CAZyme Information: MGYG000003538_00677

Basic Information

• Species: UBA737 sp900769375
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA737; UBA737 sp900769375
• CAZyme ID: MGYG000003538_00677
• CAZy Family: GH13
• CAZyme Description: Glucan 1,6-alpha-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
436		49834.23	4.9832

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003538	1465303	MAG	Fiji	Oceania

• Gene Location: Start: 3156; End: 4466 Strand: -

Full Sequence      

MQILIDKAHNLGIKVLLDLVVGHTSDQHKWFKKSSEAERNEFWDYYIWSDDVFGACPYQH
ISGNSDRDGNYLINFFCFQPAINFGFSSKKYSWQNLYTDDVCMKMRDIVTDIIKFYLDKG
VDGFRVDLASSIVKGDVNGKYSCEVWRDIFSRVRKEYPEAIFISEWGQPIYAVKNGDFDI
DFFTHGFNDGYNKLFRQEAGANVIKSDGNSFFKKEGKGEAKEFFDYFLFNIKEIEEKGYV
SIVTGNHDLPRVALGRTQEEMKTVFAFILALPNIPLIYYGDEIGMTYEKLKSKDGGYCRT
GSRTPMQWSSELNAGFSKTEGNTYLPINSDFELVNVETEEANPNSLINEVKKLVAIKREN
PDLFGCSNDFELVSDTYPLIFKRKTDKGELLCAINPSEREYKFSSSGEVLASSNAEIKDG
RVAMGPISYAWIAKTF

Enzyme Prediction     

No EC number prediction in MGYG000003538_00677.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	4	290	1.7e-41	0.7591973244147158

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11348	AmyAc_2	1.78e-153	1	356	72	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.
cd11333	AmyAc_SI_OligoGlu_DGase	1.18e-62	1	359	75	428	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.
cd11359	AmyAc_SLC3A1	3.54e-53	1	364	78	452	Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins. SLC3A1, also called Neutral and basic amino acid transport protein rBAT or NBAT, plays a role in amino acid and cystine absorption. Mutations in the gene encoding SLC3A1 causes cystinuria, an autosomal recessive disorder characterized by the failure of proximal tubules to reabsorb filtered cystine and dibasic amino acids. 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.
cd11316	AmyAc_bac2_AmyA	1.86e-49	4	363	75	400	Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Chloroflexi, Dictyoglomi, and Fusobacteria. 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	4.21e-49	4	411	82	498	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ARP50647.1	2.19e-115	6	430	85	508
QKO29708.1	2.19e-115	6	430	85	508
QKN23619.1	2.19e-115	6	430	85	508
QNO18477.1	1.31e-113	6	399	85	474
CBK82683.1	1.55e-110	7	400	86	485

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4AIE_A	3.12e-38	1	409	82	511	Structureof glucan-1,6-alpha-glucosidase from Lactobacillus acidophilus NCFM [Lactobacillus acidophilus NCFM]
2ZE0_A	3.81e-36	4	419	84	529	Alpha-glucosidaseGSJ [Geobacillus sp. HTA-462]
5H2T_A	5.06e-35	4	397	101	511	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]
4WLC_A	9.96e-35	1	400	81	497	Structureof dextran glucosidase with glucose [Streptococcus mutans UA159],4XB3_A Structure of dextran glucosidase [Streptococcus mutans UA159]
2ZIC_A	1.07e-34	1	400	81	497	ChainA, Dextran glucosidase [unidentified]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q54796	4.35e-35	1	409	81	505	Glucan 1,6-alpha-glucosidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=dexB PE=3 SV=2
P29094	3.74e-34	4	399	84	514	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
Q99040	5.45e-34	1	400	81	497	Glucan 1,6-alpha-glucosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=dexB PE=1 SV=2
O34364	2.41e-33	4	403	84	518	Probable oligo-1,6-glucosidase 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=ycdG PE=2 SV=1
O06994	1.14e-32	4	410	83	527	Oligo-1,6-glucosidase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=malL 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
1.000072	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003538_00677.