CAZyme Information: MGYG000003508_00291

Basic Information

• Species: UBA7597 sp003448195
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; UBA7597; UBA7597 sp003448195
• CAZyme ID: MGYG000003508_00291
• CAZy Family: GH13
• CAZyme Description: Oligo-1,6-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
558		64695.48	5.8677

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003508	1808290	MAG	Fiji	Oceania

• Gene Location: Start: 22088; End: 23764 Strand: +

Full Sequence      

MYAARWETAAKTIIQGEKMKEAKNDYLDWAVYQIYPRSFYDSNGDGIGDLNGIREKIPYL
KELGINAVWICPCYKSPNYDNGYDIADYRDIMDEFGTLDDWKKLAEELHKNGIKIIMDLV
VNHTSSEHYWFKQARSSKNNPYHDYYIWADKPLTAWTACFGGSAWEYNAATNEYYLHSFA
VQQPDLNWENPKVRQECCDIVDFWANLGVDGFRCDVLDFISKDFSANKMLNGPHLHEYIR
QLFGRDEVKHLFTVGECQSDVKSICDICGKNRNELKSVFQFEHIGLGRSDKYTPAPYSGD
DIKNVLVKWQNFTEKHDLAYILFTDNHDQPFFISRLGNDKELRYECATAYAGMFYLLKGI
PFIYQGQEFGSANSHYNDISCFNDVETVNYYRENEHKKTHAQLIAEINYGSRDNTRRPVA
WTNETKTHGFTSGTPWLKMPSRADEINLEKDRSSEKSVFAFYKKVLSLRHSGDTIKYGSF
KDLTKNGGCFVYERALEKNKIVVAVNFDKPNNVILPDLSSFRADMILSNYADAEPFSESF
RPFEIRVYSYTEDTIARS

Enzyme Prediction     

No EC number prediction in MGYG000003508_00291.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	48	373	3.4e-120	0.994269340974212

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11333	AmyAc_SI_OligoGlu_DGase	0.0	31	471	5	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.
TIGR02403	trehalose_treC	7.39e-169	31	550	7	543	alpha,alpha-phosphotrehalase. Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.
PRK10933	PRK10933	1.82e-147	31	544	13	544	trehalose-6-phosphate hydrolase; Provisional
COG0366	AmyA	2.20e-118	31	523	3	499	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	4.43e-116	48	376	1	333	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASS91133.1	8.10e-161	31	548	11	557
QNU38283.1	1.85e-159	31	548	11	557
QXJ37939.1	5.23e-159	31	548	11	557
ALC91440.1	1.44e-158	23	548	3	557
QSB48736.1	5.95e-158	31	548	11	557

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UOK_A	2.44e-146	23	548	3	555	CrystalStructure Of B. Cereus Oligo-1,6-Glucosidase [Bacillus cereus]
5ZCB_A	3.21e-143	23	548	3	552	Crystalstructure of Alpha-glucosidase [Bacillus sp. (in: Bacteria)]
5ZCC_A	9.08e-143	23	548	3	552	Crystalstructure of Alpha-glucosidase in complex with maltose [Bacillus sp. (in: Bacteria)],5ZCD_A Crystal structure of Alpha-glucosidase in complex with maltotriose [Bacillus sp. (in: Bacteria)],5ZCE_A Crystal structure of Alpha-glucosidase in complex with maltotetraose [Bacillus sp. (in: Bacteria)]
5DO8_A	4.62e-140	28	548	5	550	1.8Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e],5DO8_B 1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e],5DO8_C 1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e]
2ZE0_A	9.23e-140	23	552	3	555	Alpha-glucosidaseGSJ [Geobacillus sp. HTA-462]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29094	3.49e-155	31	548	11	557	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
Q9K8U9	9.20e-147	31	548	11	556	Oligo-1,6-glucosidase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=malL PE=3 SV=1
P21332	1.34e-145	23	548	3	555	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1
Q45101	4.48e-140	31	548	10	551	Oligo-1,6-glucosidase OS=Weizmannia coagulans OX=1398 GN=malL PE=3 SV=1
O06994	3.48e-135	31	544	10	554	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
0.999124	0.000829	0.000051	0.000005	0.000002	0.000028

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003508_00291.