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Database: UniProt
Entry: G8NNS9_GRAMM
LinkDB: G8NNS9_GRAMM
Original site: G8NNS9_GRAMM 
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
//
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