CAZyme Information: MGYG000000127_03431

Basic Information

• Species: Catenibacillus sp902363555
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Catenibacillus; Catenibacillus sp902363555
• CAZyme ID: MGYG000000127_03431
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
696		77646.79	4.7025

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000127	6637359	Isolate	Canada	North America

• Gene Location: Start: 153012; End: 155102 Strand: +

Full Sequence      

MVTLRNEGITCCFDETSGQLLTVERGSLTIPFGGLAFDFGCNGEMAVGLLAYESMLDFRT
WNLPDIAPTGKPFSLEPEQVQTGEKVVRVSYPMSMGIMQVSYELLDSSVKVDLELTNTSQ
ETLYLNTCGILLSLAQTKGVVFDYPANAPIFHYAVEKLAERKPVQTGLINFATHFALPEG
NLNLLFIDPIEKWGCGTFREQDHTCQVYHAGLEMDLAPGASCAVGSLYIQPCAPETEHEP
DDGNPYLKIRQLVKSLGYAPCTGGITEGVMYSGHPAGTMDKDFPLKDDLYAYAKGLPALK
EMGVDHIWLLPVFDHTEEGVYHSNDQSVIHERYGGEDGCRYFCDLAHDLGMTILFDYVPH
GPVPEYPLVAEHPDWPGKRRDGTLQEEWDCVSMDYNHPGYQEYTSELVHDHVRRFGIDGA
RIDCAMGGLSNWRPYRGNRPSGNSVLAGVHITESIRNGFLRGGEPSFILPENFNPLPNYY
HCTDLFYGMNLYRAFVELEHLLKEKPAQYVAHLTDFLEREAWTTPPDYHKMRFLDNHDTV
SWVWQSARAVDCYGPAAARALFALISLIDGVPMIYQGDEDPSIYGGTGENLVPFFTKLFH
DRRNFIPAKSNQTTYLHTGTPVMAFIREPRETPVPEPCDRYATMGSGRVLVLINLSGEAK
NFDLTGYAAELLTWGGGSEAAKPGVVPAYGYQMYQL

Enzyme Prediction     

No EC number prediction in MGYG000000127_03431.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	280	579	1e-31	0.9364548494983278

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11313	AmyAc_arch_bac_AmyA	2.41e-38	291	611	23	335	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	1.35e-27	269	576	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	3.28e-14	296	579	10	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	1.71e-12	296	579	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	5.98e-11	296	604	35	376	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEE96957.1	7.10e-181	1	696	10	682
QHT61281.1	1.42e-178	9	664	17	649
AZN42601.1	6.02e-173	13	659	24	659
AZI66732.1	3.24e-25	291	600	63	363
AQQ70337.1	3.66e-25	269	658	503	880

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4GKL_A	4.39e-18	294	579	29	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	9.45e-18	296	579	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]
2Z1K_A	1.22e-08	289	590	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]
3VM7_A	1.26e-08	296	622	70	405	ChainA, Alpha-amylase [Malbranchea cinnamomea]
4M8U_A	9.65e-08	267	435	7	210	TheStructure of MalL mutant enzyme V200A from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q1H1K2	2.09e-10	296	455	274	443	1,4-alpha-glucan branching enzyme GlgB OS=Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875) OX=265072 GN=glgB PE=3 SV=1
A8AQY3	3.63e-10	296	423	273	405	1,4-alpha-glucan branching enzyme GlgB OS=Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) OX=290338 GN=glgB PE=3 SV=1
A6VP15	1.16e-09	296	423	273	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
Q0AGJ0	1.44e-09	274	423	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
Q65TI0	3.28e-09	296	423	273	405	1,4-alpha-glucan branching enzyme GlgB OS=Mannheimia succiniciproducens (strain MBEL55E) OX=221988 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
1.000040	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000127_03431.