ID K9DYL9_9BACE Unreviewed; 955 AA.
AC K9DYL9;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Beta-glucuronidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9447_02654 {ECO:0000313|EMBL:EKU90144.1};
OS Bacteroides oleiciplenus YIT 12058.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=742727 {ECO:0000313|EMBL:EKU90144.1, ECO:0000313|Proteomes:UP000009872};
RN [1] {ECO:0000313|EMBL:EKU90144.1, ECO:0000313|Proteomes:UP000009872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12058 {ECO:0000313|EMBL:EKU90144.1,
RC ECO:0000313|Proteomes:UP000009872};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides oleiciplenus YIT 12058.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:EKU90144.1}.
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DR EMBL; ADLF01000010; EKU90144.1; -; Genomic_DNA.
DR RefSeq; WP_009130211.1; NZ_JH992941.1.
DR AlphaFoldDB; K9DYL9; -.
DR STRING; 742727.HMPREF9447_02654; -.
DR PATRIC; fig|742727.4.peg.2715; -.
DR eggNOG; COG3250; Bacteria.
DR eggNOG; COG3940; Bacteria.
DR HOGENOM; CLU_308749_0_0_10; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000009872; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18820; GH43_LbAraf43-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..955
FT /note="Beta-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003929130"
FT DOMAIN 43..161
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 241..300
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 303..457
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT SITE 746
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 955 AA; 109352 MW; 7DA557B15A02BDCC CRC64;
MEIKKILIAA LLAAGMAFQV NAADVPRKEY PRPQFERATW MNLNGEWDYT FDFANSGMEQ
GYPKATSFDG KITVPFCPES SLSGVEHKDF INHIWYHREI SVPQDWSGKN VLLNFGAVYF
NSEIYIDGTL AGRHFGGSSS FSIDITKLVT PGKKHHLVVR ASSDLRSAMQ SAGKQSLQFG
SYGCNYTRTT GIWQTVWMEA VNPSGLKSVQ AIADVDQEQL IVWPAFYSDS NNKLKIILKD
GSKVVASTTV KGTNSSVAVL PVKKAKLWSP ESPFLYDITY QVIDPAGKVI DEVSSYIGMR
KVHIEGNKIY LNNKPYYQRL VLDQGFYPDG IWTAPTDEAL KRDIELSMAA GFNGARLHQK
AFEERFYYWA DKLGYITWGE APSWGMDANS IEVARNFLME WSELVLRDRN HPSLLIWTPM
NEEWWPDRVQ YPRFTTDLYN LTKSLDPTRP VNDASGGCHI KTDIWTVHNY EQDPAKLKDI
IYKDGKFFQA PNYAIGVPSA NIGFNGLRQN EMYDFPVYDG KMPYLIDEVG GIKWVKDQDK
TNSSTQSWGY GTPPKTEKEF LERLEGQMNG ILELKDQVWG YCYTQLTDVE QEQNGIYYYD
RTPKFDTKLI HDIFSKNPED VADTYTNPLL NYGPDPWALW HDGCYYYMHT MVDSLVLWKT
KDVTNIRNAE KKTIWIPTDP SNKHNLWAPE IHNIDGKWYI YYAADDGNSD NHQMYVLENV
NKDPFEGEFV MKGRISTDKD NNWAIDGSVF ENKGKLYMVW SGWQTRRVDT ETQCIYIAEM
KNPWTLGSER VLISKPELDW ERHYKNDNGW NPPHKVFVNE GPQPLKSPKG KYIHVVYSAS
GVWTPYYALG MLTADTNADL LDPASWKKSP QPLFRQSPEN GVYGTGHNSF FKSPDGKEHY
ILYHARDTQT DPPGMGDTRS PRTQKIEWKA DDYPVFGTPY PKSTRLKKPS GTQVK
//
