ID A0A087C6U2_9BIFI Unreviewed; 812 AA.
AC A0A087C6U2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:KFI78992.1};
DE EC=3.2.1.21 {ECO:0000313|EMBL:KFI78992.1};
GN ORFNames=BMON_1402 {ECO:0000313|EMBL:KFI78992.1};
OS Bifidobacterium mongoliense DSM 21395.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437603 {ECO:0000313|EMBL:KFI78992.1, ECO:0000313|Proteomes:UP000029082};
RN [1] {ECO:0000313|EMBL:KFI78992.1, ECO:0000313|Proteomes:UP000029082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21395 {ECO:0000313|EMBL:KFI78992.1,
RC ECO:0000313|Proteomes:UP000029082};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:KFI78992.1}.
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DR EMBL; JGZE01000003; KFI78992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087C6U2; -.
DR STRING; 1437603.GCA_000771525_00947; -.
DR eggNOG; COG1472; Bacteria.
DR Proteomes; UP000029082; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:KFI78992.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFI78992.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029082}.
FT DOMAIN 581..650
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 812 AA; 87490 MW; 8E4698679D167C59 CRC64;
MRDDLSITEQ AALLSGASEW ESRANERAGV PAFVMSDGPH GVRRQLGSGD HLGLGESKPA
TCFPTAGTVA NSWDPVLVER MGRALGREAH DLDVNILLGP GMNIKRNPLC GRNFEYFSED
PIVSGRMAAG LITGVQSQGV GACPKHFAVN SQELRRQSSN SVVDDRTMRE LYLTAFEIAV
REAKPWSVMT SYNRVNGVYA HENAHLLQDI LRKEWGFDGW LSPTGGGSNS AVAAVRAGGS
LEMPSPGYTS VRELVAAVHA GTLSKDDVER RAREVATTAR RTGGRQVDRN GVLRPDVIDA
HHDIARQVAE ASDVLLKNDG RVAGGSVLPL KRGTRVAIIG DMAKIPRFQG SGSSKVNATR
SESLLDQFMR SSDVAVAGYR QGYERRCAPN TVLLDDAVAL AADKGTDVVV VVIGLDERSE
SEGLDRSTMA IPQLQVDLIG ALHATGKPIV AVLVAGSPVQ TSWIDDADAV LYVGLSGQAG
ASAAVRILTG EVNPSGRLAE TWPIDYADCP SAAWYPADGP DAIYREGPFV GYRYYRTADI
PVRFPFGYGL SYASFSFGAL SVNDDGVSFT VTNTSDVEGA TVAQLYVRGP QVGYSGRIVN
SSFIKVRLAA HERRVVHIDF DQYTFRHYDP TVQRWCTESG SWTVMVGEDC DHDRLRAQFT
VEGDVEPVPA DPALGAYLTG RVKDATDDEL ATLFRGHVPL TSPSSVFGVN DPIVSWQHSR
GLVARAVART LVRREARISR KKGAPDLDTL FVLNMPPRAM SKMTGGLVDG AMVDAIVLVA
NGHAVRGLGA FVVAYLRNRS AARNIAKELH HD
//
