CAZyme Information: MGYG000000574_04419

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae
• CAZyme ID: MGYG000000574_04419
• CAZy Family: GH27
• CAZyme Description: Alpha-galactosidase A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
375		42374.37	5.1354

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000574	5306470	MAG	Madagascar	Africa

• Gene Location: Start: 397; End: 1524 Strand: +

Full Sequence      

MIQKYPPMGWNSWNTFGSKINEQLIFETADKLVSTGLAAAGYNYLVIDDCWALKERDENG
RLAADPQKFPHGMRYVSDYVHGKGLKFGMYSCAGNLTCAGYPGSFEHEFIDAATFAEWGV
DLLKYDYCYHSDIIHGKYLYRRMGLALENCGRDILFSACTWGVDKTPEWIRETTAGMWRS
AGDIMDSWESIKKLTDAQDDRLGYGGIGCFNDMDMLVVGMYGEGHVGLEGLSDTQYKTHF
SIWSLMGSPLMIGCDVRNMNEAAFGILSNKKVIAINQDPACRQVMKLKTIGDKELRCYAR
MLEGGDIALGFFNFLEEDTYACFNLDQLGLAESTGKTLELHNLWEDEIVMVINGTFQHMV
KKHDTLLYRCRVVNK

Enzyme Prediction     

No EC number prediction in MGYG000000574_04419.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	100	346	2.9e-66	0.9781659388646288

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14792	GH27	1.10e-137	6	278	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.
PLN02229	PLN02229	1.14e-109	6	368	63	415	alpha-galactosidase
PLN02808	PLN02808	3.60e-108	6	368	32	381	alpha-galactosidase
PLN02692	PLN02692	1.44e-96	6	345	56	382	alpha-galactosidase
pfam16499	Melibiase_2	6.14e-96	6	278	2	284	Alpha galactosidase A.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VCV24057.1	1.92e-185	1	374	1	375
QAA34453.1	6.11e-148	1	373	1	373
AEE96273.1	6.55e-148	1	373	1	375
QUL57156.1	8.39e-145	6	373	16	392
APO43919.1	1.00e-144	6	373	11	386

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UAS_A	6.46e-89	2	368	5	357	ChainA, alpha-galactosidase [Oryza sativa]
6F4C_B	4.29e-84	2	368	5	358	Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana]
4NZJ_A	6.54e-78	6	328	100	442	Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343]
3LX9_A	1.56e-76	2	313	5	324	ChainA, Alpha-galactosidase A [Homo sapiens],3LX9_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXA_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXA_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXB_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXB_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXC_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXC_B Chain B, Alpha-galactosidase A [Homo sapiens]
1R46_A	1.86e-76	2	313	5	324	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
P14749	4.85e-92	6	368	56	405	Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1
Q8VXZ7	4.17e-91	2	368	69	425	Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
Q8RX86	1.11e-89	6	368	40	389	Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
Q42656	1.45e-88	6	368	24	373	Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1
Q9FXT4	1.85e-87	2	368	60	412	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 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
1.000047	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000574_04419.