CAZyme Information: MGYG000003156_01639

Basic Information

• Species: Eubacterium_R sp900544515
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900544515
• CAZyme ID: MGYG000003156_01639
• CAZy Family: GH27
• CAZyme Description: Alpha-galactosidase A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
323	MGYG000003156_205|CGC1	37390.64	7.4221

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003156	1833273	MAG	United States	North America

• Gene Location: Start: 57; End: 1028 Strand: +

Full Sequence      

MRGIPRQAVHVDMPIKNSKFTARQVAHHFSVCSWNTDMYGMKNCKGAQDYYNSIIEMYAG
WGVDFIKCDDICVTEFRQWDNPYSADYEIEMIRKAIDNCGREIVLSLSPGPAHIENADHL
AKNANMWRMTGDFWDQWDKLHDMFDRCLLWQDKVKKGNYPDCDMLPLGRLSKNGTCHGPQ
NRMTQFTKPEQLTMMSLWGIFRSPLMMGGNMPENDEWTLSLLTNDEYMKMHRTSYGAHQH
SRNEKNGKGDIIWISNGKGCKYTALFNTRDKEAAIKLDLTEILMPDEKYNVYDIWNKKTY
SDVKNTFKATIAPHGAGLYKITS

Enzyme Prediction     

EC	3.2.1.88

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	54	299	1e-55	0.9388646288209607

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14792	GH27	7.36e-51	46	226	100	264	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.
PLN03231	PLN03231	6.38e-42	1	236	107	351	putative alpha-galactosidase; Provisional
PLN02899	PLN02899	3.66e-38	1	224	134	369	alpha-galactosidase
PLN02808	PLN02808	1.20e-20	58	322	142	384	alpha-galactosidase
PLN02229	PLN02229	9.09e-17	56	322	170	418	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGC68671.1	1.15e-115	1	322	113	430
AGI39682.1	1.15e-115	1	322	113	430
ANW99008.1	1.15e-115	1	322	113	430
ANX01536.1	1.62e-115	1	322	113	430
QYR23169.1	2.22e-111	1	321	113	425

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NX0_A	5.29e-100	1	322	128	441	Crystalstructure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
4NXK_A	8.46e-99	1	322	128	441	Crystalstructure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_B Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_C Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_D Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_E Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_F Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_G Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_H Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NZF_A Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_B Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_C Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_D Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_E Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_F Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_G Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_H Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus]
3CC1_A	5.20e-85	2	322	116	430	ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
6F4C_B	6.24e-15	42	322	103	361	Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana]
1SZN_A	3.26e-07	34	314	124	403	ChainA, alpha-galactosidase [Trichoderma reesei],1T0O_A Chain A, alpha-galactosidase [Trichoderma reesei]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8RX86	3.70e-21	46	322	138	392	Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
Q55B10	3.08e-16	40	322	115	382	Probable alpha-galactosidase OS=Dictyostelium discoideum OX=44689 GN=melA PE=3 SV=1
Q42656	4.51e-15	42	322	118	376	Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1
Q5AX28	1.11e-14	43	321	130	399	Alpha-galactosidase D OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=aglD PE=1 SV=2
A1D9S3	3.56e-14	40	321	119	400	Probable alpha-galactosidase D OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=aglD 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
1.000065	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003156_01639.