CAZyme Information: MGYG000002870_00637

Basic Information

• Species: CAG-605 sp900545005
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; CAG-605; CAG-605 sp900545005
• CAZyme ID: MGYG000002870_00637
• CAZy Family: GH31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
836		97691.16	8.3766

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002870	1225239	MAG	United States	North America

• Gene Location: Start: 72434; End: 74944 Strand: +

Full Sequence      

MSTLGNHFLPNMNNRMTNPKAVFKGKNYRISIISDMILRLEYDETGVFNDYLTENIQNRS
FPLPTLDIQEDHATLIVNTKYYRLQYLKEKPFKGSLFAPDSTLRVNVLNSSAYWYYGSDE
SKNITSPIFNLDLKKEFISASESLENNNSKDDKKKKEATDTYKKARNSIFERQKSLYSLD
GFSTLDDSDSMIIDDKGYMVPRTHKSIDIYVFVYNKDFRMFLGEYASLAGRCPLIPRYSL
GVWWYKDDVYTFDNIRKLVYDFNSHHIPLNVLVLGSNWHIKDPNDLKKFKSGFTFNRDKL
GTLSNFTTFLHERGIRLGLSLDPTEGIHPHEFKYRDYASELGINDSQDLPFNVLDTNVVA
AYLDKLINPLYNENVDFFFLDVRTKDKRVMNALNYYHYNDYKKFTNIRGMVLARPASLGA
LRYPILYSGETKVSWDTLKKLPEYISSAYNMGITWWSHDIGGFKGGIEDSELYLRYVEFG
TFSPIFRFASSYGHYYKREPWRWNSQVLRVVQDYLLLRLKLSSYLYAEGYKYYKLGIPIF
MPLYHAVPGMIDELDYKNEYFLGSELLVSPITTKKDALMQRSVEKIYLPNGTWYDFKTGK
RFNGNTRYVMFFNDDDYPVFAKKGSIIPLYIPDKNINNIGVAKSLEIHIFPGNSNIYNLY
EDDGISSLYEQGYYIVTRIDYNYLQNNYTLIIRPYEGKSGIIPDTRNYKIRFRNTRTATD
VRVLQEADKKEFTAYSEDNDFVIEVNEVSTVKQLTIICRGKDIEIDATRILNEDIDSIIS
DIPVETNVKDEIAKIMFSDKDYSDKRILVKKLKSKGLSDLYIRMLLRLLEYTSNKK

Enzyme Prediction     

No EC number prediction in MGYG000002870_00637.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH31	210	627	3.5e-80	0.9976580796252927

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06595	GH31_u1	9.66e-142	229	525	1	304	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	3.54e-71	207	679	234	722	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
pfam01055	Glyco_hydro_31	3.58e-70	220	627	2	442	Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
cd06589	GH31	2.86e-36	230	515	1	265	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.
cd06603	GH31_GANC_GANAB_alpha	2.59e-29	406	629	211	428	neutral alpha-glucosidase C, neutral alpha-glucosidase AB. This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AMC08870.1	4.71e-148	16	763	16	734
QJS18698.1	3.25e-141	16	732	16	700
AEO99951.1	5.14e-133	18	713	10	676
QDI61567.1	1.07e-132	18	713	22	688
AWP36067.1	1.07e-132	18	713	22	688

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7WJ9_A	6.60e-100	5	663	18	645	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	1.79e-99	5	663	18	645	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]
6JR6_A	5.20e-36	209	721	237	784	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]
6JR8_A	3.75e-35	209	721	237	784	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]
5X7O_A	1.78e-29	203	711	224	763	Crystalstructure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase [Paenibacillus sp. 598K],5X7O_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase [Paenibacillus sp. 598K],5X7P_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with acarbose [Paenibacillus sp. 598K],5X7P_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with acarbose [Paenibacillus sp. 598K],5X7Q_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with maltohexaose [Paenibacillus sp. 598K],5X7Q_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with maltohexaose [Paenibacillus sp. 598K],5X7R_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with isomaltohexaose [Paenibacillus sp. 598K],5X7R_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with isomaltohexaose [Paenibacillus sp. 598K],5X7S_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase, terbium derivative [Paenibacillus sp. 598K],5X7S_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase, terbium derivative [Paenibacillus sp. 598K]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9P999	8.10e-49	205	676	188	671	Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
Q9F234	3.34e-37	206	693	229	740	Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q8TET4	9.29e-29	224	669	347	823	Neutral alpha-glucosidase C OS=Homo sapiens OX=9606 GN=GANC PE=2 SV=3
Q9BE70	2.79e-28	224	669	202	678	Neutral alpha-glucosidase C (Fragment) OS=Macaca fascicularis OX=9541 GN=GANC PE=2 SV=2
Q8BVW0	1.93e-27	224	669	331	807	Neutral alpha-glucosidase C OS=Mus musculus OX=10090 GN=Ganc 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
1.000065	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002870_00637.