ID A0A395JFQ9_9GAMM Unreviewed; 626 AA.
AC A0A395JFQ9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=DFR28_10655 {ECO:0000313|EMBL:RBP48569.1};
OS Arenicella xantha.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Arenicellales;
OC Arenicellaceae; Arenicella.
OX NCBI_TaxID=644221 {ECO:0000313|EMBL:RBP48569.1, ECO:0000313|Proteomes:UP000253083};
RN [1] {ECO:0000313|EMBL:RBP48569.1, ECO:0000313|Proteomes:UP000253083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24032 {ECO:0000313|EMBL:RBP48569.1,
RC ECO:0000313|Proteomes:UP000253083};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-2018) 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|ARBA:ARBA00000966,
CC ECO:0000256|RuleBase:RU361153};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|RuleBase:RU361153}.
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:RBP48569.1}.
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DR EMBL; QNRT01000006; RBP48569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395JFQ9; -.
DR InParanoid; A0A395JFQ9; -.
DR OrthoDB; 9775889at2; -.
DR Proteomes; UP000253083; 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; cd04080; CBM6_cellulase-like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361153};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000253083};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..626
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017372820"
FT DOMAIN 381..503
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 518..626
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 336..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 65478 MW; BCC125C2B7169F82 CRC64;
MPFYQARTLL SKLGLMSRFL RPFAISLSIL ISFTASAAVA PLTVNGSQIL VGGQAQGLAG
NSYFWSNTGW GAERFYNADA VAWLKNDWKS NIVRAAMGVD EAGGYLSDQA GNKARVTAVV
DAAIAQDMYV IIDWHTHHAE DYRTDAVAFF SEMAQTYGSH NNVIYEIYNE PLQVSWSSTI
KPYAEAVIGA IRAHDPDNLI VVGTPTWSQD VDQAAADPIT AYSNIAYALH FYAGTHKQWL
RDRAEQAMNA GIAIMVTEWG SVNASGDGAV DTAETNAWVN WMAQYNLTHL NWSVHDKAEG
ASILQPGASS TGNWPSSTLT ASGAFVRDII RAYNDGTDTG GGDNGGGDNG GGDNGGGDNG
GGDNGGGNSP CDSASAIGLP GTVQAEDFCQ QSGIQTEATS DTGGGDNIGW IQNGDSSQYR
VNVSAADTYQ VELRVATPTI GGSVDILVDG NKVGSIAVGD TGGWQNWQTK STDVQLNAGQ
QTLRLNYVGG SDYLMNINWA KFNLQADNGG GDNGGGDNGG GNTGVSCDFI IANQWSSGFV
GEVKITNNGT SAISSPWSVN FGFSDGSNVT SSWNGNLSGS NPYTIAPLSW NQTIQPGGST
SFGVQVNKGA SGQPASTPTV GGSICN
//
