CAZyme Information: MGYG000002693_00873

Basic Information

• Species: Anaerobutyricum sp002161065
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerobutyricum; Anaerobutyricum sp002161065
• CAZyme ID: MGYG000002693_00873
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
823	MGYG000002693_28|CGC2	92711.91	7.3192

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002693	2842397	MAG	Canada	North America

• Gene Location: Start: 14801; End: 17272 Strand: +

Full Sequence      

MKRTNTSKKKSRKKRVTAAAAAVETAAAATTEEPAAKAAAKAEPKAEAKAAAEPEVKAAA
KAEPKAEVKAAAEPEVKAAAKAEPKAEPKAEVKAAAKAEPKAEPKAAAEPAVKAAAKAEP
AKTEAKPAVKEAAKEVEAKAAAEKSAVKETVKAEEKKPAAKEPAPKKAAKKASKTSAAKK
ATEAVAKTAAAAKKAAAEAAKKAAEAAAKAARTAVDEEFYYRMEKKNDELRWLYMELYGN
DSMYAELCDNLHRFYMERNKDLKAMDIEREKNPEWYKSNDMLGMMLYIDNFAGNIKGVES
KLDYLEKANVNYLHLMPFLDTVPGKSDGGYAVKDFRKVREDLGTMEDLEHLTAACHKKNM
NVCMDFVMNHTSEDHEWARRARAGEGEYMSRYFFFDNPQIPQQFEQTVPQVFPRNAPGNF
TWLPDIGHYVMTTFYPYQWDLNYRNPRVFNEMMYNFLFLANKGIDVIRIDAVPYIWKELG
TPCRNLRRVHTIVRMMRIIGEIVCPSVLLLGEVVMEPEKVVPYFGTVEKPECHMLYNVTT
MATTWHTVATRDVSLLKRQLDIVAGLPKEYVFLNYLRCHDDIGWGLDYDFLKARGQEEVP
HKKFLNDYFQGYTENSTSRGELYEYDPNTQDARFCATTASMCGIEKAGFEQDNVAMEKAI
KLDVMLHAYMFTQSGIPVIYSGDEVAQVNDYTYKNDPNKAHDSRYIHRGAMRWDLAEHVD
DANTVEGKLFQSLSELEKIRKTEKVFMTNADMWTVETYDPSILCIGRYYDGEKMFGLFNF
SEYDKTAWINETDGMYKNMLTGEVRKAAGVDIPGYGFCWLKKL

Enzyme Prediction     

No EC number prediction in MGYG000002693_00873.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	292	689	8.2e-168	0.9975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11324	AmyAc_Amylosucrase	0.0	216	746	2	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.
cd11356	AmyAc_Sucrose_phosphorylase-like_1	5.60e-59	310	763	38	458	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.
cd11334	AmyAc_TreS	2.11e-57	293	582	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.
cd11343	AmyAc_Sucrose_phosphorylase-like	1.88e-55	310	750	36	443	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.
COG0366	AmyA	8.68e-44	293	782	26	485	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWY96820.1	0.0	216	822	7	612
CBL26996.1	0.0	219	821	16	617
QEK18306.1	4.88e-316	216	821	7	611
QDW74185.1	1.03e-304	215	822	3	609
QRT49301.1	4.50e-304	222	822	11	610

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7ESH_A	4.62e-134	217	782	31	600	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]
5N7J_A	4.02e-130	237	795	50	596	Crystalstructure of Neisseria polysaccharea amylosucrase mutant efficient for the synthesis of controlled size maltooligosaccharides [Neisseria polysaccharea]
4FLR_A	7.95e-130	237	795	50	596	Crystalstructure of Amylosucrase double mutant A289P-F290L from Neisseria polysaccharea [Neisseria polysaccharea]
4FLQ_A	7.95e-130	237	795	50	596	Crystalstructure of Amylosucrase double mutant A289P-F290I from Neisseria polysaccharea. [Neisseria polysaccharea]
4FLO_A	1.12e-129	237	795	50	596	Crystalstructure of Amylosucrase double mutant A289P-F290C from Neisseria polysaccharea [Neisseria polysaccharea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZEU2	2.15e-128	237	795	58	604	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
Q84HD6	5.99e-128	237	795	58	604	Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
G0GBS4	6.75e-38	313	785	92	531	Glucosylglycerate phosphorylase OS=Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203) OX=869211 GN=Spith_0877 PE=1 SV=1
P72235	1.03e-37	271	582	11	329	Trehalose synthase OS=Pimelobacter sp. (strain R48) OX=51662 GN=treS PE=3 SV=1
O06458	6.95e-37	272	698	2	386	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
1.000035	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002693_00873.