269WBU1; -.
DR Proteomes; UP000215741; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00942; CBM_3; 2.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM01067; CBM_3; 2.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51172; CBM3; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU10059};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU10059};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Reference proteome {ECO:0000313|Proteomes:UP000215741};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 36..912
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5011823052"
FT DOMAIN 496..657
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT DOMAIN 667..758
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 760..912
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT ACT_SITE 414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 452
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 461
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 912 AA; 100851 MW; C77508417F97AC95 CRC64;
MRSKWSKKSG ILLFSIVLAL TTMLGSMTHS PVANAAASDY NYAEALQKSI YFYEAQRSGP
LPDNNRVEWR GDSGLQDGAD VGHDLTGGWY DAGDHVKFGF PMAATATMLA WSVYEYREGY
EQAGQLDEIL DNIRWATDYF MKAHTAPNEL WGQVGNGTAD HNWWGPAEVM PMERPAYKID
ANNPGSDLAG ETAAALAASS IIFRDSDPAY ADKLLRHAKE LYDFADQYRG KYSDSITDAR
QFYNSWSGYA DELSWGGVWL YLATEDEAYL DKAIAASELW GTNQQGEWDY KWTHAWDDKH
YGAQLLLARI TEDPRFIRSV EKNIEFWTTG VQGTGERVTY TPGGLAHLDQ WGVLRYAANQ
AFLAFVYSDW VDDPAKQLNA RSFAERQILY MLGDNPRNSS YVVGFGNNPP QRPHHRTSHG
SWADSQNVPD YHRHILYGAL VGGPTATDSY TDSISDYVSN EVAIDYNAGF TGALARMMIL
HGQGQQPLPS FPAPEEREDE MFVEASVNAS GSNFVEIRAL LNNRSGWPAR ASEEMSFRYY
VDLSEAVEAG YGPEDITVTA GGYNQGAAVS QLQPHDTARH IYYTTVDFTG TRIYPGGQSA
YRKEVQFRIT APLNTSFWDN TNDFSFQGLA PQGASPIKTP YIPVFDAGQH VFGELPQGGG
NPGEPVAPAA PRNVTAVPGD SLVRLTWNAV SGAHDYAVRR SLVSGGPYET IGTTTEPAYI
DTDVVNDTAY YYVITARNAA GESLPSTQVN ARPRVAPVPV EGDLKVQYRN GDGSSADNQI
RPHFRIVNTS EETVPLSEIT LRYYYTIDGD VPQQFHCDYA VIGSGNVNGR FVKLDSAQTG
SDYYLEISFA PGAGSLAPGA DSGEIQARFN KSNWSNYNET DDYSYNGTQQ TFADWDKVTL
YRNGTLIWGV EP
//
