CAZyme Information: MGYG000000160_01775

Basic Information

• Species: Collinsella sp003479805
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp003479805
• CAZyme ID: MGYG000000160_01775
• CAZy Family: GH31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1981		216336.25	4.4313

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000160	2098512	Isolate	China	Asia

• Gene Location: Start: 387; End: 6332 Strand: -

Full Sequence      

MHHSSILKRNWVRGSAVIATAALSLALAVPASAAPLTGVKDAKADKNVVTVTFQQGDNEV
TGRITFLEDDIFRYNVDPSGEFSEYAKPKSDAHKARIQAQPDSSSKYNHPDAQVKAEGDR
FVITSGDTTIEFAKDSALMTVKRGGKVVMEETSPLDVDKAGTVQTLKKHDGEDFFGGGTQ
NGRFIHTGTTINIANESNWVDGGVASPNPFYWSDSGYGVMRNTFADGSYDFGATDAGVTT
ARHNENELDAYYFVADAKEGKATAPIAQDLLQDYFQVTGNPVLLPEYAFYVGHLNAWNRD
MWSSEAKDGYGKWQIKGSEPAGAGTGKVQYEKGGTGTSMQPGSHVESLNGHGATEQGENI
PEGTDFPKEFSAQSRLDNYLENDMPLGYFLPNDGYGAGYGVNGFGKTGGVNDDGTSSAER
LAAVAANVQNLKEFTDYANGKGVATGLWTQSQLSPDSNPDTQWQLLRDFKAEVNTGGVTT
LKTDVAWVGNGYSMALDGVKTAYDIITEDVNFRPNIISLDGWAGTQRFAGIWTGDQTGGN
WEYIRFHIPTYIGQSLSGNPNIGSDMDGIFGGQPVVATRDYQWKTFTPLMLDMDGWGSYV
KSPQTHGDPYTGISRMYLKLKSQLLPYIYTSAASAANINTGNGDTGLPMIRAILLNDDSA
YAQSTKTQYEYTFGGSFLVAPVYQNTDGDAANGGIGDGNDLRNGIYLPNYGTEEEPTIWI
DYFTGDQYRGGQVLNNFNAPLWKLPLFVKANAIVPMYEPNDNPEDIDRTKREVEFFATSG
KGEYTLFEDTGTYIENKSDSSNEAYGKEDNIDYGKSVKTTFTSEADVKSGTATFKAGKSE
GAYDGYDSNRTTVFTVNVSKEPESVVAKNGDKELTVEKVDSFDAFKKAEPAEGKAVYFYE
QTPNLNYGATAESEQVRNEDFSKQPINTTPKLHVKFAKTDVNSSEQTLEVKGFENKGELP
GNTLDKNLKAPANLAAPEDGLTPTSIKLTWDKVEGATAYDIEIDGMVNNIPSGDTVEFNV
TDLPYNTEHEFKIRTRTATGYSEWSAPLKVKTLEDPWRNAPKPVHVDWEGGEKWGKLDLA
FDHDDKSGSSFHSTDSVIGMPMTIDYGKTYSLDKFVYTPRQDNGGNGNVSKMKVEVSLDG
ANWTDLGVQTWDNKGEGKMQPKTVDLNGKSARYLRLTVEESTGGFFSATELALYKADKTE
AAETGSLKAPGTVGEEDANHLPNCYGRENRGTGTNDWTSHIVQSNADYNLNNAYDVYDMS
FTMSKLNGGTKKDGKVAGAISVVPEKTSVKAGETITVAVKVKDGKNVNAMGALVKYPVAD
FDFVKDSLKVADSTKGMESHSGMYTFNEPSNSVNIALANRGDKDLWNGSEDVATFQLTAK
KDCEVNLESEAWLIGPTQDFITSTGSEVLPEVKELGRDDFNITITNEHFPTDDGTNVEKL
IQQKSYDNLFNGTETYVDGKVFEFLWNWEPNYVDGKFPEYVKLPVDIHFELKEPRALSDI
EVCNRESGNGRVKKLNVTVFFEDGTKQTFSAGEEDTYTVQIAAENKGKKVKSVDVSPQEA
NGTQMLTICEINFNYTEEDPKPEELKEVSQEQFGITMTNDILTTDDGTNVEKLVESKKYD
GLFNGKEGDADNDFEFKWDLGYNYVNGKLPDYVKLPTTMHFELKDPIVLRDVQILNRKNS
NGSVNSLEAVITYTDGSTTEFKDGDFAKKQEVYTLTADNTKKVKSVDITPLTSDGTATGY
QGEDAKNRMLTLREINFRYVEGDQKPEVPEVNKADLQAKYDELKGKANDGYTEDSWNAFQ
KALEGAKAVLDKADATQSEVDTALKALTDANAGLVKPEVPEVNKADLQAKYDELKGKAND
GYTEDSWNAFQKALEGAKAVLDNEKATQSEVDAALDALVKADAGLTKAENPSPNPDPEDP
KPENPDGNGGQDGSNPGNTNKPGSGLPQTGDPAVVAVAGTGIIGSVTAALGAFFHRRRRD
Q

Enzyme Prediction     

No EC number prediction in MGYG000000160_01775.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH31	266	754	3.5e-47	0.9812646370023419
CBM32	1074	1191	6.2e-19	0.8548387096774194

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06596	GH31_CPE1046	5.88e-137	277	725	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	4.15e-55	46	792	37	708	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd08759	Type_III_cohesin_like	3.12e-42	1278	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.
pfam01055	Glyco_hydro_31	8.24e-41	490	754	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.
cd06589	GH31	2.19e-32	371	618	25	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	17	1951	21	2135
BBK61154.1	0.0	32	1907	35	2069
QNM10857.1	0.0	43	1916	52	2024
BCT46261.1	0.0	43	1916	51	2051
QUO30799.1	0.0	47	1414	38	1380

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6M76_A	1.10e-243	43	1058	45	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	5.95e-243	43	1058	45	963	ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
7F7Q_A	1.64e-242	43	1058	45	963	ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
5X7O_A	1.57e-20	34	801	18	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]
4LPL_A	2.39e-19	1020	1195	8	182	Structureof CBM32-1 from a family 31 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens ATCC 13124]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9F234	1.40e-22	513	799	462	720	Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q9FN05	2.36e-18	360	755	416	780	Probable glucan 1,3-alpha-glucosidase OS=Arabidopsis thaliana OX=3702 GN=PSL5 PE=1 SV=1
B9F676	2.72e-17	513	755	564	778	Probable glucan 1,3-alpha-glucosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os03g0216600 PE=3 SV=1
P79403	8.31e-15	513	791	596	849	Neutral alpha-glucosidase AB OS=Sus scrofa OX=9823 GN=GANAB PE=1 SV=1
O43451	2.62e-14	491	760	587	827	Maltase-glucoamylase OS=Homo sapiens OX=9606 GN=MGAM PE=1 SV=6

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
0.000473	0.998577	0.000228	0.000271	0.000225	0.000191

TMHMM  Annotations     

start	end
12	34
1952	1974