CAZyme Information: MGYG000004498_01020

Basic Information

• Species: CAG-345 sp000433315
• Lineage: Bacteria; Firmicutes; Bacilli; RFN20; CAG-288; CAG-345; CAG-345 sp000433315
• CAZyme ID: MGYG000004498_01020
• CAZy Family: GH31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
846		99538.85	6.0611

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004498	1649118	MAG	Israel	Asia

• Gene Location: Start: 121112; End: 123652 Strand: -

Full Sequence      

MKSLILNENIRIQKLDECILRIEYSKYGEFCDENTFLVAGKSSFTEEYNLNYKEDEYNYL
LDFKDYEIRVDKNLKQLTGIAVYKNNKLVYKYKKIANSGELPSIEKTPLIFPLIDKPQII
VPECGYSYLNKKNNGFKVNKNANDLYLFFVEGGYKLLRKEYVKLTGRPDMVRLKTLGSWN
SKYYPYRQDEAEQVIRDYENHNIPLDNIVIDTDWRKASDRGIGYDIDENLFPDMKGFFNF
AHDNKVEVMLNDHPEPQDGAKNCCSPNEVKFREEKLTGLLEMGLDYWWYDRNWHTKLISL
DGVINPETWGQYLFHDITRHYYEKNKKGKYPLRALAMSNIDNVSNGYYYHITNSASHRYP
FQWTGDITSSSSSLMENIYDICRANLNEIIYANPDCGGHIGNPDKELFLKWMQVGSLLPV
LRPHCSNMVIRYREPWNYDEETEDICRNYFSLRYRLLEKIYKDAHKSYEDGSPLVKSLSW
DYPKDKNCTKYFGEYFFADILVGYLDYASANFCQKSLLSGKDYVGKIKCRYYLGTNLEGE
PILEKEYKKIDFELVNVPPEKEVPTYNFSAIFEGKINLTKKVSLLVENDDGVRVYIDNKL
VFDDWNNHGAIIMPIGEFEKGIHDLKIEYYQAGGEAFLKLFKSTYDYSIQNKMYLPEGEW
LNPFNGKIIQGNKAIHVVAGIDELPMYLKLGTIYSLLKEANHVEDLDFSKMTLDYYPSMT
NFIEDEIYEDDGKTTGYQFGEYRKNRYKTSFDEKEQAFVLDLFKAEGKYQPYSEREYILK
FHFLKRYEVEKIVLDGREITYRNYSKDNKLFVLSYGDKARESKVSSAHFKVDLNADHQVK
IYIKKH

Enzyme Prediction     

No EC number prediction in MGYG000004498_01020.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH31	265	499	5.2e-45	0.5199063231850117

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01055	Glyco_hydro_31	6.02e-58	148	502	1	388	Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
cd06595	GH31_u1	4.74e-47	165	457	1	301	glycosyl hydrolase family 31 (GH31); uncharacterized subgroup. This family represents an uncharacterized GH31 enzyme subgroup found in bacteria and eukaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 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.
COG1501	YicI	5.62e-46	144	782	235	756	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06589	GH31	4.62e-43	166	449	1	264	glycosyl hydrolase family 31 (GH31). GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 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. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases 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.
cd06604	GH31_glucosidase_II_MalA	2.99e-30	166	471	1	339	Alpha-glucosidase II-like. Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIE84875.1	1.95e-107	9	797	19	787
ARN57252.1	5.72e-97	93	808	256	825
AQQ09813.1	1.54e-94	93	808	256	825
AKC95359.1	8.54e-47	2	502	16	536
AMV60363.1	2.92e-44	1	502	1	525

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7WJ9_A	1.68e-43	1	574	25	634	ChainA, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_B Chain B, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_C Chain C, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_D Chain D, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_E Chain E, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_F Chain F, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJA_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJB_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_B Chain B, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_C Chain C, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_D Chain D, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_E Chain E, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_F Chain F, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363]
7WJC_A	1.72e-42	1	574	25	634	ChainA, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJD_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJE_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJF_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363]
6JR8_A	2.13e-20	125	782	206	776	Flavobacteriumjohnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101]
6JR6_A	2.13e-20	125	782	206	776	Flavobacteriumjohnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR7_A Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101]
2F2H_A	2.35e-19	113	499	209	612	Structureof the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_B Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_C Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_D Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_E Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_F Structure of the YicI thiosugar Michaelis complex [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9F234	4.91e-27	140	798	215	770	Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q9P999	7.38e-23	120	502	155	566	Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
Q9FN05	3.21e-20	148	486	336	707	Probable glucan 1,3-alpha-glucosidase OS=Arabidopsis thaliana OX=3702 GN=PSL5 PE=1 SV=1
Q5AW25	5.68e-19	130	502	240	634	Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1
P31434	1.29e-18	113	499	209	612	Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2

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
1.000051	0.000007	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004498_01020.