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Database: UniProt
Entry: I8W068_9BACE
LinkDB: I8W068_9BACE
Original site: I8W068_9BACE 
ID   I8W068_9BACE            Unreviewed;       672 AA.
AC   I8W068;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=CBM6 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1062_02243 {ECO:0000313|EMBL:EIY32060.1};
OS   Bacteroides cellulosilyticus CL02T12C19.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=997874 {ECO:0000313|EMBL:EIY32060.1, ECO:0000313|Proteomes:UP000003741};
RN   [1] {ECO:0000313|EMBL:EIY32060.1, ECO:0000313|Proteomes:UP000003741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL02T12C19 {ECO:0000313|EMBL:EIY32060.1,
RC   ECO:0000313|Proteomes:UP000003741};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA   Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides cellulosilyticus CL02T12C19.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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:EIY32060.1}.
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DR   EMBL; AGXG01000051; EIY32060.1; -; Genomic_DNA.
DR   RefSeq; WP_007216948.1; NZ_JH724086.1.
DR   AlphaFoldDB; I8W068; -.
DR   GeneID; 66306324; -.
DR   PATRIC; fig|997874.3.peg.2298; -.
DR   HOGENOM; CLU_019255_0_0_10; -.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000003741; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; cd04084; CBM6_xylanase-like; 1.
DR   CDD; cd09001; GH43_FsAxh1-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR041542; GH43_C2.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR   PANTHER; PTHR42812:SF13; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00930)-RELATED; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF17851; GH43_C2; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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}.
FT   DOMAIN          348..534
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   DOMAIN          554..671
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|Pfam:PF03422"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        223
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            169
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   672 AA;  76475 MW;  45150A34FD31C3B5 CRC64;
     MYNLSITTGK IADGFSALLM LCCILMVQSC TVPVQTTASL SSDNGDGTYT NPVINADYPD
     PDIIRVGEDF YMVSSSFVAM PGIPICHSKD LINWRIIGHA YDSITFRPQY RMENEQTAYS
     RLCWAPSIKY HDGTYYIGVN IADDGFVMFK SNKPEGPYSM HKFDKRLYDP GFFIDDDGKK
     YVTHGKTKIY LTRLKDDGTG VLYPNDEGTL IITAPKGYEY LFEGCHTYKR NGWYYIFNPA
     LGYNGVQMIS RSRNLYGPYE TKVLIDDDIN YADAGVHQGG YVETLEGESW AYTFQDRDYM
     GRCVMLYPMK WEEDWPVVGP EGKPGKGVVT YRKPAVKAKQ EITFPQHSDD FSSSKLAHVW
     EFNHVPRKDK WSLTDRPGYF RIYAQYAKGF EWARNSLTQK VSGPYSTGTV SLDLTGLREG
     DFAGNGIMGR VMYQLGVRKK ADGFWLEMRQ GGREGETVVD SLPVKTDKIY LRTEVTKQGS
     LLFYYSLDNL EYNRLGPEGV SNFWGFLGIR HALCCYNLNK GATGGYADFD YFELESNRRG
     NHYDAFTEID FSQYDDREGM KLVRPVAKRP MQFISGVRDG NWLVFNNMCF KQNPQKVTIE
     LQAETPGTVI EIREGSLDGK LIATCPINQN QTPGEWEKQA FEVSGAVKDK SKIYFLFRGQ
     SQGLAIKNFV FY
//
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