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BGLB_ACET2
ID   BGLB_ACET2              Reviewed;         755 AA.
AC   P14002; A3DEV9;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Thermostable beta-glucosidase B;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Cellobiase;
DE   AltName: Full=Gentiobiase;
GN   Name=bglB; OrderedLocusNames=Cthe_1256;
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2505054; DOI=10.1007/bf00330944;
RA   Graebnitz F., Ruecknagel K.P., Seiss M., Staudenbauer W.L.;
RT   "Nucleotide sequence of the Clostridium thermocellum bgIB gene encoding
RT   thermostable beta-glucosidase B: homology to fungal beta-glucosidases.";
RL   Mol. Gen. Genet. 217:70-76(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RG   US DOE Joint Genome Institute;
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   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA   Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; X15644; CAA33665.1; -; Genomic_DNA.
DR   EMBL; CP000568; ABN52488.1; -; Genomic_DNA.
DR   PIR; S04381; S04381.
DR   RefSeq; WP_003517480.1; NC_009012.1.
DR   AlphaFoldDB; P14002; -.
DR   SMR; P14002; -.
DR   STRING; 203119.Cthe_1256; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   EnsemblBacteria; ABN52488; ABN52488; Cthe_1256.
DR   KEGG; cth:Cthe_1256; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_4_1_9; -.
DR   OMA; VEPAYEF; -.
DR   OrthoDB; 949956at2; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000002145; 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:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
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   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; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome.
FT   CHAIN           1..755
FT                   /note="Thermostable beta-glucosidase B"
FT                   /id="PRO_0000210778"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000250"
FT   CONFLICT        125
FT                   /note="S -> P (in Ref. 1; CAA33665)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="F -> I (in Ref. 1; CAA33665)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        300..301
FT                   /note="DK -> EQ (in Ref. 1; CAA33665)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        371
FT                   /note="G -> A (in Ref. 1; CAA33665)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        481..493
FT                   /note="ALADVLFGEVNPS -> RWRMCYSVKSIV (in Ref. 1; CAA33665)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   755 AA;  83900 MW;  944A4D782E6AEAB8 CRC64;
     MAVDIKKIIK QMTLEEKAGL CSGLDFWHTK PVERLGIPSI MMTDGPHGLR KQREDAEIAD
     INNSVPATCF PSAAGLACSW DRELVERVGA ALGEECQAEN VSILLGPGAN IKRSPLCGRN
     FEYFSEDPYL SSELAASHIK GVQSQGVGAC LKHFAANNQE HRRMTVDTIV DERTLREIYF
     ASFENAVKKA RPWVVMCAYN KLNGEYCSEN RYLLTEVLKN EWMHDGFVVS DWGAVNDRVS
     GLDAGLDLEM PTSHGITDKK IVEAVKSGKL SENILNRAVE RILKVIFMAL ENKKENAQYD
     KDAHHRLARQ AAAESMVLLK NEDDVLPLKK SGTIALIGAF VKKPRYQGSG SSHITPTRLD
     DIYEEIKKAG GDKVNLVYSE GYRLENDGID EELINEAKKA ASSSDVAVVF AGLPDEYESE
     GFDRTHMSIP ENQNRLIEAV AEVQSNIVVV LLNGSPVEMP WIDKVKSVLE AYLGGQALGG
     ALADVLFGEV NPSGKLAETF PVKLSHNPSY LNFPGEDDRV EYKEGLFVGY RYYDTKGIEP
     LFPFGHGLSY TKFEYSDISV DKKDVSDNSI INVSVKVKNV GKMAGKEIVQ LYVKDVKSSV
     RRPEKELKGF EKVFLNPGEE KTVTFTLDKR AFAYYNTQIK DWHVESGEFL ILIGRSSRDI
     VLKESVRVNS TVKIRKRFTV NSAVEDVMSD SSAAAVLGPV LKEITDALQI DMDNAHDMMA
     ANIKNMPLRS LVGYSQGRLS EEMLEELVDK INNVE
 
 
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