CAZyme Information: MGYG000002461_01085

Basic Information

• Species: Yersinia kristensenii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Yersinia; Yersinia kristensenii
• CAZyme ID: MGYG000002461_01085
• CAZy Family: GH36
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
632	MGYG000002461_2|CGC2	71658.09	6.1182

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002461	4771112	Isolate	Finland	Europe

• Gene Location: Start: 213229; End: 215127 Strand: +

Full Sequence      

MKTILKSSLLLLLVSNTAFSAEYLLNNDKISISFDDTNSAVVVKDKISDHKLAPLELFFL
TLPNEDIIRAADFKIKHVSQTDDAIHIDYEHKDFDVTVVLNVLKDKYASIDYTIKAKGAS
RYVAKITFFPTKGQSQAPYVDGAVNSSPIIADSFFILPEKPIVNTYAYETTTNLNVELKT
PIKTDAPLTFTTYFGTFEENNQLRRSFNQFINALRARPYQPYLHYNSWMDIGFFTTYTEQ
EVLERMDTYANELIKKRGVKLDGFLLDDGWDDRTGKWLFGPAFSEGFSAVKEKADSLHTS
VGLWLSPWGGYNKPRDIRVSHAKENGFETVDGKFALSGPNYFHNFNEQIIKLIKDEHITS
FKLDGMGNANSYIKGSPFASDFDASIELIKNMRAANKDLFINLTTGTNASPSWLFYADSI
WRQGDDINVFGKGSPAQQWMTYRDAETYRSIVRKGPLFPINSLMYHGIVSAENAYFGLEK
VQTDRDFADQVWSYFATGTQLQELYITPSMLNSNKWDTLANAAKWSRKNSDILVDTHWIG
GDPTALEVYGWASWSPNKAILGLRNPSDKAQSYYLDLTKNFEIPLKETTRFTLKPIYGTN
ATLVEDYHKPMIVTLQPLETLVVEAIPVANKK

Enzyme Prediction     

No EC number prediction in MGYG000002461_01085.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06592	GH31_NET37	6.36e-07	225	365	5	151	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.
COG3345	GalA	0.002	215	307	290	377	Alpha-galactosidase [Carbohydrate transport and metabolism].
cd06589	GH31	0.002	231	277	15	56	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.
cd14791	GH36	0.002	216	401	1	194	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKJ16738.1	0.0	1	632	1	632
ATM95585.1	0.0	1	630	1	630
AHM73621.2	0.0	1	632	1	632
QGR66890.1	0.0	1	632	1	632
QGR71906.1	0.0	1	632	1	632

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000559	0.998645	0.000216	0.000194	0.000183	0.000172

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002461_01085.