CAZyme Information: MGYG000001085_01159

Basic Information

• Species: RC9 sp000434935
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp000434935
• CAZyme ID: MGYG000001085_01159
• CAZy Family: GH97
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1466	MGYG000001085_29|CGC2	166599.94	5.2776

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001085	2352626	MAG	Sweden	Europe

• Gene Location: Start: 99582; End: 103982 Strand: +

Full Sequence      

MKNLLTFLLAAFMTLSLVAAPKQYNLTSPDGRLEMKIHVGEGLSYDVLHDGVLLLENSRM
SMTLQDGTVYGAPGQTLKRARTRSVDRTVKSPVYKKSEVEEKFNELTLEFKGFKAVFRAY
DEGCAYRFISGSEKPFIVSDEQADFRFPEDRTAYIPYVNKKWKGSLQDILINDFQCPYTC
SKLSEWIDRWSIAPILVQCSEGKSVVITEADLMDYPGMFLYNYKKGTGETLSGYFARVPD
DVEIGGHNMVQEMVNSRKDYIAECEPGAEFPWRVIAVASSDKELTDSDIVWKLATPADAD
EDWSWVRPGKVAWEWWNAWNIKGVDFEAGVNNDTYKYYIDFAAENRIEYVILDEGWAVKY
ANDLTQVVPEIDLKELVEYGRKRGVGIILWAGWYPFTKDMENVCRRFSEMGVKGFKVDFM
NRDDQKMVEWYRDAAAMCAKYHMLMNFHGAYKPTGLQRTYPNVVNFEGVFGLEQMKWSAT
DVDHVTYDVTIPFIRMVAGPMDYTQGAMRNAVKKNYRPIRTEPMSQGTRCHQLAEYVIFE
SPLNMMCDSPNNYRAEQECTDFISAIPTVWDETVALDGKVAEYVAMARRKGDRWYVGAMT
NWDSRALELDLSFLPAGDYTMTIYQDGVNAHRIATDYKKVTCSVPASRKVEVKMAPGGGW
AAELKPVKPVSREFVLQAHRGIAARYPENTSLSFSKAAEIPVYGGMETDVQMTKDGIIVC
MHDKKLDRTTDGTGMVSQYTFNELQKFWIDGGYGWDEKYAKTLKIPTFATYLEACREGGL
TPYVELKRVNEEGIRKTIEMLHDFGFDGKYVLTSFNWNSILTASKLTDAPLQFMKAGGRY
TKEDVDTCSLRVKNLVIRPKSTDLTKEFVDYCHAKGLTVECYGIPVGDEKLVEQLIGWGV
KGGTCNDWKGLGLDDCPDKVQTYPKWLDNAAIYHIYPSSFKDSDGDGYGDLEGIRSKLDY
VKTLGFNTIWISPVFCSMFEDGGYDITDYYKVDPRFGTNTDLENLVKDAHAKGLRICLDL
VAGHTSDKHPWFVESANGDRNGHYSDYYIWMDSKDGKPRDSEKKKWVDCNYPRGVRYMKN
YYDVQPALNYGYLSPDPSRPWEQSYDAPGPKAVRQELKNIIAFWFDKGVDGFRCDLAWSL
VKGDDEEFHGVRKLWDEIFAWTSANYPDRIFLSEWSSPVESISCGFDIDIIRHNGCGKTM
YRDLVYNTRRNADPSTGIYPPCDCWFDKAGKGKISSFVIPFTEMYRKTHGQGFPCMPTSS
HDTWRMNRNQRSDPEELKTMMTFFLTMPWVPIVYYGEEIGMRSMDGVPAVEGSRDRSAER
TPMQWGDGPTAGFSTCAPEKLYLPIDPSPTRPTVDNEINDASSMYSWTKGLLALRASIPA
LGNTGDWKYASNPNQPYPAVYERSANGEKYLVVINPRAEKAKCTITGYDGMESVVWGDPE
NISMKSSGQELVITIKGISSVICKMK

Enzyme Prediction     

EC	3.2.1.22

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH97	13	664	1.6e-203	0.9920760697305864
GH13	949	1302	9.6e-65	0.9904458598726115

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11348	AmyAc_2	0.0	932	1374	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	3.22e-130	302	567	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	1.31e-98	929	1375	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	2.15e-87	926	1375	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	1.18e-81	924	1381	2	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	9.40e-309	923	1465	23	564
AHZ59910.1	1.14e-274	24	664	10	647
ARK08559.1	2.95e-267	22	664	28	667
QIK58765.1	3.82e-263	4	664	9	666
QIK53348.1	6.01e-262	4	664	9	666

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3A24_A	5.17e-232	28	665	6	641	Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron]
5E1Q_A	9.28e-231	28	665	20	655	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]
4M8U_A	9.54e-62	925	1459	3	559	TheStructure of MalL mutant enzyme V200A from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]
4M56_A	1.32e-61	925	1421	3	518	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]
7LV6_B	2.24e-61	925	1421	28	543	ChainB, Oligo-1,6-glucosidase 1 [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8A6L0	3.63e-236	1	665	1	662	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
Q45101	1.89e-61	925	1415	3	512	Oligo-1,6-glucosidase OS=Weizmannia coagulans OX=1398 GN=malL PE=3 SV=1
O06994	7.21e-61	925	1421	3	518	Oligo-1,6-glucosidase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=malL PE=1 SV=1
P29094	3.33e-60	926	1415	5	510	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
P07191	1.86e-58	926	1415	27	514	Maltase A2 OS=Drosophila melanogaster OX=7227 GN=Mal-A2 PE=2 SV=2

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
0.000329	0.998895	0.000274	0.000167	0.000171	0.000161

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001085_01159.