CAZyme Information: MGYG000003293_01536

Basic Information

• Species: CAG-110 sp900544405
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-110; CAG-110 sp900544405
• CAZyme ID: MGYG000003293_01536
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
685		76517.37	4.7264

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003293	2030729	MAG	Mongolia	Asia

• Gene Location: Start: 13496; End: 15553 Strand: -

Full Sequence      

MTLSNDFLTCRFDDAGKLLSVSHGALRLPFDGFAFDLGCQEQSVNGLLEYESMLEFRTWN
LPDIRPTGKRFSRTPKSIAQAKDQITVTYALEQLDVAVSYVLIPTALKIDLRILNTTAEP
LYLNACAFLLSLAQTEGVVFDFPGNAPIYHCESTLLENRKPVQTGLINFATHTSLPGGDM
NLLFLDKIEKWGCGVYRDDDRTTYVYNAGLEIDLKAQESCCVGSLYLTPCIPAEDGNPYL
QIRDLVASLGYAPTTQGIHDGVMYSCHPSGTMDAGFPLKDDLYQYAEYLPKLKSMGIDHV
WLLPVFDHNENGVYHSNDQSVIDQRYGGEEGCKYYCDKAHDLGMTILFDYVPHGPAPEFP
VARDNPEWPSKRRDGSLQDEWECVSMDYNHPGYQEYTAELVHDHVRRFGVDGARIDCAMG
GLSNWRPYRDNRPSGNSVLAGVHITEAIRNGFLRGGKPSFILPENFNLIPNYYHCTDLFY
GMNLYRAFVELESLLKTDPAQYAALLTDFLERESWITPADYHKMRFLGNHDTVSWVWQSK
RAVDCYGVGGAKALFALISLIDGVPMIYQGDEGPTIYGGTTENLTDFFTRLFADRKHFLP
RGSNLTTYLHTGTPVMAFFREPQEVPAADYQTEGSGRVLVLINLSDTPQPVPAQAQSCSV
LADSAGAAQADTDLAPFAYRLLQVV

Enzyme Prediction     

No EC number prediction in MGYG000003293_01536.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	276	572	5.4e-31	0.9264214046822743

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11313	AmyAc_arch_bac_AmyA	1.32e-34	289	596	28	328	Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. 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.
cd00551	AmyAc_family	1.19e-25	262	569	1	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.
pfam00128	Alpha-amylase	3.12e-18	281	572	2	325	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
cd11338	AmyAc_CMD	2.13e-15	289	572	62	341	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.
COG0366	AmyA	1.80e-13	289	603	35	385	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEE96957.1	4.68e-187	1	645	11	642
AZN42601.1	1.65e-175	34	646	47	657
QHT61281.1	1.59e-174	8	624	17	631
AWI27297.1	7.31e-25	285	651	63	416
CCH01189.1	1.63e-23	276	651	69	436

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4GKL_A	1.01e-17	289	572	31	291	Crystalstructure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana],4GKL_B Crystal structure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana]
3DHU_A	8.90e-16	289	572	36	313	Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum]
2WC7_A	3.73e-12	281	572	54	359	Crystalstructure of Nostoc Punctiforme Debranching Enzyme(NPDE)(Acarbose soaked) [Nostoc punctiforme],2WCS_A Crystal Structure of Debranching enzyme from Nostoc punctiforme (NPDE) [Nostoc punctiforme],2WKG_A Chain A, Alpha Amylase, Catalytic Region [Nostoc punctiforme PCC 73102]
5OT1_A	2.21e-11	281	620	350	709	ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis]
2Z1K_A	9.68e-10	282	583	49	362	CrystalStructure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_B Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_C Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_D Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q0AGJ0	1.30e-11	267	416	267	415	1,4-alpha-glucan branching enzyme GlgB OS=Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57) OX=335283 GN=glgB PE=3 SV=1
P29964	1.72e-10	281	572	170	457	Cyclomaltodextrinase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=Teth39_0676 PE=1 SV=2
Q8GQC5	3.20e-09	287	454	275	444	1,4-alpha-glucan branching enzyme GlgB OS=Dickeya chrysanthemi OX=556 GN=glgB PE=1 SV=1
A6VP15	5.89e-09	287	416	271	405	1,4-alpha-glucan branching enzyme GlgB OS=Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z) OX=339671 GN=glgB PE=3 SV=1
Q3SH78	7.36e-09	286	448	284	456	1,4-alpha-glucan branching enzyme GlgB OS=Thiobacillus denitrificans (strain ATCC 25259) OX=292415 GN=glgB 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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003293_01536.