CAZyme Information: MGYG000002168_00556

Basic Information

• Species: Prevotella sp900556825
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900556825
• CAZyme ID: MGYG000002168_00556
• CAZy Family: GH27
• CAZyme Description: Alpha-galactosidase A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
405	MGYG000002168_9|CGC4	45543.87	7.6664

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002168	3553249	MAG	Denmark	Europe

• Gene Location: Start: 54625; End: 55842 Strand: -

Full Sequence      

MKRKLILLIIACLAIGMQAQTKHVTDRTKLAQTPPMGWMSWNLFSSDISEDVVKEMADAM
VSGGFRDAGYQYIFIDDCWQGGRDNRNNIIPDPQKFPHGIKALADYVHSKGLKLGIYSDA
APLTCAGYTASYGFEEQDAKTFADWGIDYLKYDYCNAPTDRATAEKRYKAMADALSKSGR
DITFGICEWGGRQPYLWAHQVGGQVWRTTYDIRDMWKDTLHKGGVGILDDINQNADLHSY
AGPGHWNDMDMLVVGLYGNSGPSSELGGVGCNDIEYETQMSMWCMFSSPLAMSNDLRNVN
AATRRILLNKDIIAINQDPLGKVAVPKVRNDNYQVYLRPLSGDRYALAILNIADRPLNIK
VTLSDLGLDKRRYSFYDVWTHQQMKSGNKWSGKVLSHQTKVFILK

Enzyme Prediction     

EC	3.2.1.22

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	129	384	1.7e-78	0.982532751091703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14792	GH27	1.16e-141	34	318	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	6.96e-112	30	404	28	383	alpha-galactosidase
PLN02229	PLN02229	2.62e-111	30	404	59	417	alpha-galactosidase
PLN02692	PLN02692	1.39e-108	30	405	52	409	alpha-galactosidase
pfam16499	Melibiase_2	2.70e-103	33	318	1	284	Alpha galactosidase A.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOZ99698.1	7.85e-188	6	405	8	414
QUB75633.1	1.01e-186	3	404	9	406
QUB40815.1	4.08e-186	26	404	29	406
QUB81382.1	1.56e-183	25	402	28	404
QUB68250.1	4.46e-183	7	402	12	404

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4OGZ_A	4.88e-116	14	405	80	473	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	3.54e-114	14	370	80	441	Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343]
1UAS_A	9.22e-97	30	404	5	359	ChainA, alpha-galactosidase [Oryza sativa]
6F4C_B	4.39e-92	30	404	5	360	Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana]
1R46_A	9.11e-89	30	395	5	383	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	1.36e-106	9	397	11	394	Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1
Q9FT97	3.52e-97	30	405	50	407	Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 SV=1
P14749	7.25e-97	19	404	36	407	Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1
Q8VXZ7	1.79e-95	30	404	69	427	Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
Q9FXT4	2.77e-95	30	404	60	414	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 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
0.000427	0.997536	0.001470	0.000193	0.000180	0.000174

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002168_00556.