ID A0A371JFJ1_9FIRM Unreviewed; 891 AA.
AC A0A371JFJ1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=CG710_009585 {ECO:0000313|EMBL:RDY31483.1};
OS Lachnotalea glycerini.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnotalea.
OX NCBI_TaxID=1763509 {ECO:0000313|EMBL:RDY31483.1, ECO:0000313|Proteomes:UP000216411};
RN [1] {ECO:0000313|EMBL:RDY31483.1, ECO:0000313|Proteomes:UP000216411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-19302 {ECO:0000313|EMBL:RDY31483.1,
RC ECO:0000313|Proteomes:UP000216411};
RX PubMed=29051240;
RA Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Raymond F.,
RA Brodeur S., Corbeil J., Isabel S., Omar R.F., Bergeron M.G.;
RT "Draft Genome Sequence of a Sporulating and Motile Strain of Lachnotalea
RT glycerini Isolated from Water in Quebec City, Canada.";
RL Genome Announc. 5:e01059-17(2017).
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:RDY31483.1}.
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DR EMBL; NOKA02000015; RDY31483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371JFJ1; -.
DR OrthoDB; 9758662at2; -.
DR Proteomes; UP000216411; 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 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; IPR005102; Carbo-bd_X2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_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 InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00942; CBM_3; 2.
DR Pfam; PF03442; CBM_X2; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM01067; CBM_3; 2.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51172; CBM3; 2.
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:UP000216411};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 482..637
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT DOMAIN 740..891
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT ACT_SITE 401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 448
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 891 AA; 97594 MW; 93830F89BE7A8713 CRC64;
MEESMRKSWS KLVAAALVCT LLPVQGIKAE AANYNYGEAL QKAVMFYEFQ RSGELPENTR
NNWRGDSGLT DGADVGLDLT GGWYDAGDHV KFNIPMAYSA TMLAWSVYEA KDALIESGQL
DYQMDNIKWV SDYLMKCHPE ANVFYYQVGN GNTDHSWWGP AEVMQMSRPS YKVDLSNPGS
SVVAQAAAEL ASTAVIFKEE DEEYAATCIS HAKELFAFAD NTKSNAGYTA ANTFYGNSSD
FYDELSWAGV WLYLATGEKE YLDKAEGYVD NWNGSAGVAY SWGQNWDDVH YGAELLLAKI
TDEPIYKKYI EQHLDFWTTG YNGERVTYTP KGLAWLSEWG SLRYATTTAF LASVYADWSG
CSAEKANTYN TFAKQQIDYA LGSTGRSYVV GFGTNSPEHP HHRTAHSSWT NSMANPTSHR
HVLYGALVGG PGKNDDYTDD INNYVVNEVA CDYNAGFVGA LAKMYEDYGG TPIENFTAME
KVTNDEYFVE ASVNASGSNF IEIKAVLNNQ SGWPAKMGDK LSFRYFVDIT KAINAGYSVS
DFKVTNNLNE GAVLSQLKPW DKENNIYYVD ADFTGTKIYP GGNSECKKEV QFRITAPSAY
EFTNDFSFTG LKTGSVAKTS YIPVYDDGVK VFGNEPGAST GEISKNSSIS VKSVSFDKAE
SNQKDISVAL TLNGNTFVGI KNGSTALAGN EDYLVNGNNV TIRKEYLAAQ NSGKLNLTFA
FSAGTDSTLA VNVSDSSVVT SGDVEVSMYN VNSQASANGI ASKIKVLNTG DTSLDLSDVK
LRYYYTIDGE KDQSFWCDWS NVGNSNITGA FGKLDTAAKG ADHYVEIGFS DAAGEISPGN
AVEVQIRFSK ADWSNYNQTD DYSFITSANE YTDTQNVTAY IAGSLAWGIE P
//
