CAZyme Information: MGYG000001908_01634

Basic Information

• Species: Ruminococcus_D sp900543145
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_D; Ruminococcus_D sp900543145
• CAZyme ID: MGYG000001908_01634
• CAZy Family: GH27
• CAZyme Description: Alpha-galactosidase A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
424	MGYG000001908_5|CGC1	48682.45	6.0265

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001908	2355088	MAG	Denmark	Europe

• Gene Location: Start: 44741; End: 46015 Strand: +

Full Sequence      

MILKNAPMGWNSWDCYGASVTEEIVRKNAEFMAKHLKQYGWEYIVVDIQWYEPRAASHEY
NPFSELCMDEYSRLIPAPNRFPSSEGGKGFAPLAEYIHSLGLKFGIHIMRGIPRQAVHRN
TKIRDTSKTARQIAKTSSICSWNTDMYGVDPEKDGAEEYYRSLFELYSDWGVDLIKCDDI
ARELPQEERELKMLSKCLRSCGREMVLSLSPGPAPLEKAELFKEVSDMWRITDDFWDNWQ
SLYNMFERTEKWCTHCGAGSWPDADMLPIGPIKQDYDRAIRTEFTRNEQLTMLTLWSIFR
SPLMIGGDMTGFDDFTISLVTNKSILKMHRDSRHSHQVWRKKICGNEYILWTSVSCNGGQ
YATVFNVGEKSGEIEIPLTDLEIYTPVNSAELWSGEKSTAEKVLKVSLDCHGAKAFLLKS
SKSI

Enzyme Prediction     

No EC number prediction in MGYG000001908_01634.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	155	397	9.1e-54	0.9344978165938864

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14792	GH27	7.81e-92	7	331	2	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.
PLN02899	PLN02899	2.96e-82	7	337	32	384	alpha-galactosidase
PLN03231	PLN03231	1.10e-79	7	332	2	349	putative alpha-galactosidase; Provisional
PLN02808	PLN02808	3.16e-38	7	418	33	383	alpha-galactosidase
PLN02229	PLN02229	1.78e-34	8	418	65	417	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL17246.1	3.82e-243	1	419	1	419
ADU21581.1	6.69e-230	1	419	1	419
AHF24669.1	1.61e-207	6	416	7	417
QYR23169.1	2.50e-172	2	418	6	425
QNU19121.1	3.19e-172	4	396	8	402

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NX0_A	2.62e-171	4	396	23	417	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	4.28e-170	4	396	23	417	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	1.50e-149	7	393	13	401	ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
1UAS_A	1.48e-32	4	418	7	359	ChainA, alpha-galactosidase [Oryza sativa]
6F4C_B	3.35e-29	4	418	7	360	Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8RX86	4.64e-36	1	423	30	396	Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
P14749	1.61e-35	4	418	54	407	Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1
Q9FT97	2.10e-34	7	419	55	407	Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 SV=1
Q9FXT4	2.01e-31	4	418	62	414	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
Q42656	1.40e-30	7	418	25	375	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
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001908_01634.