CAZyme Information: MGYG000000393_01325

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9
• CAZyme ID: MGYG000000393_01325
• CAZy Family: GH27
• CAZyme Description: Isomalto-dextranase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
476		54162.65	5.5972

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000393	2242585	MAG	Sweden	Europe

• Gene Location: Start: 608; End: 2038 Strand: +

Full Sequence      

MIKKLIISAFVAGCTLLGTCACQKDYSDMRLPNQHEHPHLEDVGNIHTFKAPLYWSIYER
AYELDGDVWETRNIPLSEWEANFEWVAKELKPYGYDMICTDGFLPITCEGNQPYMTRLGQ
VPIKDLIAAAKKRGLRVGIYDSPLEMWCDPKTLIPGTEYTVGSLLYDKAIDKVNHPKAKD
KWHTYIVFSHPGAKEYIDGFFKHYNELGVEMLRMDFLSWFEDGFYRFSDSPVGKGYGRQM
YADALAYICKTAKKYNIFLSLVMPHLYNDAEIESRYGNMVRIVNDTFKGGWNFTSVQDQG
KAATSWPNCLNQFDGFTYWSHIAGRDKVILDGDFTIMHSYKTPAEKQSVVSIQLMAGGPI
AVTDQYCTIGEGDVEYYTNEEMLALNKDRFVGHPMDDALMSPGSNVWYGRMSNGDYVVGL
FNREDEPKDFKVALSDLGINGPMKVRDLWKHADEGTASSIEATIEPHGCKIMRLSK

Enzyme Prediction     

No EC number prediction in MGYG000000393_01325.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	199	454	1.6e-33	0.9388646288209607

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17801	Melibiase_C	6.36e-18	406	474	6	74	Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
PLN02229	PLN02229	2.25e-09	342	471	279	414	alpha-galactosidase
PLN02808	PLN02808	2.56e-08	342	475	249	384	alpha-galactosidase
cd14792	GH27	7.17e-08	86	388	28	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.
PLN02692	PLN02692	7.47e-05	351	471	282	405	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCP71216.1	1.29e-312	1	476	1	475
QCD40129.1	1.29e-312	1	476	1	475
AHF13125.1	1.21e-194	16	476	16	470
QNT67171.1	1.27e-175	1	474	1	473
QUU07210.1	2.53e-172	42	476	49	492

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5AWO_A	3.51e-65	51	475	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]
4NX0_A	9.51e-13	73	475	38	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]
4NXK_A	3.95e-12	73	475	38	441	Crystalstructure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_B Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_C Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_D Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_E Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_F Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_G Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_H Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NZF_A Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_B Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_C Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_D Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_E Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_F Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_G Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_H Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q44052	1.25e-65	51	475	63	492	Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1
Q8VXZ7	2.38e-07	342	475	289	428	Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 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
0.000692	0.419459	0.579194	0.000220	0.000236	0.000193

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000393_01325.