Species | Anaerococcus hydrogenalis | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus; Anaerococcus hydrogenalis | |||||||||||
CAZyme ID | MGYG000001355_00960 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | 1,4-alpha-glucan branching enzyme GlgB | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 13642; End: 14853 Strand: - |
MDTFIQYLKN NNFTHLNFMP IFSNRIEGSL GFSPSSFYAL NENFTSIDNF KSFIDLCHKN | 60 |
NIGIILDFDI GEFDPFNKGL IKFDGSNMYN YDYDDILYNY QGSVNMDPKK DIVKSFIFSL | 120 |
ISYWIDEYNI DGIKFANLEN MVFWQGDKSR GNNEYWLALL KEINFYIKSL GKISIGSFYY | 180 |
IWKNEFDEDL GFSYIYDRTF SSLIKIMQKY PYQRDNYSNI VENIIRGKYD EYILGFDFSD | 240 |
SLSEGASLCM KMYSDNKKYQ QLKTLFLLLY SLSSQKMIFM EDEIGSLKSF DINRKVDFNK | 300 |
INKEEKDFNE FYKGLSKFYQ DHKNLYKKDT QTKILEIEGY SLYAFIREYK KEKYLVLINL | 360 |
TDLDYKIDLD FKFEKILTSF EGKYKEDDKI KIPAFGSGIF RIK | 403 |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH13 | 7 | 285 | 4.7e-42 | 0.9900332225913622 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd11322 | AmyAc_Glg_BE | 6.40e-100 | 1 | 321 | 61 | 402 | Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1,4-alpha-glucan branching enzyme). The glycogen branching enzyme catalyzes the third step of glycogen biosynthesis by the cleavage of an alpha-(1,4)-glucosidic linkage and the formation a new alpha-(1,6)-branch by subsequent transfer of cleaved oligosaccharide. They are part of a group called branching enzymes which catalyze the formation of alpha-1,6 branch points in either glycogen or starch. This group includes proteins from bacteria, eukaryotes, and archaea. 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. |
PRK12313 | PRK12313 | 1.29e-32 | 5 | 403 | 177 | 628 | 1,4-alpha-glucan branching protein GlgB. |
PRK05402 | PRK05402 | 7.95e-22 | 2 | 164 | 269 | 442 | 1,4-alpha-glucan branching protein GlgB. |
PRK12568 | PRK12568 | 2.35e-21 | 2 | 347 | 273 | 644 | glycogen branching enzyme; Provisional |
COG0296 | GlgB | 3.15e-20 | 2 | 156 | 168 | 321 | 1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QQN55949.1 | 3.92e-175 | 1 | 403 | 144 | 546 |
QQB61276.1 | 7.87e-175 | 1 | 403 | 144 | 546 |
ACV28816.1 | 1.30e-107 | 2 | 403 | 144 | 551 |
CBL17307.1 | 4.08e-47 | 5 | 365 | 115 | 490 |
SQH56751.1 | 3.41e-42 | 5 | 379 | 173 | 568 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5GQW_A | 3.45e-28 | 2 | 331 | 319 | 669 | Crystalstructure of branching enzyme W610N mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GQX_A Crystal structure of branching enzyme W610N mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142] |
6KLF_A | 1.09e-27 | 2 | 331 | 295 | 645 | ChainA, 1,4-alpha-glucan branching enzyme GlgB [Crocosphaera subtropica ATCC 51142] |
5GR5_A | 3.71e-27 | 2 | 331 | 319 | 669 | Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142] |
5GR3_A | 5.00e-27 | 2 | 331 | 319 | 669 | Crystalstructure of branching enzyme L541A/W655A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142] |
5GR2_A | 5.00e-27 | 2 | 331 | 319 | 669 | Crystalstructure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GR4_A Crystal structure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8XK15 | 3.38e-35 | 2 | 403 | 207 | 664 | 1,4-alpha-glucan branching enzyme GlgB 2 OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=glgB2 PE=3 SV=1 |
Q8DT52 | 5.09e-35 | 2 | 403 | 169 | 623 | 1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=glgB PE=3 SV=1 |
Q8E5V8 | 3.16e-34 | 2 | 403 | 165 | 617 | 1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus agalactiae serotype III (strain NEM316) OX=211110 GN=glgB PE=3 SV=1 |
Q8E081 | 4.30e-34 | 2 | 403 | 165 | 617 | 1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R) OX=208435 GN=glgB PE=3 SV=1 |
Q3K1K5 | 4.30e-34 | 2 | 403 | 165 | 617 | 1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700) OX=205921 GN=glgB PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000064 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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