CAZyme Information: MGYG000000806_01929

Basic Information

• Species: Blautia_A sp900541345
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A sp900541345
• CAZyme ID: MGYG000000806_01929
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
542	MGYG000000806_67|CGC1	62095.37	5.328

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000806	2686211	MAG	China	Asia

• Gene Location: Start: 8244; End: 9872 Strand: -

Full Sequence      

MASKRLQKKKAVAASRLETKKTDYIKISTQKAEPAKITTENQKEPRLTAAPKEDFIYQQR
FSRYYDELKWLYCELYENSKDALSYLKDLTLQMRRFYDEREQELQNSDIERAENPNWYRT
ESLSGMEIYKDSLPETEAAQNELLNYMEECLVNFLFLKGTGKDCSAFAARSHGRNICICS
DFSFHFPETFVQSSDAFSPAAFNNMIFQLLSLANQGTDMICVNPLPPLHSIGRMMRLVCE
IVCPGVLLLGKTDTEQESSFSWFGSLENPVFHLLFSSENMADIWHTAATRDVSLLRRQID
KCTSLPENCVFQNCLRNHDEIRWNLDYSYLKDCAMEEIPHKKYLNDFFTGKYPGSFARGE
QFKEGVYGTTASLCGIEKADFEGNTPALEKAVRYDITLHSFLLSLPGIPVLLSGDEIGKL
NDYSLPTGDFDKNLAENRKLTHTVQGQIFSSLNQLKSVRSSHKVFNSSVPARTIESWDVS
VLALVRETDEEKFIGIYNFSEYDKTAWINEEDGIYTDLISGREMKAKGVNIPAFGFLWLL
RK

Enzyme Prediction     

No EC number prediction in MGYG000000806_01929.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	198	421	4.4e-52	0.615

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11324	AmyAc_Amylosucrase	2.92e-103	56	465	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	4.61e-09	224	426	211	382	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	1.01e-04	181	476	155	453	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.
pfam16657	Malt_amylase_C	0.002	480	538	12	75	Maltogenic Amylase, C-terminal domain. This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyzes starch material. Maltogenic amylases are central to carbohydrate metabolism.
pfam18612	Bac_A_amyl_C	0.002	481	528	10	57	Bacterial Alpha amylase C-terminal domain. This is a bacterial alpha amaylase C-terminal domain found mostly in bacilli.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL22253.1	3.01e-163	53	541	96	707
QCU02723.1	6.23e-144	54	540	158	691
SNU99921.1	1.32e-131	53	542	33	648
BDA10513.1	3.67e-129	42	541	16	638
QIB60618.1	9.09e-127	42	541	16	638

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7ESH_A	2.39e-32	187	539	261	644	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]
4AYS_A	8.05e-31	57	540	27	645	TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans]
5N7J_A	1.41e-29	198	539	261	625	Crystalstructure of Neisseria polysaccharea amylosucrase mutant efficient for the synthesis of controlled size maltooligosaccharides [Neisseria polysaccharea]
3UCQ_A	2.11e-29	198	501	264	604	Crystalstructure of amylosucrase from Deinococcus geothermalis [Deinococcus geothermalis DSM 11300],3UER_A Crystal structure of amylosucrase from Deinococcus geothermalis in complex with turanose [Deinococcus geothermalis DSM 11300]
4FLO_A	1.48e-28	198	539	261	625	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
Q84HD6	8.35e-28	44	539	26	633	Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
Q9ZEU2	8.35e-28	198	539	269	633	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
D7BAR0	3.30e-06	229	497	251	518	Glucosylglycerate phosphorylase OS=Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) OX=526227 GN=Mesil_0665 PE=1 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
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000806_01929.