CAZyme Information: MGYG000004715_00078

Basic Information

• Species: Eubacterium_T saphenum_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Anaerovoracaceae; Eubacterium_T; Eubacterium_T saphenum_A
• CAZyme ID: MGYG000004715_00078
• CAZy Family: GH13
• CAZyme Description: HMP-PP phosphatase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
900	MGYG000004715_1|CGC4	103492.14	4.9742

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004715	2297538	MAG	China	Asia

• Gene Location: Start: 80471; End: 83173 Strand: -

Full Sequence      

MKKEMRSEKSSFQQRFAEYEDELKWLYMELYSGRDEDYQNYVKMLREYCTERSPELKAWD
RSKQEDPDWYKRNDLLGTMMYTENFGKTLKGVESRLDYLQECGINFLHLMPLLESPEGKS
DGGYSVSDFRKVQPQLGTMEDLSELTHACHKRNIQVCLDFVMNHTSDEHEWAKQAKAGDP
YAQGRYFFFDNWDIPNQFEQTVPQVFPQTAPGNFSWCDEAHKVVMTTFHPYQWDLNFRNP
SVMHDMTANLLNLCNHGIDIIRLDAVPYIWKELGTSCRNLLRVHTLVRILRMVLDIVCPG
TLLLGEIVMKPNEVAPYFGTPEKPECHMVYNAPIMATTWHTVATRDVRLLKHQIGQTLVL
PHDFVFLNYLRCHDDIGWGLDYDFLAQFGTTEAAHKHFLNDYLQGHWEGSDARGELYNDD
PRLQDARLCGTTASLCGIEAAEYEQNDWKLERAETLDIMLHAFLLTQSGIPMLYSGDEIG
QRNDYSYHEDPLKWDDSRYLHRGKFPWEQAAMRDDETTRPGRIFQAIKRMEKIRRSHVCF
ENNADVWIMEPYNDHILALGRYYKGEKLVALFNFNVYDETAWVNESEEYVDLITGEHCHA
QGVPVPARSFRWLLTDFGTNSDQQEKKKDGPKIVFLDIDGTLTKSGENTPPKSALQAIRK
AQENGHYVFLCTGRNLAMAEPLLKYGFDGIIASAGALVIAGGEVLHDEPMEPEDFCKAMD
ALQSNHVYCTIESKEGSYCDPDIGKLLKGQPRGNSELERWRKQINESLGIKPMKEYKGEP
VYKIVIMFNDRRQLKEAEELLPQYDFVLQDEVFGVQNGELIRKTCNKGTGVKCVSEKLNI
PLEDTIGFGDSMNDYAMMKTTGISVCMGNGSETLKKQSDIIADPVDEDGLAGAFEKLHLI

Enzyme Prediction     

No EC number prediction in MGYG000004715_00078.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	87	483	4.9e-166	0.995

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11324	AmyAc_Amylosucrase	0.0	11	537	4	533	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	1.42e-64	88	498	25	397	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	2.50e-62	97	544	32	446	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.
pfam08282	Hydrolase_3	1.27e-55	634	891	1	251	haloacid dehalogenase-like hydrolase. This family contains haloacid dehalogenase-like hydrolase enzymes.
cd11343	AmyAc_Sucrose_phosphorylase-like	2.12e-54	87	544	19	443	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUI96207.1	0.0	12	617	6	611
BBH25288.1	3.94e-316	12	625	10	623
AHF24012.1	2.62e-294	12	614	10	613
QTE69671.1	3.21e-289	44	617	1	574
QTE72082.1	2.44e-287	12	617	10	616

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7ESH_A	2.51e-133	52	575	73	599	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]
5N7J_A	1.61e-128	50	580	73	587	Crystalstructure of Neisseria polysaccharea amylosucrase mutant efficient for the synthesis of controlled size maltooligosaccharides [Neisseria polysaccharea]
4FLQ_A	8.79e-128	50	580	73	587	Crystalstructure of Amylosucrase double mutant A289P-F290I from Neisseria polysaccharea. [Neisseria polysaccharea]
4FLR_A	8.79e-128	50	580	73	587	Crystalstructure of Amylosucrase double mutant A289P-F290L from Neisseria polysaccharea [Neisseria polysaccharea]
4FLO_A	1.23e-127	50	580	73	587	Crystalstructure of Amylosucrase double mutant A289P-F290C from Neisseria polysaccharea [Neisseria polysaccharea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q84HD6	2.20e-127	50	580	81	595	Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
Q9ZEU2	1.20e-126	50	580	81	595	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
P72235	8.88e-49	65	480	11	396	Trehalose synthase OS=Pimelobacter sp. (strain R48) OX=51662 GN=treS PE=3 SV=1
A0R6E0	3.06e-48	61	498	27	434	Trehalose synthase/amylase TreS OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=treS PE=1 SV=1
P9WQ18	1.57e-47	66	498	40	442	Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treS PE=3 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
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004715_00078.