CAZyme Information: MGYG000003676_00037

Basic Information

• Species: Fusicatenibacter sp900772675
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Fusicatenibacter; Fusicatenibacter sp900772675
• CAZyme ID: MGYG000003676_00037
• CAZy Family: GH27
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
434	MGYG000003676_8|CGC1	48792.37	5.135

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003676	1891122	MAG	United Republic of Tanzania	Africa

• Gene Location: Start: 2701; End: 4005 Strand: -

Full Sequence      

MHLTNKNTCAPTPPMGWNSYDYYDTTVDEAAVKANADYMAKHLKAYGWEYIVVDIQWYAK
KAGSMRDRYQYIPFSELEMDEYSRLLPDPERFPSSADGSGFKPLADYVHSLGLKFGIHIM
RGIPRIAAHHHGKIKNSSLGAEHVADPTVICGWNPDMYGVRDLPEGQLYYDSLLELYASW
GVDYIKCDDICNTNMHKNPFAAAHEIEMLSNAIQKCGRPIVLSLSPGPALIEKAWFYEKH
ANLWRITDDFWDNWAQLKDMFQRCELWQSHVSAGCYPDCDMLPLGELGKGFATEHHTYFT
PDEQKTMMTLWCLFGSPLMLGAEMTLLDDDTLALLTNTDILAMLPPSVRPHQITRTDNEA
VWYAKDDTTGTTYVALFNLSDALQTVSSTLADADCTLKSVAAKELWSGKALSLNGGFSAS
LAPHACSVCRFETR

Enzyme Prediction     

No EC number prediction in MGYG000003676_00037.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	172	411	1.9e-60	0.9388646288209607

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14792	GH27	6.89e-95	13	342	1	267	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	2.67e-75	10	324	28	356	alpha-galactosidase
PLN03231	PLN03231	2.76e-66	13	324	1	326	putative alpha-galactosidase; Provisional
PLN02692	PLN02692	1.06e-37	7	428	50	405	alpha-galactosidase
PLN02808	PLN02808	9.40e-36	7	426	26	378	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL12733.1	3.14e-221	5	432	2	436
CBL08208.1	3.64e-220	5	432	2	436
VCV23243.1	1.21e-218	5	432	2	436
QQQ91692.1	1.70e-211	5	426	2	429
ASU31152.1	1.70e-211	5	426	2	429

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NX0_A	1.32e-141	10	424	22	433	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	2.13e-140	10	424	22	433	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	2.18e-123	10	424	9	422	ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
1UAS_A	1.81e-33	6	428	2	356	ChainA, alpha-galactosidase [Oryza sativa]
3A5V_A	4.76e-29	6	418	2	373	Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14749	1.01e-35	6	428	49	404	Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1
Q8RX86	1.90e-33	6	428	33	388	Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
Q9FT97	4.56e-33	7	428	48	403	Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 SV=1
Q9FXT4	2.53e-32	6	428	57	411	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
Q8VXZ7	3.41e-32	3	428	63	424	Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 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
1.000065	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003676_00037.