CAZyme Information: MGYG000003437_00398

Basic Information

• Species: Eubacterium_R sp900767025
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900767025
• CAZyme ID: MGYG000003437_00398
• CAZy Family: GH27
• CAZyme Description: Alpha-galactosidase A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
433		50160.22	7.6024

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003437	2166830	MAG	Fiji	Oceania

• Gene Location: Start: 36604; End: 37905 Strand: +

Full Sequence      

MHRKLAKTPPLGWNSWDCFGAGVNEKQIKENADYMAKHLKQYGWEYIVCDIQWYEPKAKD
NNYFSFTELNMDEYGRLIPAENRFPSAKNGNGFKDIADYCHALGLKFGIHIMRGIPRQAA
HANTPIKNSKYTARQAAHHFSVCSWNTDMYGMYNCQAAQDYYNSIFELYAQWGVDFIKCD
DICVTEFRQWDNPYSADYEIEMIRKAIDNCGRDMVLSLSPGPAHIENADHLAKNANMWRM
TGDFWDDWGKLHDMFDKCLLWQDRVRPGNYPDCDMLPLGRLSKNGVCHGPRDRMTQFTKP
EQLTMMSLWGIFKSPLMMGGNMPDNDEWTLSLLTNGEYMKMHRECYSAHQHYRNEKNGSG
EIIWIANGKGCKYAALFNTSPKPRIVKLNLSDILMPDKKYSVYNIWKKEDLGTFKNTFKA
NVEPHGAVLIKIL

Enzyme Prediction     

No EC number prediction in MGYG000003437_00398.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	158	412	1.7e-54	0.9432314410480349

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14792	GH27	7.81e-97	9	335	1	262	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.
PLN02899	PLN02899	5.66e-82	2	335	24	369	alpha-galactosidase
PLN03231	PLN03231	6.97e-80	9	335	1	339	putative alpha-galactosidase; Provisional
PLN02808	PLN02808	5.43e-35	5	425	28	376	alpha-galactosidase
PLN02692	PLN02692	4.06e-34	5	425	52	401	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGC68671.1	2.07e-187	4	432	5	429
AGI39682.1	2.07e-187	4	432	5	429
ANW99008.1	5.90e-187	4	432	5	429
ANX01536.1	8.38e-187	4	432	5	429
QYR23169.1	2.27e-175	2	433	3	426

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NX0_A	1.39e-168	2	432	18	440	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	2.26e-167	2	432	18	440	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	4.17e-149	1	432	4	429	ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
1UAS_A	1.54e-30	5	425	5	352	ChainA, alpha-galactosidase [Oryza sativa]
6F4C_B	1.57e-30	5	425	5	353	Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q55B10	4.23e-34	5	432	24	381	Probable alpha-galactosidase OS=Dictyostelium discoideum OX=44689 GN=melA PE=3 SV=1
Q8RX86	4.66e-32	1	425	32	384	Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
Q9FT97	1.42e-30	5	429	50	403	Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 SV=1
Q9FXT4	1.98e-29	5	425	60	407	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
Q42656	2.09e-29	5	425	20	368	Alpha-galactosidase OS=Coffea arabica OX=13443 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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003437_00398.