ID G8NNS9_GRAMM Unreviewed; 739 AA.
AC G8NNS9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:AEU35954.1};
DE EC=3.2.1.21 {ECO:0000313|EMBL:AEU35954.1};
DE Flags: Precursor;
GN OrderedLocusNames=AciX8_1615 {ECO:0000313|EMBL:AEU35954.1};
OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU35954.1, ECO:0000313|Proteomes:UP000007113};
RN [1] {ECO:0000313|EMBL:AEU35954.1, ECO:0000313|Proteomes:UP000007113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC {ECO:0000313|Proteomes:UP000007113};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA Haggblom M., Woyke T.;
RT "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003130; AEU35954.1; -; Genomic_DNA.
DR RefSeq; WP_014264833.1; NC_016631.1.
DR AlphaFoldDB; G8NNS9; -.
DR STRING; 682795.AciX8_1615; -.
DR KEGG; gma:AciX8_1615; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_3_0; -.
DR Proteomes; UP000007113; Chromosome.
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:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic 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; IPR044993; BXL.
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; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:AEU35954.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEU35954.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007113};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..739
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003512796"
FT DOMAIN 656..726
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 739 AA; 80294 MW; 2FB39B2E339193B3 CRC64;
MLAQKFSLSL NSKTTVPVRT AFLLLCLVPV ASVMAAQKVA APPVYLDSHA DPESRVTALL
AAMTLDEKIH ALSTDPSVPR LGVAGTNHVE GLHGLALGGP GHWEGHSEGR TMLNVIPTTQ
FPQSRGLGQT WDPALLQKAA AQEAYETRFA FGKYHRGGLV VRAPNADLSR DPRWGRGEES
YGEDPFLVGT LATAFAHGLQ GDDPHVWMTA SLLKHFLANS NEDGRDGSSS NFDARLFHEY
YAVPFRMAIE EGHADAMMTS YNAWNSVPMT ANPVVRDVVM AQWGLDGIVC TDAGALTNMV
KQHHTYATMP EAAAAAIHAG INQFLDDYQQ PVRDALQQKL ITEQDIDRNL RGVYRVMLHL
GLLDPTANSP YSHIGAFDQA QSDPWNTEAP RALVRRATDE SIVLLKNTGG ALPLDAAKLK
SIAVIGQWGD TVALDWYSGT PLLSVTPVEG IRRRAAGASV VFNDGKDEAA AAALAARSEA
VIVIVGNHPT CDAGWNKCAL PSEGKEAIDR KSLTLPDESL VKAVLAANPH AVVVLQTSFP
YTTNWTQEHA PAILEITHNS EEQGTALADV LFGDYNPAGR LTQTWPASLE QLPPMMDYDL
RHGRTYLYAE KAPLYPFGFG LSYTSFAYSD LTVTQRGKSI AVQVTVANTG SRAGDEVVQI
YAAHQGSTVP RPIEELKAFR RVALRAGEKQ VVRFEMPVTS LAYWDEATHR FIVEGDRVEF
RAAASSADVR LKHTLLVQP
//