CAZyme Information: MGYG000001063_05631

Basic Information

• Species: Robinsoniella sp900540475
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella sp900540475
• CAZyme ID: MGYG000001063_05631
• CAZy Family: GH36
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1257	MGYG000001063_146|CGC2	139968.8	5.371

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001063	7637037	MAG	Sweden	Europe

• Gene Location: Start: 76734; End: 80507 Strand: -

Full Sequence      

MKKKTFAMIGALLMLAGTLGGSGFHVNASSTEAKQITGNGVSVTFSRDEGTVQLYRIDAN
GNQTVMTQSSQVSSPVVKGQEVRDFSDFQCEVQENVTGDAGAGSRMTITSVSKNTGLQRS
VVIETVDEVKGLLHISSSYKAMEEEINAEEFIDSRFSLDHPSNTMWSYNGGGEGSQSWYD
TLQKIDLTDGERFYRENLQDDTAAGIPVADIYGEQGGVTVGDASVTRRQLSTPVNEKNGS
VEVSVKHPGTVLALHEETKTSQSFVNVHSGDYYMGLRGYSDGMKQIGFTTLSRDQIPESS
YELRWESWGWEFDWTVELIINKLDELKEMGIKQITLDDGWYNAAGEWGLNSWKLPNGAAD
MRRLTDAIHERGMTAVLWWRPCDGGREDSALYQEHPEYFIKNQDGSLGKLAGPGQFNSFL
GSCGYALCPLSEGAVQSQVDFINRAMNDWGFDGFKSDYVWSLPKCYSQEHRHARPEESTE
QQAQFYRAVYEAMTANNPDAFHLLCNCGTPQDFYSLPYVTQVPTADPTSVDQTRRRVKAY
KALCGDYFPVTTDHNEVWYPSTVGTGAILIEKRDLSGWEEEEYAKWLKIAQENELYKGTF
IGDLYSYGYDPYETYTVDKDGVMYYAFYKDGSRYRPEGNPDIELKGLEDGKLYRIVDYVN
NLVVATNITTSNAVFSYPFSDYLLVKAVEISEPDTEGPGPVPDPVGTVTVEENAPELEYS
GNWVREENEGYHGGGACYTKEAEASVELEFYGTGAAWYGQHDVNFGTARISIDGTYVQTV
SCMGAPGINIKLFEVSDLKLGSHRIRIECETPVIDIDRLTYTKGEEIPSKLKTGDLRALA
DLANKYDMSSFEDGSYKDQMGVSLVRANQLLAADNVTQSAVNEEQKYLLNAMLKLRKKVH
KDWIGLSGPTPGEIPTEDISRENLAKVIAYTEQLEKDRIIPAVKEQLSTSYEQAVSISER
QDASQAEIDRAWSALMNAVQYSGYTQGSKEKLSVLLDECKKVDTDIYKDTAAFLASLEAA
EKVYQDENAMDGEIGDCIGQLQNAKEQLELKDPVNPPKPDPDPQPKPDPSPGPNPNPILK
KPEQVAGVKVKAETASLTVSWKKLHNAKSYKVYIYKSGKWRLAGKTTKTTYKIKKLASGT
RYTIKVAAVNKSGQGKYSQQVYTAAKPEKVKLKSVSRYRTTKVRLNYGKVKAGGYEIWMK
DGNHAYKKAGTSSKTTAVKGGLKKGKTYYFKIRAYVKNKNKVIYGSFSNVKKYKRVL

Enzyme Prediction     

No EC number prediction in MGYG000001063_05631.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH36	275	529	4.8e-32	0.35755813953488375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14791	GH36	6.96e-35	305	554	6	244	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 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. GH36 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.
pfam02065	Melibiase	2.63e-14	279	528	11	262	Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.
COG3345	GalA	1.27e-13	305	401	296	396	Alpha-galactosidase [Carbohydrate transport and metabolism].
cd11313	AmyAc_arch_bac_AmyA	3.04e-06	319	408	24	124	Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
cd06592	GH31_NET37	5.45e-06	305	486	5	181	glucosidase NET37. NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIA30399.1	0.0	36	821	46	824
QQR05374.1	0.0	36	821	46	824
ANU41754.1	0.0	36	821	46	824
ABF39669.1	2.50e-87	7	687	20	681
ARU29327.1	2.64e-86	77	690	76	689

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6PHU_A	3.94e-11	222	401	272	447	SpAgawild type apo structure [Streptococcus pneumoniae TIGR4],6PHV_A Chain A, Alpha-galactosidase [Streptococcus pneumoniae TIGR4]
6PHW_A	3.94e-11	222	401	272	447	ChainA, Alpha-galactosidase [Streptococcus pneumoniae TIGR4],6PHX_A SpAga D472N structure in complex with raffinose [Streptococcus pneumoniae TIGR4],6PHY_A Chain A, Alpha-galactosidase [Streptococcus pneumoniae TIGR4],6PI0_A AgaD472N-Linear Blood group B type 2 trisaccharide complex structure [Streptococcus pneumoniae TIGR4]
4FNU_A	1.03e-09	275	447	303	480	Crystalstructure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus],4FNU_B Crystal structure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus],4FNU_C Crystal structure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus],4FNU_D Crystal structure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus]
4FNR_A	1.78e-09	275	400	303	432	Crystalstructure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_B Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_C Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_D Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
4FNP_A	3.08e-09	275	400	303	432	Crystalstructure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_B Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_C Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_D Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNS_A Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_B Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_C Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_D Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P0DTR5	0.0	36	821	46	824	A type blood alpha-D-galactosamine galactosaminidase OS=Flavonifractor plautii OX=292800 PE=1 SV=1
P0DTR4	2.45e-18	699	821	647	769	A type blood N-acetyl-alpha-D-galactosamine deacetylase OS=Flavonifractor plautii OX=292800 PE=1 SV=1
Q9ALJ4	9.77e-09	275	400	303	432	Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.028563	0.731760	0.238636	0.000458	0.000295	0.000267

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001063_05631.