CAZyme Information: MGYG000001683_00452

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Frisingicoccus
• CAZyme ID: MGYG000001683_00452
• CAZy Family: GH165
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
484	MGYG000001683_15|CGC1	55255.13	4.7018

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001683	2591996	MAG	United States	North America

• Gene Location: Start: 8359; End: 9813 Strand: +

Full Sequence      

MAKYLMLDRRFLNPQAMENVALRITPPEKDQANNPLFIQDQPWEIRIDNGYPNVIYDEQA
QIFRCYYTLFTDDLDTEGTTLAERTSRDYLPRMDRVTSLAYAESRDGIHWEKPALGRVEW
RGSKENNILFLFAHGTGVMVDYHGSDSATKYKMVTKVDIPGHGAYMAVAFSPDGVNWSDL
IPWPEYNPPADSHNLPFWNEEEGCYMLLSRIWKDGIRMTTLSRSDDFIHWSEPEETLRGR
GFENQIYSMPVFFWNNLYLGLASIIHEGDRTDVDFDTVDCELTWAVSPEHFDFVAPGQSV
IPRGAGTYPTGDFDCGCIYASQPVKGPDGSLWIYYMGGNGRHTNFRESSLARARWKADRF
ASMVPKREEENSLLTSCKLKFQGPSLEILAEAVEPSVPIYLEAQIHRVWTEAPISGFSYE
ESRVSEMEGGWKRIGWTQGLESLAGTSGCIKLKFKNLKIWAVRGDICLDGHRLWEGADME
NEGF

Enzyme Prediction     

No EC number prediction in MGYG000001683_00452.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH165	16	455	3.6e-54	0.6740157480314961

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08995	GH32_EcAec43-like	2.34e-05	169	258	95	194	Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2). This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). GH32 family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize.
cd08996	GH32_FFase	0.001	102	253	37	187	Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
smart00640	Glyco_32	0.002	102	231	43	174	Glycosyl hydrolases family 32.
cd18622	GH32_Inu-like	0.002	102	230	38	164	glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM12975.1	1.98e-138	1	466	1	467
QGK04006.1	3.36e-127	3	466	6	472
QJS36974.1	3.36e-127	3	466	6	472
QEL28519.1	2.56e-119	3	466	9	458
QFX85916.1	2.59e-107	3	466	61	531

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.999059	0.000853	0.000064	0.000006	0.000002	0.000048

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001683_00452.