ID A4XH27_CALS8 Unreviewed; 770 AA.
AC A4XH27;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN OrderedLocusNames=Csac_0586 {ECO:0000313|EMBL:ABP66212.1};
OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS 6331).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP66212.1, ECO:0000313|Proteomes:UP000000256};
RN [1] {ECO:0000313|Proteomes:UP000000256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331
RC {ECO:0000313|Proteomes:UP000000256};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA Kengen S.M.W., Richardson P.;
RT "Genome sequence of the thermophilic hydrogen-producing bacterium
RT Caldicellulosiruptor saccharolyticus DSM 8903.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP66212.1, ECO:0000313|Proteomes:UP000000256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331
RC {ECO:0000313|Proteomes:UP000000256};
RX PubMed=18776029; DOI=10.1128/AEM.00968-08;
RA van de Werken H.J., Verhaart M.R., VanFossen A.L., Willquist K.,
RA Lewis D.L., Nichols J.D., Goorissen H.P., Mongodin E.F., Nelson K.E.,
RA van Niel E.W., Stams A.J., Ward D.E., de Vos W.M., van der Oost J.,
RA Kelly R.M., Kengen S.W.;
RT "Hydrogenomics of the extremely thermophilic bacterium Caldicellulosiruptor
RT saccharolyticus.";
RL Appl. Environ. Microbiol. 74:6720-6729(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; CP000679; ABP66212.1; -; Genomic_DNA.
DR RefSeq; WP_011916159.1; NC_009437.1.
DR AlphaFoldDB; A4XH27; -.
DR STRING; 351627.Csac_0586; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR KEGG; csc:Csac_0586; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_9; -.
DR OMA; WTYLQPP; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000000256; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABP66212.1}.
FT DOMAIN 670..739
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 770 AA; 85996 MW; 593EFE93DEC7E479 CRC64;
MSVEKKVNDL LQKMTIEEKV YQLTSILIQD ILENDKFSPQ KAKEKIPHGI GQITRLAGAS
NLSPQEAAKT ANEIQKFLIE NTRLGIPAMI HEESCSGFMA KGATVFPQSI GVACTFDNEI
VEELAKVIRT QMKAVGAHQA LAPLIDVARD ARWGRVEETF GEDPYLVANM AVSYVKGLQG
DDIKKGIVAT GKHFVGYAMS EGGMNWAPVH IPERELREVY LYPFEVAVKV AGLKSIMPAY
HEIDGIPCHA NRKLLTDIAR NEWGFDGIYV SDYSGVRNLL DYHKSVKTYE EAAALSLWAG
LDIELPKIEC FTEEFIKALK EGKFDMTLVD AAVKRVLEMK FRLGLFDNPY IKTDGIVELF
DNKEQRQLSR RVAQESMVLL KNDNFLPLSK DSKKIAVIGP NANSVRNLLG DYSYPAHIAT
LEMFFIKEDK GVGNEEEFVR NVINMKSIFE AIKDKVSSNT EVVYAKGCDV NSQDRSGFEE
AKKAAADADA VILVVGDKAG LRLDCTSGES RDRASLRLPG VQEDLVKEIV SVNPNTVVVL
VNGRPVALDW IMENVKAVLE AWFPGEEGAN AVADVLFGDY NPGGKLAISF PRDVGQVPVY
YGHKPSGGKS CWHGDYVEMS TKPLLPFGYG LSYTTFEYKN FAIEKEKIGM DESIKISVEI
ENTGKYEGDE IVQLYTRKEE YLVTRPVKEL KGYKRVHLKP GEKKKVVFEL YPDLFAFYDY
DMNRVVTPGV VEVMIGASSE DIKFTGTFEI VGSKKDAKEL KHYFSKVWCE
//