Species | Caulobacter sp903900155 | |||||||||||
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Lineage | Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; Caulobacteraceae; Caulobacter; Caulobacter sp903900155 | |||||||||||
CAZyme ID | MGYG000001261_01386 | |||||||||||
CAZy Family | GH3 | |||||||||||
CAZyme Description | Beta-glucosidase BoGH3B | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1442; End: 3916 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH3 | 135 | 355 | 3.4e-65 | 0.9583333333333334 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1472 | BglX | 7.27e-106 | 66 | 491 | 1 | 396 | Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism]. |
pfam00933 | Glyco_hydro_3 | 9.34e-79 | 67 | 391 | 1 | 316 | Glycosyl hydrolase family 3 N terminal domain. |
PRK15098 | PRK15098 | 5.65e-78 | 37 | 641 | 16 | 648 | beta-glucosidase BglX. |
pfam18559 | Exop_C | 5.03e-48 | 674 | 812 | 1 | 155 | Galactose-binding domain-like. This is the C-terminal domain found in ExoP (exo-1,3/1,4-beta-glucanase) from Pseudoalteromonas. This domain contains a beta-sandwich fold which is common in glycosyl hydrolases (GH7, 11, 12 and 16) and in some 23 carbohydrate-binding modules. It is suggested that the main role of this domain is to provide structural stability necessary for ExoP activity, however no substrate-binding role has been shown. |
pfam01915 | Glyco_hydro_3_C | 2.82e-32 | 428 | 641 | 1 | 216 | Glycosyl hydrolase family 3 C-terminal domain. This domain is involved in catalysis and may be involved in binding beta-glucan. This domain is found associated with pfam00933. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AVQ01631.1 | 0.0 | 10 | 822 | 9 | 822 |
AZS20975.1 | 0.0 | 6 | 822 | 5 | 820 |
ATC25008.1 | 0.0 | 6 | 822 | 5 | 820 |
AZH13162.1 | 0.0 | 6 | 822 | 5 | 820 |
ATC28921.1 | 0.0 | 6 | 822 | 5 | 820 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3USZ_A | 1.06e-232 | 52 | 818 | 19 | 805 | Crystalstructure of truncated exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1 [Pseudoalteromonas sp. BB1],3UT0_A Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1 [Pseudoalteromonas sp. BB1],3UT0_B Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1 [Pseudoalteromonas sp. BB1],3UT0_C Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1 [Pseudoalteromonas sp. BB1],3UT0_D Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1 [Pseudoalteromonas sp. BB1] |
3RRX_A | 8.52e-232 | 52 | 818 | 19 | 805 | CrystalStructure of Q683A mutant of Exo-1,3/1,4-beta-glucanase (ExoP) from Pseudoalteromonas sp. BB1 [Pseudoalteromonas sp. BB1] |
5M6G_A | 4.36e-154 | 59 | 641 | 51 | 614 | Crystalstructure Glucan 1,4-beta-glucosidase from Saccharopolyspora erythraea [Saccharopolyspora erythraea D] |
1LQ2_A | 7.25e-145 | 59 | 640 | 16 | 598 | Crystalstructure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with gluco-phenylimidazole [Hordeum vulgare],1X38_A crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with gluco-phenylimidazole [Hordeum vulgare],1X39_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with gluco-phenylimidazole [Hordeum vulgare] |
1EX1_A | 7.96e-145 | 59 | 640 | 16 | 598 | Beta-d-glucanExohydrolase From Barley [Hordeum vulgare],1IEQ_A Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 [Hordeum vulgare],1IEV_A Crystal Structure Of Barley Beta-d-glucan Glucohydrolase Isoenzyme Exo1 In Complex With Cyclohexitol [Hordeum vulgare],1IEW_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 2-deoxy-2-fluoro-alpha-D-glucoside [Hordeum vulgare],1IEX_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4I,4III,4V-S-trithiocellohexaose [Hordeum vulgare],1J8V_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4'-nitrophenyl 3I-thiolaminaritrioside [Hordeum vulgare],3WLH_A Crystal Structure Analysis of Plant Exohydrolase [Hordeum vulgare subsp. vulgare],3WLJ_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme EXO1 in complex with 3-deoxy-glucose [Hordeum vulgare subsp. vulgare],3WLK_X Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme EXO1 in complex with 4-deoxy-glucose [Hordeum vulgare subsp. vulgare],3WLL_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme EXO1 in complex with PEG400 [Hordeum vulgare subsp. vulgare],3WLM_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with octyl-O-glucoside [Hordeum vulgare subsp. vulgare],3WLN_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme EXO1 in complex with octyl-S-glucoside [Hordeum vulgare subsp. vulgare],3WLP_A Crystal Structure Analysis of Plant Exohydrolase [Hordeum vulgare subsp. vulgare] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q23892 | 3.88e-67 | 56 | 641 | 77 | 699 | Lysosomal beta glucosidase OS=Dictyostelium discoideum OX=44689 GN=gluA PE=1 SV=2 |
A7LXU3 | 2.12e-66 | 45 | 641 | 25 | 659 | Beta-glucosidase BoGH3B OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02659 PE=1 SV=1 |
Q56078 | 3.67e-62 | 50 | 641 | 29 | 648 | Periplasmic beta-glucosidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=bglX PE=3 SV=2 |
P33363 | 9.38e-62 | 50 | 641 | 29 | 648 | Periplasmic beta-glucosidase OS=Escherichia coli (strain K12) OX=83333 GN=bglX PE=3 SV=2 |
T2KMH0 | 9.45e-37 | 136 | 641 | 65 | 604 | Beta-xylosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22130 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000405 | 0.998735 | 0.000288 | 0.000217 | 0.000177 | 0.000151 |
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