ID A0A1H7Y4C9_9BACT Unreviewed; 822 AA.
AC A0A1H7Y4C9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361167};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361167};
GN ORFNames=SAMN04488505_104288 {ECO:0000313|EMBL:SEM40188.1};
OS Chitinophaga rupis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=573321 {ECO:0000313|EMBL:SEM40188.1, ECO:0000313|Proteomes:UP000198984};
RN [1] {ECO:0000313|EMBL:SEM40188.1, ECO:0000313|Proteomes:UP000198984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21039 {ECO:0000313|EMBL:SEM40188.1,
RC ECO:0000313|Proteomes:UP000198984};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC {ECO:0000256|ARBA:ARBA00009209, ECO:0000256|RuleBase:RU361167}.
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DR EMBL; FOBB01000004; SEM40188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7Y4C9; -.
DR STRING; 573321.SAMN04488505_104288; -.
DR Proteomes; UP000198984; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002037; Glyco_hydro_8.
DR InterPro; IPR019834; Glyco_hydro_8_CS.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; NF033679; DNRLRE_dom; 1.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF01270; Glyco_hydro_8; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR PRINTS; PR00735; GLHYDRLASE8.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361167};
KW Glycosidase {ECO:0000256|RuleBase:RU361167};
KW Hydrolase {ECO:0000256|RuleBase:RU361167};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361167};
KW Reference proteome {ECO:0000313|Proteomes:UP000198984};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..822
FT /note="Glucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011662970"
FT DOMAIN 397..540
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT ACT_SITE 155
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10058"
SQ SEQUENCE 822 AA; 88124 MW; 06D5C37E786D63F3 CRC64;
MRKPYAILAT GMLCIAGLIV QAQKKPFPQA VSYPGCIKPN NVTQADMNTS VASFYDYWKS
KYLKNNLASL PGGYYIKGEI SGDADGYTPL GSSEGQGYGM VITVLMAGHD ANARTIYDGL
FKTARAYRSS INSNIMGWVV ADNASAQGHF DSATDGDIDI AYSLILAHYQ WGSDGAINYL
NEAKKMITNG IKAANVTTTN RLNLGDWDSK SALNTRPSDW MLSHMRAFYQ ETNDAAWLNL
INNLYSVYNQ FSATYSPSTG LISDFVVKNP PEPAPKNFID EGPQTNEYNY NACRVPLRVV
MDYALYGSTS AQTISNKIAT WIIQKSGGNP ASIRDGYQLN GTTSGTDPEA VFVAPFVAAA
VANSANQAFV NSGWNFLKTK KSGYYSDSYS LLCQLFISGN WWKPEAGTTP PPACVPASAS
SDDGNVATNV LDNDLNTRWS ASGDGQWIQL CLDNPVSVTG VDIAFYQGNT RRALFDVQTS
TDGLTFTNAA TGLQSSGTSL ALESFTFAAK TAKYVRILGH GNNVSAWNSY TEVKVRTGTQ
SGQQVTLSAA KDAYVRNGVY ADSAYGALDP VNLISKLNST TTTGNDRQAY LGFDLSSVSG
TITSAVLKVY GHQDDNRVTN VPVGAYPVAN TTWTEAGITW NNKPAPGATA LATATVTDSI
GRYYSWDITA YVQSEKAAGR SAISLALLNG LMANPRTLWN SKETGSNAPQ LVITTTSTAK
TAARQAFVAS PSDTHGDKLQ QVSVFPNPLS SNATVAFTLQ QAGPVHLAVY NTNGEVVKVL
ANEQLPAGRH TRTFAPGNMP GGLYVLKLVH NGKVSTVKLV KQ
//
