CAZyme Information: MGYG000003246_00495

Basic Information

• Species: Borkfalkia sp900761665
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; Borkfalkia; Borkfalkia sp900761665
• CAZyme ID: MGYG000003246_00495
• CAZy Family: GH36
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
685		76695.11	6.3019

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003246	1581010	MAG	United States	North America

• Gene Location: Start: 25819; End: 27876 Strand: +

Full Sequence      

MTCKKYIFGDTAVCYIETPDFGAGLALLPASLPVPDPAQLCCDGMVQAALRGSRTLVDYT
QGVTMRNRESSVLHIAEQRKVKNGVRTLLSDGQGNEYLHLLEHDEATGVLSVCVEYRNNT
GRPQVLESLQSFSVSGIFNPSAGRVCDEGLTLVRMTSAWSRECRLKEEEFCTLGLDASWG
RFGPKCERFGQCGSMPNRGYFPFAALRDRESGFILAAMLEAPYSWQMEVYKEKDTCALSG
GLADYESGHWCKEIEAGGSFRTHKAYLRVRYGSVNDVCNDFVHFQDGRLRVPESEESMPV
LFNEYCTTWGVPSEKNISEILDSIAGIPFGAFVIDAGWYKPDDRGWGNATGDWNESKTLF
PHGIKSVAESIRARGMVPGVWFEFENAGCDSGIFSREEWMLRRDGAVLRCKNRRFFDLRR
EDVRAYLRKKVCAFLRKNGFSYIKIDYNDTFGIGCDGAESCGEGGRQVTEESLAFLNELK
KSVPDIVIENCSSGGSRIEPLRMGMVSMCSFSDAHECAEIPLVAANVSRVVPARQNQIWA
VIRENDTIDRIVWSMTAAMIGRICVSGDVHKIESGQRAKIAEGIGFYNAVKDVVRGGDIA
EISCNIRYYRDPKGCQIYKKISRDKSRLLILAHYFERPHELFEADVSGYKLAASYTTIPF
DVSEGRLRLRPEREYQAGAFLFEKV

Enzyme Prediction     

No EC number prediction in MGYG000003246_00495.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH36	101	631	1.5e-76	0.7441860465116279

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14791	GH36	2.89e-82	298	587	2	297	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.
pfam02065	Melibiase	1.12e-26	259	597	1	347	Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.
COG3345	GalA	2.33e-22	164	520	147	515	Alpha-galactosidase [Carbohydrate transport and metabolism].
cd14792	GH27	1.37e-06	302	494	5	160	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.
cd06589	GH31	0.002	307	381	16	86	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBF42267.1	5.31e-164	2	681	3	697
BBI32765.1	2.89e-161	24	685	39	713
QNU68202.1	2.89e-160	4	679	6	691
AIQ64284.1	4.11e-155	4	683	7	714
QTE69360.1	2.39e-152	1	677	1	679

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2XN0_A	1.43e-19	202	605	234	647	Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN0_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN1_A Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_C Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_D Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM]
2XN2_A	1.43e-19	202	605	234	647	Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM]
4FNQ_A	2.49e-19	105	597	154	635	Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
4FNP_A	2.31e-18	153	597	193	635	Crystalstructure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_B Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_C Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_D Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNS_A Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_B Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_C Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_D Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus]
4FNR_A	2.31e-18	153	597	193	635	Crystalstructure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_B Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_C Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_D Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
G1UB44	7.85e-19	202	605	234	647	Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1
Q9ALJ4	1.26e-17	153	597	193	635	Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1
P43469	8.01e-16	149	534	167	563	Alpha-galactosidase 2 OS=Pediococcus pentosaceus OX=1255 GN=agaS PE=3 SV=1
G4T4R7	2.16e-12	275	499	317	526	Bifunctional alpha-galactosidase/sucrose kinase AgaSK OS=Ruminococcus gnavus OX=33038 GN=agaSK PE=1 SV=1
Q0CEF5	1.70e-11	114	636	159	666	Probable alpha-galactosidase G OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglG PE=3 SV=1

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
1.000060	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003246_00495.