ID A0A0H3C8F1_CAUVN Unreviewed; 758 AA.
AC A0A0H3C8F1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:ACL94484.1};
DE EC=3.2.1.21 {ECO:0000313|EMBL:ACL94484.1};
GN OrderedLocusNames=CCNA_01019 {ECO:0000313|EMBL:ACL94484.1};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL94484.1, ECO:0000313|Proteomes:UP000001364};
RN [1] {ECO:0000313|EMBL:ACL94484.1, ECO:0000313|Proteomes:UP000001364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX PubMed=20472802; DOI=10.1128/JB.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; CP001340; ACL94484.1; -; Genomic_DNA.
DR RefSeq; WP_010918852.1; NC_011916.1.
DR RefSeq; YP_002516392.1; NC_011916.1.
DR AlphaFoldDB; A0A0H3C8F1; -.
DR SMR; A0A0H3C8F1; -.
DR GeneID; 7329768; -.
DR KEGG; ccs:CCNA_01019; -.
DR PATRIC; fig|565050.3.peg.1002; -.
DR HOGENOM; CLU_004542_4_1_5; -.
DR OrthoDB; 9781691at2; -.
DR PhylomeDB; A0A0H3C8F1; -.
DR Proteomes; UP000001364; 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: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:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ACL94484.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACL94484.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001364};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..758
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002606022"
FT DOMAIN 666..735
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 758 AA; 79652 MW; 6D688DB73EEEEE93 CRC64;
MISTTLRSLS LALLISASAS ALSVVPALAD AAKPAAALAH PWMDKSLDAD KRADLVLKAM
TNDEKFTLIF GYFGADMKPK YTRIPESLPG SAGYIAGVPR LGIPAQFQTD AGVGVATQGS
AKEFRERTAL PSGMATTATW NPELAFQGGA MIGKEARDSG FNVQLAGGVN LVREPRNGRN
FEYGGEDPLL AGVMVAAQIR GIQSNNIIST IKHYALNAQE TGRFVVSSNI DDTAARMSDL
LAFQFAIEQS DPHSVMCAYN RVNSVYACES DWLLNTVLKK DWGYKGYVMS DWGAAHSSAK
AANAGLDQES AGDAFDKQPF FAAPLKADLA SGAVSQARID DMARRVLRAM FASGVVDHPL
TGAPLAMPAE TLAAHAKITQ ADAEEGIVLL KNDGGLLPLA KTAKTIAVIG SYADVGVLSG
GGSSQVYPVG GRAVQGLEPK TWPGPVIYYP SSPLKAIAAR YPGAKVVYDD GTDPARAAKL
AASSDLALVF ADQWTTESVD VTTLNLPKNQ DATIDAVASA NKKTVVVLLT GGPLLMPWLD
KVGAVVEAWF PGTAGGEAIA RVLTGEVDAS GRLPVTFPKS VAELPRPKLD GLGKPDGEMF
DVDYTLEGAA VGYKWYDLKK IEPLFAFGHG LSYTQFAYSN LTASASGDTL TVSFEVKNVG
RRPGKDVPQV YVGPKAGGWE APKRLAGFQK VSLAPGASQR VTVTVDPRLL AVWDSKAHGW
SIAAGQYDIA LGASSRAISS TAQVTLAARS LPVSPAAK
//