Species | Limosilactobacillus caviae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus caviae | |||||||||||
CAZyme ID | MGYG000004287_01899 | |||||||||||
CAZy Family | GH70 | |||||||||||
CAZyme Description | Glucosyltransferase-SI | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 142; End: 3423 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH70 | 163 | 958 | 0 | 0.9900373599003736 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam02324 | Glyco_hydro_70 | 0.0 | 163 | 969 | 1 | 804 | Glycosyl hydrolase family 70. Members of this family belong to glycosyl hydrolase family 70 Glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) catalyze the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules, EC:2.4.1.5. This family roughly corresponds to the N-terminal catalytic domain of the enzyme. Members of this family also contain the Putative cell wall binding domain pfam01473, which corresponds with the C-terminal glucan-binding domain. |
pfam19127 | Choline_bind_3 | 1.68e-08 | 967 | 1005 | 8 | 47 | Choline-binding repeat. Pair of presumed choline-binding repeats often found adjacent to pfam01473. |
NF033840 | PspC_relate_1 | 1.88e-08 | 967 | 1075 | 516 | 636 | PspC-related protein choline-binding protein 1. Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC. |
cd11318 | AmyAc_bac_fung_AmyA | 4.72e-08 | 723 | 825 | 3 | 100 | Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes bacterial and fungal proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. |
COG5263 | COG5263 | 6.48e-07 | 904 | 1073 | 97 | 277 | Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AYP74780.1 | 0.0 | 1 | 1092 | 680 | 1766 |
QLL76134.1 | 0.0 | 1 | 1092 | 688 | 1774 |
QDK48460.1 | 0.0 | 1 | 1092 | 688 | 1774 |
AMY13042.1 | 0.0 | 1 | 1092 | 683 | 1769 |
AAU08001.1 | 0.0 | 1 | 1092 | 685 | 1771 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3KLL_A | 0.0 | 58 | 1092 | 3 | 1032 | Crystalstructure of Lactobacillus reuteri N-terminally truncated glucansucrase GTF180-maltose complex [Limosilactobacillus reuteri] |
4AMC_A | 0.0 | 58 | 1035 | 3 | 983 | Crystalstructure of Lactobacillus reuteri 121 N-terminally truncated glucansucrase GTFA [Limosilactobacillus reuteri] |
3HZ3_A | 0.0 | 58 | 1092 | 3 | 1032 | Lactobacillusreuteri N-terminally truncated glucansucrase GTF180(D1025N)-sucrose complex [Limosilactobacillus reuteri] |
3KLK_A | 0.0 | 58 | 1092 | 3 | 1032 | Crystalstructure of Lactobacillus reuteri N-terminally truncated glucansucrase GTF180 in triclinic apo- form [Limosilactobacillus reuteri],4AYG_A Lactobacillus reuteri N-terminally truncated glucansucrase GTF180 in orthorhombic apo-form [Limosilactobacillus reuteri],4AYG_B Lactobacillus reuteri N-terminally truncated glucansucrase GTF180 in orthorhombic apo-form [Limosilactobacillus reuteri] |
6SYQ_B | 9.00e-302 | 73 | 1031 | 125 | 1144 | ChainB, Alternansucrase [Leuconostoc mesenteroides] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P49331 | 2.11e-288 | 55 | 977 | 174 | 1134 | Glucosyltransferase-S OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfD PE=3 SV=3 |
P13470 | 2.15e-276 | 112 | 977 | 244 | 1112 | Glucosyltransferase-SI OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfC PE=1 SV=2 |
P08987 | 1.20e-274 | 55 | 977 | 162 | 1083 | Glucosyltransferase-I OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfB PE=3 SV=3 |
P11001 | 4.44e-262 | 55 | 954 | 160 | 1064 | Glucosyltransferase-I OS=Streptococcus downei OX=1317 GN=gtfI PE=3 SV=1 |
P29336 | 1.54e-261 | 25 | 977 | 123 | 1069 | Glucosyltransferase-S OS=Streptococcus downei OX=1317 GN=gtfS PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000056 | 0.000003 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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