CAZyme Information: MGYG000000365_00443

Basic Information

• Species: CAG-269 sp900556695
• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-269; CAG-269 sp900556695
• CAZyme ID: MGYG000000365_00443
• CAZy Family: GH57
• CAZyme Description: 1,4-alpha-glucan branching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
263		30695.41	7.4994

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000365	1394461	MAG	Sweden	Europe

• Gene Location: Start: 167325; End: 168116 Strand: +

Full Sequence      

MQQKKGYVSFVLHAHLPFIHHPESDDYLEESWLYEAISETYIPLLINFQKLVDEGVNFRI
TMSMTPPLLSMLDNKLLQRKYIKYLKKMIELSKKEIKRTAGDERLNKLSHYYFDRYSNDL
HIFKDVYNCNIIQGFKHFQDIGVLEIITCGATHGYFPILYVNEKTVKAQIAVGVQTYEKY
FGRKPRGIWLPECGYVPEADKYLKEFGIDYIITESHGILYADPTPIYGTFAPIVSPEGVI
AFGRDIESSRQVWSSINRISWRL

Enzyme Prediction     

EC	2.4.1.18	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH57	10	255	5.6e-56	0.5221932114882507

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10792	GH57N_AmyC_like	1.14e-150	6	255	1	250	N-terminal catalytic domain of alpha-amylase ( AmyC ) and similar proteins. Alpha-amylases (alpha-1,4-glucan-4-glucanohydrolases, EC 3.2.1.1) play essential roles in alpha-glucan metabolism by catalyzing the hydrolysis of polysaccharides such as amylose starch, and beta-limit dextrin. This subfamily is represented by a novel alpha-amylase (AmyC) encoded by hyperthermophilic organism Thermotoga maritime ORF tm1438, and its prokaryotic homologs. AmyC functions as a homotetramer and shows thermostable amylolytic activity. It is strongly inhibited by acarbose. AmyC is composed of a N-terminal catalytic domain, containing a distorted TIM-barrel structure with a characteristic (beta/alpha)7 fold motif, and two additional less conserved domains. There are other two canonical alpha-amylases encoded from T. maritime that lack the sequence similarity to AmyC, and belong to a different superfamily.
COG1543	COG1543	8.69e-106	4	255	1	248	Predicted glycosyl hydrolase, contains GH57 and DUF1957 domains [Carbohydrate transport and metabolism].
cd10816	GH57N_BE_TK1436_like	1.34e-67	6	255	1	277	N-terminal catalytic domain of Gh57 branching enzyme TK 1436 and similar proteins. The subfamily is represented by a novel branching-enzyme TK1436 of hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. Branching enzymes (BEs, EC 2.4.1.18) play a key role in synthesis of alpha-glucans and they generally are classified into glycoside hydrolase family 13 (GH13). However, TK1436 belongs to the GH57 family. It functions as a monomer and possesses BE activity. TK1436 is composed of a distorted N-terminal (beta/alpha)7-barrel domain and a C-terminal five alpha-helical domain, both of which participate in the formation of the active-site cleft.
cd01022	GH57N_like	4.90e-52	9	254	1	204	N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57. Glycoside hydrolase family 57(GH57) is a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation.
cd10785	GH38-57_N_LamB_YdjC_SF	3.51e-33	10	242	2	179	Catalytic domain of glycoside hydrolase (GH) families 38 and 57, lactam utilization protein LamB/YcsF family proteins, YdjC-family proteins, and similar proteins. The superfamily possesses strong sequence similarities across a wide range of all three kingdoms of life. It mainly includes four families, glycoside hydrolases family 38 (GH38), heat stable retaining glycoside hydrolases family 57 (GH57), lactam utilization protein LamB/YcsF family, and YdjC-family. The GH38 family corresponds to class II alpha-mannosidases (alphaMII, EC 3.2.1.24), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides by employing a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. GH57 is a purely prokaryotic family with the majority of thermostable enzymes from extremophiles (many of them are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57 cleaves alpha-glycosidic bond by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation. Although the exact molecular function of LamB/YcsF family and YdjC-family remains unclear, they show high sequence and structure homology to the members of GH38 and GH57. Their catalytic domains adopt a similar parallel 7-stranded beta/alpha barrel, which is remotely related to catalytic NodB homology domain of the carbohydrate esterase 4 superfamily.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGB41093.1	2.29e-103	1	255	1	255
CAJ71922.1	2.85e-96	4	255	2	253
QII13593.1	2.85e-96	4	255	2	253
QTA37720.1	1.09e-94	5	255	3	254
ADG81752.1	1.25e-94	5	254	3	252

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2B5D_X	3.04e-81	5	255	2	248	Crystalstructure of the novel alpha-amylase AmyC from Thermotoga maritima [Thermotoga maritima MSB8]
5WU7_A	1.90e-52	5	255	2	274	Crystalstructure of GH57-type branching enzyme from hyperthermophilic archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],5WU7_B Crystal structure of GH57-type branching enzyme from hyperthermophilic archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]
3N8T_A	1.87e-49	5	255	2	272	ChainA, alpha-amylase, GH57 family [Thermococcus kodakarensis],3N92_A Chain A, alpha-amylase, GH57 family [Thermococcus kodakarensis],3N98_A Chain A, alpha-amylase, GH57 family [Thermococcus kodakarensis]
3P0B_A	2.97e-29	9	255	25	296	Thermusthermophilus family GH57 branching enzyme: crystal structure, mechanism of action and products formed [Thermus thermophilus]
1UFA_A	4.94e-29	9	255	5	276	Crystalstructure of TT1467 from Thermus thermophilus HB8 [Thermus thermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q5JDJ7	4.15e-48	5	255	2	272	1,4-alpha-glucan branching enzyme TK1436 OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1436 PE=1 SV=1
Q5SH28	1.44e-28	9	255	5	276	1,4-alpha-glucan branching enzyme TTHA1902 OS=Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) OX=300852 GN=TTHA1902 PE=1 SV=1
P9WQ26	3.82e-11	6	254	10	261	Probable 1,4-alpha-glucan branching enzyme MT3115 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3115 PE=3 SV=1
P9WQ27	3.82e-11	6	254	10	261	Probable 1,4-alpha-glucan branching enzyme Rv3031 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv3031 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
1.000060	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000365_00443.