CAZyme Information: MGYG000002840_00147

Basic Information

• Species: UMGS1872 sp900549475
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UMGS1872; UMGS1872 sp900549475
• CAZyme ID: MGYG000002840_00147
• CAZy Family: GH13
• CAZyme Description: Amylosucrase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
610	MGYG000002840_1|CGC3	70355.96	5.4181

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002840	2700049	MAG	Germany	Europe

• Gene Location: Start: 161193; End: 163025 Strand: -

Full Sequence      

MTSAFARRLQDRRDELEWLYMELYDRRDKLDELLERMEDAYRQRSQNLRRLDTKREKDPA
WFRSGKMLGMTMYTDLFSGDLTGLEKRLDYLTEQGITYLHLMPLLKMPHPDNDGGYAVED
FNQVDPTLGTNEDLSRLTAAMRRRGMSLCLDFVINHTADTHPWAMRAKAGEQEYIDRYIC
FDTPDIPREMEKTIPDVFPETAPGSFIYQEDMKKYVCSSFHPYQWDLNYRNPAVFNDMVC
SMLHLANLGVEILRIDAVPYLWKEMGTTCRNLPKVHTIMRMIRLITEAVCPAVILKGEVV
MAPKELAPYFGTAEKPECHLLYNASTMATQWSALASADVRQLKRQLDDLHSLPSHCWFVN
YLRCHDDIGWGLNEEYGKTIGIDPVAHKKYLYEFFEGSFPGSFARGERYNYNPATLDART
CGTTASLCGIEKGLYEGDEGQVAMGIQRDLMMHAAMMCMAGFPMLSSGDEIGQLNGYDYH
NDPDRREDSRNLHRTRFNWENAAARTQPGTVQQRIWDGLRQLEDLRCQEPCFGPDAWVTT
WDTANRHVLALVRRTAGETLVCLFNFSGEDQTVYMDAVEGEFTDLITGEKGPCSCRQLRP
YQYCLCRHKA

Enzyme Prediction     

No EC number prediction in MGYG000002840_00147.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	79	475	2.4e-173	0.995

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11324	AmyAc_Amylosucrase	0.0	4	532	4	536	Alpha amylase catalytic domain found in Amylosucrase. Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. 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.
cd11334	AmyAc_TreS	2.26e-59	79	368	24	306	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.
cd11356	AmyAc_Sucrose_phosphorylase-like_1	2.57e-46	96	369	38	296	Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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.
COG0366	AmyA	1.71e-43	79	573	26	490	Glycosidase [Carbohydrate transport and metabolism].
cd11343	AmyAc_Sucrose_phosphorylase-like	4.14e-42	96	369	36	294	Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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
CBL25412.1	5.28e-281	8	609	5	606
ATL90312.1	3.70e-277	3	609	5	609
ATP00062.1	2.46e-275	3	609	5	609
QIA44210.1	2.46e-275	3	609	5	609
CBK98444.1	4.60e-275	1	609	1	607

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7ESH_A	3.98e-147	40	571	69	603	ChainA, amylosucrase [Calidithermus timidus DSM 17022],7ESH_B Chain B, amylosucrase [Calidithermus timidus DSM 17022],7ESH_C Chain C, amylosucrase [Calidithermus timidus DSM 17022],7ESH_D Chain D, amylosucrase [Calidithermus timidus DSM 17022]
4FLR_A	5.25e-137	40	602	71	621	Crystalstructure of Amylosucrase double mutant A289P-F290L from Neisseria polysaccharea [Neisseria polysaccharea]
4FLQ_A	5.25e-137	40	602	71	621	Crystalstructure of Amylosucrase double mutant A289P-F290I from Neisseria polysaccharea. [Neisseria polysaccharea]
4FLO_A	7.41e-137	40	602	71	621	Crystalstructure of Amylosucrase double mutant A289P-F290C from Neisseria polysaccharea [Neisseria polysaccharea]
1G5A_A	2.08e-136	40	602	71	621	AmylosucraseFrom Neisseria Polysaccharea [Neisseria polysaccharea],1JG9_A Crystal Structure of Amylosucrase from Neisseria polysaccharea in Complex with D-glucose [Neisseria polysaccharea],1MW1_A Amylosucrase soaked with 14mM sucrose. [Neisseria polysaccharea],1MW2_A Amylosucrase soaked with 100mM sucrose [Neisseria polysaccharea],1MW3_A Amylosucrase soaked with 1M sucrose [Neisseria polysaccharea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZEU2	1.30e-136	40	602	79	629	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
Q84HD6	8.11e-135	40	602	79	629	Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
P9WQ18	1.36e-41	58	576	40	544	Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treS PE=3 SV=1
P9WQ19	1.36e-41	58	576	40	544	Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treS PE=1 SV=1
O06458	2.32e-41	58	472	2	375	Trehalose synthase OS=Thermus thermophilus OX=274 GN=treS PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000065	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002840_00147.