CAZyme Information: MGYG000003520_00482

Basic Information

• Species: RC9 sp900769145
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp900769145
• CAZyme ID: MGYG000003520_00482
• CAZy Family: GH97
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1212	MGYG000003520_54|CGC1	136490.07	5.1055

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003520	2768956	MAG	Fiji	Oceania

• Gene Location: Start: 12987; End: 16625 Strand: +

Full Sequence      

MKTLLSCLLAVALTCFTAGASGTYSLKSPGGRILVNVNAGEHLSWSLACAGETLVEDSPI
SLTLGDGTVLGTGLKSARVIRRSVDLNVPATVYKKSTIRDNFNEMTLDFRTFRVVFRAYD
TGAAYRFVVKSGKPFKVLGEQAEFAFPEDWKVLASYSNTKGDVTAQLINNFESEYEEMSV
SQVDTGRIAFLPVLVTSPSGRRVCIAESGLMDYPGMFLRAGGDGRSLSGYFAGYPKNLAV
GGKRGHHEIVTERYPHIAEYSAGEIALPWRTAVVSENDKELLDNDLVWLLGDAPSVDIDF
SWVRPGKVAWEWWNAWNIKGVDFESGVNDATYKYYIDFAASKGIEYVILDEGWSVPGVRD
LMQIVPSIHLEELVRYAGERNVGIILWAGYTSFSRDVEAVCRHYSKMGVKGFKVDFMERD
DQKMVAFQARAAEIAAKYHLMLDFHGTFKPAGIQRTWPNVVNFEAVFGLEQMKWKEGADM
VKYDVTIPFVRQLAGPMDYTQGAMRNATAKNWKPIYSEPMSQGTRCRQLAEYVIFESPLN
MLCDSPSAYLSEPECTDFIAAVPTVWDETLALDGKVGEYVVMARRKGDDWYVGAITDWTP
REMRLELPFAGGDGWKIEFFRDGANAAKIASDYRREILPFTGSIDVKMAPGGGFAARIYR
DDDQMLAAQTYPAWLDSAAIYHIYPSSFQDSNGDGYGDLEGIRSRLGYVRQTGFNTIWLS
PVFCSEFEDGGYDITDFYRIDPRFGTNADLVRLVEEAHDMGIKVCLDLVAGHTSDKHPWF
VESAGGDRNGHYSDYYIWTDGKEITPPQPDRGGWVDKDYPRGGYYLMNYYDIQPALNYGY
LSPDPTHSWEQAYDDPGPTAVRQELKNIIAFWFDKGVDGFRCDMAWSLVKGDDEEFHGVR
KLWNEIFTWQSERYPDRIFLSEWSSPIESISCGFDIDIIRHNGCGKTMYRDLVHNTYRNQ
ETDGTYKPKNCWMDKAGKGRFDTFAIPFTKMYNATRGHGFPCMPTSSHDTWRLNRNQRST
PEELRTAMTFFLTMPWVPIVYYGEEIGMRSMDGAPYIEGSRDRSAQRTPMQWDSSVNAGF
STCSTDKLYLPIDPSPERPTVEEEVGDAASLYNWTRGLLALRASVPALGNRGEWRMLTNP
KKPYPVVYERFAAGERYIVVLNPSGNEVAADIDMNGKSEVIFGDRESVRFSRIAGGLRVR
IKGTSSVVCRIF

Enzyme Prediction     

EC	3.2.1.22

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH97	15	658	3.2e-188	0.9873217115689382
GH13	697	1049	9.4e-60	0.9904458598726115

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11348	AmyAc_2	0.0	680	1121	2	429	Alpha amylase catalytic domain found in an uncharacterized protein family. 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 catalytic triad (DED) is not present here. 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.
pfam10566	Glyco_hydro_97	2.51e-126	299	563	1	278	Glycoside hydrolase 97. This domain is the catalytic region of the bacterial glycosyl-hydrolase family 97. This central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, form two additional non-catalytic domains. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands.
cd11333	AmyAc_SI_OligoGlu_DGase	3.24e-97	677	1122	2	426	Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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.
cd11334	AmyAc_TreS	1.35e-90	674	1122	1	447	Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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.
cd11328	AmyAc_maltase	1.83e-89	674	1128	4	465	Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related proteins. Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. In most cases, maltase is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and the term "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT74738.1	1.05e-313	664	1211	16	564
BBK99907.1	5.61e-249	20	659	20	663
BBL10724.1	5.61e-249	20	659	20	663
BBL07933.1	5.61e-249	20	659	20	663
QIK58765.1	2.79e-247	8	660	11	668

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3A24_A	1.99e-234	28	658	6	640	Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron]
5E1Q_A	1.82e-233	22	658	14	654	Mutant(D415G) GH97 alpha-galactosidase in complex with Gal-Lac [Bacteroides thetaiotaomicron VPI-5482],5E1Q_B Mutant (D415G) GH97 alpha-galactosidase in complex with Gal-Lac [Bacteroides thetaiotaomicron VPI-5482]
5H2T_A	2.75e-61	672	1174	20	521	Structureof trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_B Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_C Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_D Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_E Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_F Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_G Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_H Structure of trehalose synthase [Thermomonospora curvata DSM 43183]
6K5P_A	1.37e-60	674	1172	31	512	Structureof mosquito-larvicidal Binary toxin receptor, Cqm1 [Culex quinquefasciatus],6K5P_B Structure of mosquito-larvicidal Binary toxin receptor, Cqm1 [Culex quinquefasciatus],6K5P_C Structure of mosquito-larvicidal Binary toxin receptor, Cqm1 [Culex quinquefasciatus],6K5P_D Structure of mosquito-larvicidal Binary toxin receptor, Cqm1 [Culex quinquefasciatus]
4M56_A	7.02e-59	674	1164	4	514	TheStructure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],4M56_B The Structure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8A6L0	2.56e-235	1	658	1	661	Retaining alpha-galactosidase OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=BT_1871 PE=1 SV=1
P29094	4.34e-62	674	1162	5	510	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
P07191	2.52e-60	674	1124	27	475	Maltase A2 OS=Drosophila melanogaster OX=7227 GN=Mal-A2 PE=2 SV=2
Q95WY5	4.47e-60	674	1172	30	511	Alpha-glucosidase OS=Culex pipiens OX=7175 GN=CPM1 PE=1 SV=1
Q45101	4.07e-59	674	1171	4	521	Oligo-1,6-glucosidase OS=Weizmannia coagulans OX=1398 GN=malL PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000407	0.998865	0.000189	0.000191	0.000163	0.000152

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003520_00482.