CAZyme Information: MGYG000000357_01779

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873
• CAZyme ID: MGYG000000357_01779
• CAZy Family: GH27
• CAZyme Description: Isomalto-dextranase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
485	MGYG000000357_35|CGC1	55059.07	5.0695

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000357	2815297	MAG	Sweden	Europe

• Gene Location: Start: 5872; End: 7329 Strand: +

Full Sequence      

MTKHSITYKLAAAAFSCAIVFSSIACSDNNSDGPGKDPEPPVPTLPELPVPGDIHNYKAP
LYWSIYEYAREMELAGVPYDQMDLSSDEWDAVIDMMATKFKPYGYDMICTDGFLPQKARD
GGIYMSHYGSMPLKELVRRAKAKGLKVGVYDNPLWIKGNLNSKVPGTNYALRSLIRNPQD
KVLYPEVTDRTDFTWLVTDHPGAREYIDEWFKHYHDLGVDFVRMDFMCWYEDGDPGRDYP
VTCGYGRERYERGLAYICESAEKYGIFTSIVMPELYNDAELERKYCNMTRIVQDANIGGW
HHFSSFNRGKIYDRWPYADNQMDGFTHWSHIGGRGKILLDGDFLRLNKCSSDDERRSQVS
LQLIAGGPVAIADTPETIRNYDKFYTNEELLALNADRFVGKPVSDIVDSDGSCIWWGTMS
NGDVVIAMFNREESGKRMSVDLSDLNLSGEFNVRDLWKHADEGTVSGTYEAPVPRHGCKV
VKLTK

Enzyme Prediction     

No EC number prediction in MGYG000000357_01779.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	211	462	2.2e-32	0.9388646288209607

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17801	Melibiase_C	3.28e-19	409	483	1	74	Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
cd14792	GH27	8.09e-14	91	396	22	271	glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 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. GH27 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.
PLN02808	PLN02808	8.55e-14	309	484	207	384	alpha-galactosidase
PLN02229	PLN02229	2.65e-09	311	484	239	418	alpha-galactosidase
cd14791	GH36	1.54e-05	133	361	67	296	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHF13305.1	3.21e-299	48	483	36	471
QNT67171.1	2.34e-173	40	483	29	473
QUT44530.1	3.76e-169	20	485	16	492
QUT79686.1	3.76e-169	20	485	16	492
QRM98947.1	5.33e-169	20	485	16	492

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5AWO_A	3.19e-74	60	484	38	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]
4NX0_A	2.45e-15	66	484	19	441	Crystalstructure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q44052	1.17e-74	60	484	64	492	Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1
Q42656	6.77e-08	354	484	244	376	Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000383	0.094631	0.904760	0.000068	0.000086	0.000067

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000357_01779.