ID A0A1Y0FWC7_9GAMM Unreviewed; 883 AA.
AC A0A1Y0FWC7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=CBR65_07655 {ECO:0000313|EMBL:ARU27323.1};
OS Cellvibrio sp. PSBB006.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1987723 {ECO:0000313|EMBL:ARU27323.1, ECO:0000313|Proteomes:UP000196143};
RN [1] {ECO:0000313|EMBL:ARU27323.1, ECO:0000313|Proteomes:UP000196143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB006 {ECO:0000313|EMBL:ARU27323.1,
RC ECO:0000313|Proteomes:UP000196143};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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}.
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DR EMBL; CP021382; ARU27323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0FWC7; -.
DR KEGG; cell:CBR65_07655; -.
DR OrthoDB; 9808897at2; -.
DR Proteomes; UP000196143; Chromosome.
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; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.30.32.30; CBM10; 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; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR036601; CBM10_sf.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR009031; CBM_fam10.
DR InterPro; IPR004197; Cellulase_Ig-like.
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; PF02013; CBM_10; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM01064; CBM_10; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR SUPFAM; SSF57615; Type X cellulose binding domain, CBDX; 1.
DR PROSITE; PS51763; CBM10; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000196143};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 691..720
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 780..883
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 640..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 539
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 589
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 598
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 883 AA; 92445 MW; E44857130AAA4643 CRC64;
MTQAPKTNKP AYSKPLLTSR LNTSAPRILT RAISAVVLSG LVAGSAWAAV GNPRVNQVGY
LPNSAKVATY SSDALAALPW ELRLNGTLVT SGTTMPRGVD AASGDNIHII DISGVTTEAD
GYKLYVGNDE SYPFEIAADA FTGALYDSIK YFYHNRSGIA IETAYTGGGN TSYAPNAQWA
RPAGHLNMGA NQGDYDVPCW SGTCNYSLDV TKGWYDAGDH GKYVVNGGIS VWKLLTMYER
ALHLSDNAGA FADGTLNIPE SGNGVPDILD EVRWQMEFML SMQVPQGQAK AGMVHHKMHD
VGWTGLPLAP HEDSQARALV PPSTAATLNV AATAAQCARL WQNIDAAFAS TCLTAAERAW
DAAQQNPSDL YTGGYDNGGG GYGDRFVADE FFWAAAELYI TTGDSKYLPT IQNYEIERTD
FGWPDTELPG LISLATVPAS HTASLRTSAR QTIVQIADYH LGVIDSTGYL TPHTEEEYYW
GSNNGVANKL FLVGLAYDFT GNEDYAKGVG KAVDYLFGRN TLSFSYISGH GENALTQPHH
RFWAGALNGA YPWLPPGAFS GGPNAGLEDE VAQGALNGCQ TRPATCYMDD INSWSTNEIT
INWNSALAWV LAFYDDYGNE GGASSSSSSQ ISSSVASSSS SSASSIPVSS SSSSSAPVSS
SSSSISSSVV ASSSSSLASS SSSSSMPTGQ QCNWYGTLYP LCVTTQSGWG WEQNRSCISR
STCSSQPAPW GIVGGGTSSS SPASSSPSSS SSPASSSSSS APASSSSSSL VASSSSSSSA
PNGSGSCEYV VTNQWNNGFT GAIRITNNGS SPINGWSVSW NYNDGSRITN SWNANLSGSN
PYSASNLGWN GTLQPGQTAE FGFQGTKGGS AASVPVVSGA PCN
//
