CAZyme Information: MGYG000002007_00016

Basic Information

• Species: Alistipes dispar
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes dispar
• CAZyme ID: MGYG000002007_00016
• CAZy Family: GH27
• CAZyme Description: Alpha-galactosidase A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
407	MGYG000002007_1|CGC1	46060.01	5.0621

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002007	2708946	MAG	Spain	Europe

• Gene Location: Start: 14405; End: 15628 Strand: +

Full Sequence      

MKRLLLFCAALCCAATSSAQKWEGLADTPPMGWSTWNKFGCNVDERMVREMADALVESGL
AEAGYVYLNIDDCWHASERDADGFPQCDPERFPGGMKALADYVHSKGLKLGIYSDAGRRT
CAGRFGSFGHEYQDALQYARWGIDYLKYDWCNTENINPVGAYTLMRDALRAAGRPILFSM
CEWGNSKPWTWAREVGHMWRTTGDIGLSFSDPAVFTGDWKPRTVMQNFDDNAGLRRYAGP
GHWNDPDMLEVGNGMSVNQDRAHFTMWCMMAAPLILGNDIRAMSDETAAIVTDRDVIAID
QDPLGVQGLRYATDNGLEIWFKPLAGGEWAFCLFNRTHEARPYTIDWQLFSFTDTEVSQC
STAFDRIVYEGRDLWNGGRSFRTDRKREVVVPAEDVVLYRLRPVVKR

Enzyme Prediction     

No EC number prediction in MGYG000002007_00016.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	126	376	4.6e-84	0.9606986899563319

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14792	GH27	4.75e-148	29	302	1	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.
PLN02808	PLN02808	1.45e-127	24	375	27	357	alpha-galactosidase
PLN02229	PLN02229	2.60e-124	24	375	58	390	alpha-galactosidase
PLN02692	PLN02692	1.49e-122	24	375	51	381	alpha-galactosidase
pfam16499	Melibiase_2	2.99e-101	28	302	1	284	Alpha galactosidase A.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBL06472.1	0.0	1	407	1	407
QUB47766.1	2.27e-190	19	401	21	405
QUB71325.1	1.78e-185	19	401	21	405
VEH15502.1	4.75e-185	4	401	9	405
QUB41946.1	7.08e-183	19	401	23	407

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UAS_A	5.08e-113	23	403	3	361	ChainA, alpha-galactosidase [Oryza sativa]
6F4C_B	1.49e-104	23	403	3	362	Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana]
4OGZ_A	1.26e-96	28	336	99	420	Crystalstructure of a putative alpha-galactosidase/melibiase (BF4189) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343],4OGZ_B Crystal structure of a putative alpha-galactosidase/melibiase (BF4189) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343]
4NZJ_A	2.83e-96	28	373	99	455	Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343]
1R46_A	3.86e-88	23	345	3	336	Structureof human alpha-galactosidase [Homo sapiens],1R46_B Structure of human alpha-galactosidase [Homo sapiens],1R47_A Structure of human alpha-galactosidase [Homo sapiens],1R47_B Structure of human alpha-galactosidase [Homo sapiens],3GXN_A Crystal structure of apo alpha-galactosidase A at pH 4.5 [Homo sapiens],3GXN_B Crystal structure of apo alpha-galactosidase A at pH 4.5 [Homo sapiens],3GXP_A Crystal structure of acid-alpha-galactosidase A complexed with galactose at pH 4.5 [Homo sapiens],3GXP_B Crystal structure of acid-alpha-galactosidase A complexed with galactose at pH 4.5 [Homo sapiens],3GXT_A Crystal structure of alpha-galactosidase A at pH 4.5 complexed with 1-deoxygalactonijirimycin [Homo sapiens],3GXT_B Crystal structure of alpha-galactosidase A at pH 4.5 complexed with 1-deoxygalactonijirimycin [Homo sapiens],3HG2_A Human alpha-galactosidase catalytic mechanism 1. Empty active site [Homo sapiens],3HG2_B Human alpha-galactosidase catalytic mechanism 1. Empty active site [Homo sapiens],3HG4_A Human alpha-galactosidase catalytic mechanism 3. Covalent intermediate [Homo sapiens],3HG4_B Human alpha-galactosidase catalytic mechanism 3. Covalent intermediate [Homo sapiens],3HG5_A Human alpha-galactosidase catalytic mechanism 4. Product bound [Homo sapiens],3HG5_B Human alpha-galactosidase catalytic mechanism 4. Product bound [Homo sapiens],3S5Y_A Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Y_B Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Z_A Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Z_B Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],4NXS_A Crystal structure of human alpha-galactosidase A in complex with 1-deoxygalactonojirimycin-pFPhT [Homo sapiens],4NXS_B Crystal structure of human alpha-galactosidase A in complex with 1-deoxygalactonojirimycin-pFPhT [Homo sapiens],6IBK_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfamidate ME763 [Homo sapiens],6IBK_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfamidate ME763 [Homo sapiens],6IBM_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfate ME776 [Homo sapiens],6IBM_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfate ME776 [Homo sapiens],6IBR_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol epoxide LWA481 [Homo sapiens],6IBR_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol epoxide LWA481 [Homo sapiens],6IBT_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol aziridine ME737 [Homo sapiens],6IBT_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol aziridine ME737 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B3PGJ1	7.81e-165	10	403	14	403	Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1
P14749	2.11e-113	23	375	50	381	Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1
Q9FXT4	1.65e-111	23	403	58	416	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
Q8VXZ7	1.75e-110	23	403	67	429	Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
Q42656	2.55e-106	23	403	18	377	Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000268	0.999054	0.000175	0.000170	0.000155	0.000143

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002007_00016.