CAZyme Information: MGYG000002537_00610

Basic Information

• Species: Kocuria rhizophila
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Micrococcaceae; Kocuria; Kocuria rhizophila
• CAZyme ID: MGYG000002537_00610
• CAZy Family: GH13
• CAZyme Description: Amylosucrase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
653	MGYG000002537_4|CGC1	72996.03	5.9327

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002537	2636961	Isolate	India	Asia

• Gene Location: Start: 73937; End: 75898 Strand: +

Full Sequence      

MLSDNIPRRITGRENLLAVLQEHLVRDTRVAAADRDVFLHRLPQQLPRIVTSLSAVYGSG
PEIWDVVARAVLTAWDAYAERPADLRDLDRQREGAAPWFTSREAVGGVCYVDRYAGTIAG
LREQIPYFRELGLSYLHLMPLYESPAGNSDGGYAVSSYRRVDPALGTMEELAELAAELRS
QGIALVLDFVFNHTSNEHEWARAAAAGDPHFERFYWIHRDRTLPDAFERTAREIFPDDHP
GVFTRVDSTPAGRAASPFDPDPRWVWTTFHRFQWDLNYANPEVFHAMAGEMLFLANQGAQ
VLRLDAVAFIWKQLGTTCESQPQVHDLLRAFRAVAALAAPAVEFKSEAIVHPDEVIRYVH
PEQCALSYNPLQMALTWEALATRDVTLLSAALAERHETPEGTAWVNYVRGHDDIGWTFSD
DDAARLGVDPAGHRRFLNAFYTGRHPGSFADGVAFQDNPRTGDCRICGTTASLLGLEAEP
GPAVDRILLAHSLAMSTGGVPLVYLGDEVGQLNDPHWSQEPGHGDDARWVHRPRRREADH
ERRHDLFSVQGRIFGGIRGMIAVRRRTPEFEGTTLIPFDTHNSHVLGYQRPGEHSLVLCL
ANVSDWSQFVTGETLSGFLPTATLLHAQSEVDLRGGILLEAHGFRWLRVIPVR

Enzyme Prediction     

EC	2.4.1.4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	115	513	4.9e-175	0.9975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11324	AmyAc_Amylosucrase	0.0	34	570	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	1.28e-50	116	524	24	400	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	9.37e-46	134	570	39	442	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	1.46e-42	109	572	8	441	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	2.08e-37	116	617	26	497	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTK31613.1	0.0	1	653	1	653
QIR68701.1	0.0	1	651	1	652
QBJ20461.1	0.0	1	651	1	652
QMS55954.1	0.0	4	651	5	652
ALU41010.1	0.0	36	653	32	640

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1G5A_A	2.98e-232	38	649	32	627	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	3.43e-232	38	649	36	631	Crystalstructure of amylosucrase from Neisseria polysaccharea in complex with turanose [Neisseria polysaccharea]
1MVY_A	5.99e-232	38	649	32	627	ChainA, amylosucrase [Neisseria polysaccharea],1MW0_A Chain A, amylosucrase [Neisseria polysaccharea],1S46_A Chain A, amylosucrase [Neisseria polysaccharea],1ZS2_A Chain A, amylosucrase [Neisseria polysaccharea]
1JGI_A	6.88e-231	38	649	32	627	ChainA, amylosucrase [Neisseria polysaccharea]
4FLR_A	1.38e-230	38	649	32	627	Crystalstructure of Amylosucrase double mutant A289P-F290L from Neisseria polysaccharea [Neisseria polysaccharea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZEU2	1.88e-232	38	649	40	635	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
Q84HD6	9.29e-228	38	649	40	635	Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
O06458	5.93e-35	116	652	28	540	Trehalose synthase OS=Thermus thermophilus OX=274 GN=treS PE=3 SV=1
P72235	2.97e-34	116	649	38	562	Trehalose synthase OS=Pimelobacter sp. (strain R48) OX=51662 GN=treS PE=3 SV=1
A0R6E0	6.49e-34	116	649	58	582	Trehalose synthase/amylase TreS OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=treS 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
1.000054	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002537_00610.