CAZyme Information: MGYG000001446_02061

Basic Information

• Species: Cutibacterium avidum
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Propionibacteriales; Propionibacteriaceae; Cutibacterium; Cutibacterium avidum
• CAZyme ID: MGYG000001446_02061
• CAZy Family: GH13
• CAZyme Description: Amylosucrase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
637		72604.81	4.8152

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001446	2726478	Isolate	not provided	not provided

• Gene Location: Start: 2200100; End: 2202013 Strand: -

Full Sequence      

MVADDSLRHASLDPSTQQSFELRWERYLPDLWIGLSSVYGDRADETLQRVRDILVTRIAK
RPDDLKRLDEARLLEPDWLQKPSMIGYATYTDRFAGTIKGINDHLDHLSEMGVRYLHLMP
LLQPRQGVNDGGYAVADHHTIRTDLGTMDDLDDLTTTLRSHGISLVVDLVVNHVAAEHEW
AQRARAGQQKYRDYFHVLKTQEEVDAWEKDLPEVFPDFARGNFTWNDDCQGWVWTTFNEF
QWDLNWANPDVFCEFLDFMCELANRGVEVFRLDAIAFIWKKLGTGCQNLPQVHDITQSLR
QAMRIVAPAVAFKAEAVVGPNDLIGYLGRGRHWSRLSDMAYHNSLMVQLWSALAARDVSL
METALSRVPDKPSTTTWATYARCHDDIGWAIDDADARDTGLDPVAHRQFLSDFYSGDFPG
SFARGLVFQDNPETGDRRISGSLASLAGLERALEAEDPALIDAAIARIVMLHTAILGYGG
VPLIWMGDEVGMLNDDWQRDPDHTDDNRWVHRPVMDWSLVEQAQAEPHSVPGRIWRGVRR
AINARRRSPEFHASVETVVLPSPSRKVIMWGRPHPEGRMIELYNISEQEVWFPMETLRSE
LDDVVTELLSGFDYDLTPMNLRLAPYECLWLSARPGS

Enzyme Prediction     

EC	2.4.1.4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	95	494	2.4e-189	0.9975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11324	AmyAc_Amylosucrase	0.0	16	551	1	536	Alpha amylase catalytic domain found in Amylosucrase. Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. 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.
cd11334	AmyAc_TreS	2.70e-55	96	502	24	385	Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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.
cd11356	AmyAc_Sucrose_phosphorylase-like_1	1.89e-48	101	565	30	456	Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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.
cd11343	AmyAc_Sucrose_phosphorylase-like	1.47e-43	89	552	8	440	Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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.
COG0366	AmyA	3.69e-41	85	592	2	490	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRH10757.1	0.0	1	637	1	637
BCQ02437.1	0.0	1	637	1	637
AGJ77921.1	0.0	1	637	1	637
BCQ04825.1	0.0	1	637	1	637
AOG27602.1	0.0	1	637	1	637

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3UCQ_A	9.72e-278	7	633	19	650	Crystalstructure of amylosucrase from Deinococcus geothermalis [Deinococcus geothermalis DSM 11300],3UER_A Crystal structure of amylosucrase from Deinococcus geothermalis in complex with turanose [Deinococcus geothermalis DSM 11300]
4AYS_A	3.39e-269	7	633	14	646	TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans]
7ESH_A	3.78e-258	6	632	19	645	ChainA, amylosucrase [Calidithermus timidus DSM 17022],7ESH_B Chain B, amylosucrase [Calidithermus timidus DSM 17022],7ESH_C Chain C, amylosucrase [Calidithermus timidus DSM 17022],7ESH_D Chain D, amylosucrase [Calidithermus timidus DSM 17022]
1G5A_A	1.15e-149	18	631	30	625	AmylosucraseFrom Neisseria Polysaccharea [Neisseria polysaccharea],1JG9_A Crystal Structure of Amylosucrase from Neisseria polysaccharea in Complex with D-glucose [Neisseria polysaccharea],1MW1_A Amylosucrase soaked with 14mM sucrose. [Neisseria polysaccharea],1MW2_A Amylosucrase soaked with 100mM sucrose [Neisseria polysaccharea],1MW3_A Amylosucrase soaked with 1M sucrose [Neisseria polysaccharea]
3UEQ_A	1.30e-149	18	631	34	629	Crystalstructure of amylosucrase from Neisseria polysaccharea in complex with turanose [Neisseria polysaccharea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZEU2	7.18e-150	18	631	38	633	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
Q84HD6	1.28e-147	18	631	38	633	Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
O06458	1.03e-41	96	586	28	489	Trehalose synthase OS=Thermus thermophilus OX=274 GN=treS PE=3 SV=1
A0R6E0	4.36e-39	96	535	58	447	Trehalose synthase/amylase TreS OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=treS PE=1 SV=1
G0GBS4	5.53e-39	89	632	61	581	Glucosylglycerate phosphorylase OS=Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203) OX=869211 GN=Spith_0877 PE=1 SV=1

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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001446_02061.