CAZyme Information: MGYG000004269_02380

Basic Information

• Species: Blautia_A schinkii
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A schinkii
• CAZyme ID: MGYG000004269_02380
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
674	MGYG000004269_195|CGC1	75628.74	5.1659

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004269	3002846	MAG	China	Asia

• Gene Location: Start: 1193; End: 3217 Strand: +

Full Sequence      

MSTKRLQKKKAAMQAKKEKQLKKNTAAAGTSASAVNSVENAKVETEKIETVKKEPLKVET
SKTEPLKVETSKTEPIKVETFKTEPIKVETSKTEPIKVETSKTEPIKVETSKTEPAKVTT
SKTEPLKVETSKEDTAYDALYEKRLNRYYNDLKWLYCELFRDHPEVAGTFSSLTKKMKEI
YRERSLSMKEADQACAQNPDWFRKTTFTGMAVNPADFADTLSGLSNKLDYVSECKADTLY
LTDLFQATSNCSLRIIPEIGTSEDLHTLAANCQKADIRLALEIPLSLSVDDPQSGSPCVL
QTPAFFNAMLLQILELANVGASVFSLGVLPMLNTEDLWKLHSLLRMTRMVCEIVCPGVLL
LGEPDRTPAEAAAFGGTSDMPELHIVNSTQLMSDIWHTVATKDTSLLRHGIDKTAALSQA
PVFQNYLRNRNTVRWNLDYDFLKDSFITEGPHRDYLNEFLSGTFPDSFARGEIYINTETE
ESELCGTTASLAGIERFDYEGNADGVSRGIRYDVTLHALLLSLPGIPVLRSGDEIGQLND
YTYKTYSSKTADPRWLHNGHFNWVLAQNRADAETIQGRIFNSLEQLEAIRNSHSVFAPEI
PSHTLETWDKALLALVRETEQEKLICLYNFSDQDKVAWINEQDGTYTDLLTGVQRDAQAV
EIPAFGFIWLMRTK

Enzyme Prediction     

No EC number prediction in MGYG000004269_02380.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	301	539	1.7e-60	0.6175

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11324	AmyAc_Amylosucrase	4.67e-112	138	596	2	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	2.00e-09	333	536	208	374	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.
pfam16657	Malt_amylase_C	1.70e-05	605	669	6	75	Maltogenic Amylase, C-terminal domain. This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyzes starch material. Maltogenic amylases are central to carbohydrate metabolism.
cd11338	AmyAc_CMD	1.82e-04	220	279	54	119	Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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.
COG0810	TonB	3.12e-04	40	147	45	161	Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCU02723.1	0.0	1	674	1	694
CBL22253.1	2.60e-161	138	674	97	709
BDA10513.1	4.78e-130	138	674	27	640
SNU99921.1	1.69e-129	138	674	34	649
QIB60618.1	7.44e-129	138	674	27	640

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4AYS_A	1.04e-42	133	632	19	600	TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans]
3UCQ_A	4.24e-41	144	633	35	605	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]
7ESH_A	5.78e-41	144	670	36	644	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]
4FLR_A	8.18e-38	141	632	32	583	Crystalstructure of Amylosucrase double mutant A289P-F290L from Neisseria polysaccharea [Neisseria polysaccharea]
4FLQ_A	1.10e-37	141	632	32	583	Crystalstructure of Amylosucrase double mutant A289P-F290I from Neisseria polysaccharea. [Neisseria polysaccharea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZEU2	9.42e-36	141	632	40	591	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
Q84HD6	1.01e-34	141	632	40	591	Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
A0R6E0	6.28e-09	200	615	34	483	Trehalose synthase/amylase TreS OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=treS PE=1 SV=1
P76041	7.27e-08	330	670	238	558	Glucosylglycerate phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=ycjM PE=1 SV=2
P9WQ18	9.14e-07	194	673	36	585	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
1.000026	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004269_02380.