CAZyme Information: MGYG000000348_01619

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485
• CAZyme ID: MGYG000000348_01619
• CAZy Family: GH27
• CAZyme Description: Isomalto-dextranase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
469	MGYG000000348_33|CGC1	53305.22	4.78

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000348	2655711	MAG	Sweden	Europe

• Gene Location: Start: 7468; End: 8877 Strand: -

Full Sequence      

MSLLASTLAAVALSGCVENIEMRRPQKFELPDLPPIEEIHNFKAPLYWSVYEYCHTQSQS
GVKNEDMDITAAQWEQITDWLARDLKPYGYDMVCTDGFISQNCKDGSPYMTHYGSMSIKE
LVEMCKKKGLKVGIYDNPLWVHAPWDTKVPDSEYTVGDLLWDHKSEVLNPGTEDMWGFQW
VVASYPGAKEYIDGFFKHYAELGIDYIRVDFLSWYEDGKDRNMGPIGRGYGRESYVRALS
YIAENAKKYGIFISLVMPHLYYDAEIEKLCGNMVRIVQDTGNGGWWHYSDCERGKSWTTW
PNCMNMFDGFVYWSHISGRGKVLLDGDFIRLNTFNTDAEKESVVSLQLMAGGPVTIADQY
NTIGDNTRFYTNTEMLALNTDGFVGKPLSDELNSKESQIWYGQLSDGNYVIGLFNRDDNA
MSVSVDFKTLGIDGEWKVRDLWKHADEGVAKSLSATLAPHGCKIVKLTK

Enzyme Prediction     

No EC number prediction in MGYG000000348_01619.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	194	447	9.4e-35	0.9388646288209607

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17801	Melibiase_C	6.18e-19	396	467	3	74	Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
PLN02229	PLN02229	1.10e-10	294	468	230	418	alpha-galactosidase
PLN02808	PLN02808	1.31e-10	294	468	200	384	alpha-galactosidase
cd14792	GH27	2.87e-09	68	381	14	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.
cd14791	GH36	1.90e-06	118	239	67	178	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
QNT67171.1	1.15e-227	3	467	6	473
QUU07210.1	2.14e-196	21	469	32	492
QUT44530.1	8.68e-196	21	469	32	492
QUT79686.1	8.68e-196	21	469	32	492
QRM98947.1	8.68e-196	21	469	32	492

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5AWO_A	1.35e-98	44	468	37	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]
1UAS_A	4.38e-15	177	468	97	360	ChainA, alpha-galactosidase [Oryza sativa]
4NX0_A	9.47e-15	79	468	49	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	1.49e-98	44	468	63	492	Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1
Q9FXT4	3.39e-14	177	468	152	415	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 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
0.000001	0.000021	1.000037	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000348_01619.