ID R7FBU6_9FIRM Unreviewed; 876 AA.
AC R7FBU6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=BN611_01573 {ECO:0000313|EMBL:CDE12310.1};
OS Ruminococcus sp. CAG:330.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1262954 {ECO:0000313|EMBL:CDE12310.1, ECO:0000313|Proteomes:UP000018377};
RN [1] {ECO:0000313|EMBL:CDE12310.1, ECO:0000313|Proteomes:UP000018377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:330 {ECO:0000313|Proteomes:UP000018377};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE12310.1}.
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DR EMBL; CBIH010000080; CDE12310.1; -; Genomic_DNA.
DR AlphaFoldDB; R7FBU6; -.
DR STRING; 1262954.BN611_01573; -.
DR Proteomes; UP000018377; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
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; 2.60.120.260; 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; 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; 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; PF02018; CBM_4_9; 1.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 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; 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|ARBA:ARBA00023001,
KW 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Reference proteome {ECO:0000313|Proteomes:UP000018377};
KW Signal {ECO:0000256|RuleBase:RU361166};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 25..876
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5039741693"
FT TRANSMEM 844..868
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..174
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 211..289
FT /note="Cellulase Ig-like"
FT /evidence="ECO:0000259|Pfam:PF02927"
FT DOMAIN 302..787
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT REGION 807..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 715
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 766
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 775
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 876 AA; 95453 MW; BF453D2B10BAA530 CRC64;
MRQNRVLGVL TALTIAVTSG SALPALSVSA GQLLGQTDFE DGVGLPWHVC ESASGKMSFE
VTDSAYRITV DNPGGASNGG EDRWDCQFRH RGLTLVSGCT YEVAYDITAS NNCTYYTKIG
DMSEPFTEDW HGNPDDSQFD AFWNVQNLTA NQTVSFHGTF TAKRTAEVEW AFHVGGDTVS
VGTVFTFDNM SLICTDNDEY DYVPTQEWQR ADIVTNQIGY FPDCRKQATL ISDETDAVDF
SLCDESGKEV YTGASKPMGE DPDSGDSVHI LDFSEFKEAG TYTLQAGNAA SREFAIGGTE
VYSGMLFDAL NYFYQNRSGI AIESQYITSG DAAALARSAG HSNDTARITT DWDDLQSNGG
SQNVSGGWYD AGDHGKYVVN GGIALWMMQN QYERAVSRKT EDSYADDTMQ IPEQQNGYPD
LLDEARWEME WMLKMIVQDG TYQGMAYHKV HDIKWTALGM APADDQEERI LKPPTTCATL
NLAACAAQAA RLWEPYDADF AKECLTAAEN AYEAAKKHDD LYAPLDQSIG GGPYGDDCAD
DEFYWAACEL YLTTGEKAYL KDLEKSDLAY TVPTTLSAGE DADTAGSFDW GNTAALGTLS
FALHKDDLEK KVAKKVTNAI TDAADVHLGR EEQQGYGQPY AQSKLSYADD DTGYVWGSNS
FVADNTVILA AAYDLTGEQN YLNGVISAMD YLLGRNPMDV SYITGYGSHA VQYPHHRYWA
HQISEEYPMA PAGVLVGGPN SGMQDPWVQG SGWKKGEIAP AKCYLDNIEA WSVNECTINW
NAPLAWLTAF VCDANGGIVA NTGSMASEQL DPSAGDSEES SQTSAGSNQQ NQANDSTEKS
SSGAFPWTLV IVLGAILLGA IIVEVFIYKI VKLKKN
//
