CAZyme Information: MGYG000003112_00521

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E
• CAZyme ID: MGYG000003112_00521
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
927	MGYG000003112_70|CGC1	100173.29	4.3821

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003112	1402119	MAG	Sweden	Europe

• Gene Location: Start: 4; End: 2787 Strand: +

Full Sequence      

MSLAGLPDFKTDSTATVGIPNILKKKWTKEGRLAQETSELSSYLSKTGKNQTVTNTISYW
LSTWVRDYGVDGFRCDTAKHVDLASWKTLKDTCVDALKEWRQNNPSKPGADWDEDFWMTG
ECWDHNIGWGYDSYYTQGGFDSMINFETQGGGLLTMSGLDGVYSNYASSINSNDKFNQLS
YLSSHDSTLARGNLISTGSAFLLLPGGIQIYYGDETNRPLVSGVPNDGNGGAGHSLRSDM
NWDSADSAVLAHWQKVGSFRNKHVSIGAGDHQQISGYSSSTGYTFSRSYDNGVISDNIIA
TIGAPSNTNLAVDVSSLWSDGTTVTNAYDGTTATVTNGKATFNTGANGTILIEGPVSTIS
MSLKGSYSFYDSQTLTVSLRGADYAMVSIDGGTEFKVVDGDTFSVGEGVEVGATIKVTMT
ASNDEETSTKSFTYKKKDPNAVVRVYFDNAKYNWSTVNAYIYDESSGNAVENKKWPGETM
TYDTATGFYMIEVPDNLTNGRVIFNAGSSSSNRYPGDSEQGLAINETNMLFSYGNKWEPY
TNQTPDPTEPTTAPDPTKTTTVYFDNSNSKFSTPTIYYWSYATNSGPNSWPGVAMTKVSG
DIWKATFDSKYDGCIFSNNGSNKTGDLTIPGSNYIYNGSSWSAYTEPTEPTTAPATTVPA
TTAPVTTAPVTTVPATTAPATTVPATTAPAPVTDELKVTASSNIFPTATKTFNKDEGTIT
VSYKLTANMDAVDAQWKLTYDNTKLEYKASNNMSGGVQTITPSAGKNLVYQNINNYIKGN
FSTLNLVPFENNADFVSVTFNIIGTGEAEVYLDLEVLSLGYTDSSDNFHHASIVDYSKMQ
NISGIKGFENASISTSTTLDSNIMLGDINGDGYIKIDDVTLILKNVVGLQSFNSLQIKAA
DVDKDGIVSVKDATLIQKFIADMISEF

Enzyme Prediction     

No EC number prediction in MGYG000003112_00521.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	216	1.5e-70	0.5527777777777778

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	2.33e-82	1	291	400	672	alpha-amylase; Reviewed
cd00551	AmyAc_family	1.97e-16	57	212	98	253	Alpha amylase catalytic domain family. 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; and 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 this 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.
cd14256	Dockerin_I	3.31e-14	865	921	1	57	Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
pfam16738	CBM26	9.08e-14	562	628	1	68	Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.
cd11339	AmyAc_bac_CMD_like_2	1.07e-12	31	263	125	344	Alpha amylase catalytic domain found in bacterial 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). This group of CMDs is bacterial. 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
QCT06045.1	3.54e-285	3	652	270	909
BCN30960.1	1.81e-155	1	631	274	885
CDM67955.1	1.98e-126	3	522	295	808
CDM67952.1	9.51e-120	3	521	301	815
AGF57034.1	1.71e-105	3	540	301	828

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	1.40e-48	1	269	399	646	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P00691	1.25e-15	8	522	147	640	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
Q05884	3.31e-07	64	215	300	462	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy 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	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003112_00521.