CAZyme Information: MGYG000001588_00814

Basic Information

• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella
• CAZyme ID: MGYG000001588_00814
• CAZy Family: GH31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2127		229316.69	4.2561

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001588	2411406	MAG	Canada	North America

• Gene Location: Start: 15653; End: 22036 Strand: +

Full Sequence      

MLATAALSLALTAPAQAAPLTGVESAAVNAENNYVVDVNFAGGIKGKITFLEDGIFRYNV
DPSGEFDEYAVPRSKDHVAKIQAQPDASDEYSHPKATVADKDGAFVISAGDTTISLDKKT
AKMTVKSGDKVVLEEQAALDLSESSTVQSLVKHSGENFFGGGTQNGRFIHTGNVINIANE
SSWTDGGVSSPNPFYWSDAGYGVLRNTFQDGSYDFGKTTDGVTTATHNENELDAYYFVAD
AASGKSTAPIAQDLLQDYFKVTGNPVLLPEYAFYVGHLNAWNRDMWSDTAQAGYNSKWQI
KGGEDSKDANAGDIEYEKGGTGTEMQANTTVETLNGTGPSVATDNIPEGVTFDKDYSAQS
RLNSYLENDMPLGYFLPNDGYGAGYGQNGYKMTGGVNEDGSSSKERLAAVDANIANLKTF
SDYASSKGVATGLWTQSQITPDSDPNTQWQLLRDFKKEVEVGGVTTLKTDVAWVGPGYSF
ALNGTKTAYDIATNPENKTATRPNIITLDGWAGTQRYAGIWTGDQSGGNWEYIRFHVPTY
IGQSLSGNPNIGSDNDGIWGGNPVIATRDYQWKSFAPLMLDMDGWGSYVKAPQTHGDPYT
GITRMYLKLKSSLMPYIYTTAASAANLDTGNGDEGLPIVRAILLSDDSDYAASTATQYEY
TLGEDILVAPIVANTDGDDSNGEVGDGDDIRNGIYLPGDENTIWVDYFTGDQYRGGQVLN
NFDAPLWKLPVFVKANAIIPMYEPNNNPADIDRTIRNVEFFATNGENSYTQYEDDGVFID
SELDTSDAAYGTENDVNYGGHVSTTYTSKVNGDKATFTAEKSTGSYTGYEKDRTTSFVVN
ASKEPASVVAKNGDTTLKQKKVTSQEEFDKATPAEGEFIYFYNTKPNMNYNSSSAATDAV
KKEGFSSKEIITTPKLYVKFAKADVQANKQTLEITGFENKGETPSDTVIDSLKVPTLKQP
SEEAGDLTPTSFRLSWDKVDGASSYELMIDGMLNTVPAGTPEEPNTTLNVLDQAYHSTHT
VQIRQRTAEGVSNWSDEITVVTLEDPWRNVPTPANVTWEGGESWGALSNAFNHSTGDMFH
ADDATALNMPMTIDYGKVYKLDKFVYTPRQDNGGNGNVAKMKIETSIDGVHWVEHDAGTW
DNKGANKLADKEVDLKGNFARYLRLTPLESNGNMFSAAELALYKVEGSQGVEQGSIAGDP
TINSVDYDQINNCIGRENRGDEAEGQWKPHVANNGADFNFNDAYDVYDMSQTMFRLDGGT
KKTDKLSGNIAVVPSKTSVKAGETITVDLYAESIKNANALGALIHFNDAQFEYVNESLTK
SPYTGSMENKSVVKTQYEDGVQSANIALVNKGDKDLFSGSGAVASFKLKAKTDIENVALE
STAWAIGPTFDVVEVADDGSIEYPDVPKPEAGELGQDAFNIKLTNKALPTDENGTNVSEL
VQSKSYEGLFNNNNTGRDFEFKWFLPTAPQDFDERVGLPATLSFELKEPRTLTNVELFNG
AQASNGSINSLEAVVTFEDGTKQEFKGGDFSTNQEKYIFQISDENKGKKVTKVEIKPLTS
TGVATGLEDPNNRMLTIGEINFNYQESEVAVDSVVLGDNAKTLHVGELSEVKASIKPETV
NYPYFKVTSSDPEVASIVTKQVGDKIVNFVRANKAGKATITVASALDETKTASYEVEVTD
AVNTTPLEEALAEARTYSADAYTAETFEKLTAAIKAGEDLLKSGELTDQKVAEATVAIRD
AIKGLEQRPVDESKLINKDKNSGVAVLKANSSAAESPYTNALDYDESTLWHSNYNDQDVL
PDYLIFDLGDTYDLTDVSFLPRQDGATNGDIFEAKIYVANSAEELDGDGKGSLVGTFTFD
NNGKVLNNRDEYKNMAFGAQATRFVKIEATRAGGDKADAYASIAETRFYGQKHTDQDQAD
KSKLDALVAEIEAKGLKAEDYTAATWKKFELALGDAKATLADPQATQTEVDSQLAALQSA
YEGLEKTEVPPVENPDRDQLQSLIDKAEKIDTTGKTNESVQALVDAIDAAKAVLANEDAT
PEQIKAAYDALAAAIDGLTDAGNGGQNGNGGQNGGDNSQGGKPGSGSNSGSGELPHTGDA
ATVAVAATGVVGSLTAAIGAFLHRRRK

Enzyme Prediction     

No EC number prediction in MGYG000001588_00814.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH31	251	739	1.1e-47	0.9789227166276346

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06596	GH31_CPE1046	8.76e-134	261	710	1	334	Clostridium CPE1046-like. CPE1046 is an uncharacterized Clostridium perfringens protein with a glycosyl hydrolase family 31 (GH31) domain. The domain architecture of CPE1046 and its orthologs includes a C-terminal fibronectin type 3 (FN3) domain and a coagulation factor 5/8 type C domain in addition to the GH31 domain. 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.
COG1501	YicI	3.90e-53	104	834	103	752	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
pfam01055	Glyco_hydro_31	7.44e-41	480	739	210	442	Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
cd08759	Type_III_cohesin_like	1.12e-32	1268	1437	1	167	Cohesin domain, interaction partner of dockerin. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. Two specific calcium-dependent interactions between cohesin and dockerin appear to be essential for cellulosome assembly, type I and type II. This subfamily represents type III cohesins and closely related domains.
cd06589	GH31	8.23e-30	365	607	33	265	glycosyl hydrolase family 31 (GH31). GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of 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. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWT17625.1	0.0	1	2065	21	2112
BCT46261.1	0.0	38	2060	59	2041
QNM10857.1	0.0	35	2061	57	2010
BBK61154.1	0.0	20	2058	39	2067
BBK23937.1	0.0	35	2058	70	1996

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6M76_A	1.76e-228	30	1048	46	963	GH31alpha-N-acetylgalactosaminidase from Enterococcus faecalis [Enterococcus faecalis ATCC 10100],6M77_A GH31 alpha-N-acetylgalactosaminidase from Enterococcus faecalis in complex with N-acetylgalactosamine [Enterococcus faecalis ATCC 10100]
7F7R_A	9.30e-228	30	1048	46	963	ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
7F7Q_A	2.53e-227	30	1048	46	963	ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
5X7O_A	1.13e-17	47	786	48	728	Crystalstructure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase [Paenibacillus sp. 598K],5X7O_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase [Paenibacillus sp. 598K],5X7P_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with acarbose [Paenibacillus sp. 598K],5X7P_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with acarbose [Paenibacillus sp. 598K],5X7Q_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with maltohexaose [Paenibacillus sp. 598K],5X7Q_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with maltohexaose [Paenibacillus sp. 598K],5X7R_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with isomaltohexaose [Paenibacillus sp. 598K],5X7R_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with isomaltohexaose [Paenibacillus sp. 598K],5X7S_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase, terbium derivative [Paenibacillus sp. 598K],5X7S_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase, terbium derivative [Paenibacillus sp. 598K]
5F7C_A	6.99e-17	447	750	438	726	Crystalstructure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_B Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_C Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_D Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9F234	1.37e-21	502	776	462	711	Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
B9F676	2.26e-17	477	740	544	778	Probable glucan 1,3-alpha-glucosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os03g0216600 PE=3 SV=1
Q9FN05	2.27e-17	459	740	531	780	Probable glucan 1,3-alpha-glucosidase OS=Arabidopsis thaliana OX=3702 GN=PSL5 PE=1 SV=1
Q8BVW0	1.15e-14	497	741	544	765	Neutral alpha-glucosidase C OS=Mus musculus OX=10090 GN=Ganc PE=1 SV=2
P79403	6.05e-14	502	742	596	813	Neutral alpha-glucosidase AB OS=Sus scrofa OX=9823 GN=GANAB 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
0.000680	0.998387	0.000232	0.000267	0.000216	0.000198

TMHMM  Annotations     

start	end
2100	2122