CAZyme Information: MGYG000000561_01298

Basic Information

• Species: CAG-115 sp003507295
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; CAG-115; CAG-115 sp003507295
• CAZyme ID: MGYG000000561_01298
• CAZy Family: GH27
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
421		47745.1	4.9352

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000561	2687682	MAG	China	Asia

• Gene Location: Start: 15670; End: 16935 Strand: -

Full Sequence      

MNEFVKTPPMGWNSWDCYGAAVNEDTVRANAEFMAKHLRQYGWEYIVVDIQWSNPIAKNH
EYQQFTELCMDEYSRLIPAVERFPSSEGGKGFAPLAEYVHSLGLKFGIHIMRGIPRQAVH
RNTAIKGTSRTAREIAKTASICQWNTDMYGVDPKKEGAREYYDSLFELYREWGVDFIKVD
DICRELPHEESELVMLSESLHSCGRDMVLSLSPGAALPGKAELYKQVSNMWRITDDFWDN
WAQLHDMFSRAETWCIHAGAGHFPDADMLPIGAILQDYGPDGWTKFTHDEQITMMSLWCI
MRSPLMIGGEMTKFDDFTMSLLTNRDIIDCLDNTHSAHPLFRQTIDGNEQIAWFATHEDG
KTFYAALFNCGESECEITAELPVACRLSAKEVWTGAVSEVSGTISAAVKPHGAAMFRLTR
V

Enzyme Prediction     

No EC number prediction in MGYG000000561_01298.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	163	395	2.4e-55	0.9301310043668122

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14792	GH27	4.18e-99	8	328	1	266	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	2.22e-89	7	336	30	379	alpha-galactosidase
PLN03231	PLN03231	8.01e-85	8	336	1	349	putative alpha-galactosidase; Provisional
PLN02808	PLN02808	6.68e-38	7	420	31	385	alpha-galactosidase
PLN02229	PLN02229	2.68e-36	2	419	57	418	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADU21581.1	4.16e-209	5	416	3	416
CBL17246.1	5.03e-203	5	418	3	418
AHF24669.1	1.17e-187	6	417	5	418
QUA54326.1	4.02e-173	5	417	3	414
QTE72472.1	1.52e-172	5	418	3	414

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NX0_A	1.47e-157	3	393	20	414	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	2.40e-156	3	393	20	414	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	2.86e-141	7	374	11	379	ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
1UAS_A	3.96e-34	2	419	3	360	ChainA, alpha-galactosidase [Oryza sativa]
6F4C_B	1.15e-28	2	419	3	361	Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14749	2.80e-34	2	419	50	408	Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1
Q8VXZ7	2.90e-33	2	419	67	428	Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
Q9FXT4	5.61e-33	2	419	58	415	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
Q42656	2.80e-32	2	419	18	376	Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1
Q9FT97	6.56e-32	2	421	48	409	Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 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	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000561_01298.