ID D2KFM4_9FIRM Unreviewed; 621 AA.
AC D2KFM4;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:ACZ98626.1};
DE Flags: Fragment;
OS Cellulosilyticum ruminicola.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC Cellulosilyticum.
OX NCBI_TaxID=425254 {ECO:0000313|EMBL:ACZ98626.1};
RN [1] {ECO:0000313|EMBL:ACZ98626.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.5065 {ECO:0000313|EMBL:ACZ98626.1};
RX PubMed=20400560; DOI=10.1128/AEM.03124-09;
RA Cai S., Li J., Hu F.Z., Zhang K., Luo Y., Janto B., Boissy R., Ehrlich G.,
RA Dong X.;
RT "Cellulosilyticum ruminicola, a newly described rumen bacterium that
RT possesses redundant fibrolytic-protein-encoding genes and degrades
RT lignocellulose with multiple carbohydrate- borne fibrolytic enzymes.";
RL Appl. Environ. Microbiol. 76:3818-3824(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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DR EMBL; GU211302; ACZ98626.1; -; Genomic_DNA.
DR AlphaFoldDB; D2KFM4; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF13; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00930)-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF14200; RicinB_lectin_2; 2.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 519..621
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 507..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACZ98626.1"
FT NON_TER 621
FT /evidence="ECO:0000313|EMBL:ACZ98626.1"
SQ SEQUENCE 621 AA; 67985 MW; 7413DDCD17A47CE5 CRC64;
SGKNLVGNSL FEGTQAIKVN GYYYVFNIAW PSGKPRSQYV SRSKSLNGPW ESRIVLQDNF
DNVGGVAQGG IVDTEDGQWY GLLFQDHGPV GRCPILVPVN WVNGWPMMGT NGRVQKTMNK
PASISSEKVI VKSDEFNGDS GKTYKSGLDL VWQWNHNPDN NSWSLKEKPG CLRLKTSGIT
NSLTSARNTL TQRTYGPTCS GKVAVDVSNM KNGDVAGLAA FSYKYGYVGI KMENGVKKIV
MVNASNNSIP QEIESVNLNS NKVYFKIDFN FEGGNRANFY YSVDGENWKK IGNSLSMEYT
LDHFMGYRFG LFNYATKTTG GYVDFDYFRV SDELKGANTE KEETKPPVVV TPSTNYATLK
DGWYYIKNTG SGKYLQVAGD KGGNGVNVEI GTGTGSTGQK WYLTNVGNGY FTLKNGHDYA
LDLVYGKDED MTNIQVYSPN GMDAQQFKLL PTDKANVYGI VTKASTDVRG LDVEGRGVTD
GANVIQYQYN GASNQIWTLE NCEVSGSGSE VVNPNPSEEQ KPSQGETLSV KVTSDWGSGA
VGDITLTNTT GKDLNGWTCT FTTDRPITSI WNVELVSKEG NTYTVTNPAW KANLAKDESY
TFGCQLSNGD GDVKVTNVSL K
//
