CAZyme Information: MGYG000000448_00527

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873
• CAZyme ID: MGYG000000448_00527
• CAZy Family: GH27
• CAZyme Description: Isomalto-dextranase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
402	MGYG000000448_21|CGC1	45498.2	5.8227

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000448	2372251	MAG	Sweden	Europe

• Gene Location: Start: 11105; End: 12313 Strand: +

Full Sequence      

MDITPAEWDKIIDWVATDLKPYGYDMVCTDGFIPMLAKDASGYMTHYGSMSLKDLVAKCK
AKGIKVGVYDNPLWIHGPGETKIAGTDYTFSDLYYKHTGDIMNPSAENQWFNWAVAENPG
TREYIDGFFKHYKDLGIEYIRIDFLSWYEDGKDRGMGIVGHGYGRASYARALAYIAESAK
KYGIFTSLVMPHLYNDAEVEAKYGNMVRIVCDTAGGGWWHCSSQEKGKSYTTWPNCMNMF
DGFTYWSHITGRGKVIPDGDFIRLNKFDTDAERETVVSLQLMAGGPVTVSDQYNTIGDNL
KFYTNSEILELNTDRFVGKPLSDKLNDRNNEVWFGQMSNGDYVVGLFNRDDNTRSYSLRL
SDLGIKGEWKQRDLWRHADEGTSAEIKANVAAHGCKIVRLSK

Enzyme Prediction     

No EC number prediction in MGYG000000448_00527.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	127	380	4.2e-33	0.9388646288209607

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17801	Melibiase_C	8.17e-17	331	400	5	74	Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
PLN02229	PLN02229	2.78e-08	232	397	242	414	alpha-galactosidase
PLN02808	PLN02808	5.52e-07	298	401	279	384	alpha-galactosidase
cd14791	GH36	2.03e-05	52	169	67	180	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
cd11320	AmyAc_AmyMalt_CGTase_like	3.86e-04	46	143	99	213	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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
QNT67171.1	2.44e-228	1	400	72	473
QUU07210.1	3.18e-195	1	402	81	492
QUT44530.1	9.08e-195	1	402	81	492
QUT79686.1	9.08e-195	1	402	81	492
QRM98947.1	9.08e-195	1	402	81	492

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5AWO_A	5.78e-92	3	401	54	466	Arthrobacterglobiformis T6 isomalto-dextranse [Arthrobacter globiformis],5AWP_A Arthrobacter globiformis T6 isomalto-dextranase complexed with isomaltose [Arthrobacter globiformis],5AWQ_A Arthrobacter globiformis T6 isomalto-dextranse complexed with panose [Arthrobacter globiformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q44052	6.18e-92	3	401	80	492	Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1
Q9URZ0	2.21e-06	113	402	124	420	Alpha-galactosidase mel1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mel1 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
1.000074	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000448_00527.