dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000004516_00273

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Basic Information help

Species

Sneathia amnii

Lineage

Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae; Sneathia; Sneathia amnii

CAZyme ID

MGYG000004516_00273

CAZy Family

GH57

CAZyme Description

1,4-alpha-glucan branching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
524	MGYG000004516_2\|CGC1	62206.78	6.4336

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004516	1228854	MAG	Israel	Asia

Gene Location

Start: 85166; End: 86740 Strand: +

Full Sequence Download help

Enzyme Prediction help

EC	2.4.1.18	3.2.1.1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH57	7	432	7.1e-82	0.8224543080939948

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10792	GH57N_AmyC_like	0.0	3	414	1	412	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	0.0	1	523	1	502	Predicted glycosyl hydrolase, contains GH57 and DUF1957 domains [Carbohydrate transport and metabolism].
cd10816	GH57N_BE_TK1436_like	3.30e-105	3	414	1	423	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	1.11e-68	6	414	1	313	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.
pfam09210	DUF1957	6.29e-43	426	522	1	98	Domain of unknown function (DUF1957). This domain is found in a set of hypothetical bacterial proteins. Its exact function has not, as yet, been defined.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AKC95265.1	0.0	1	524	1	524
AVL43718.1	1.11e-312	1	523	1	523
ACZ00778.1	1.15e-312	1	523	2	524
ALA95152.1	9.86e-306	1	523	1	525
BBM54219.1	4.01e-305	1	523	1	525

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2B5D_X	1.70e-154	1	521	1	522	Crystalstructure of the novel alpha-amylase AmyC from Thermotoga maritima [Thermotoga maritima MSB8]
3N8T_A	1.92e-91	1	517	1	526	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]
5WU7_A	6.23e-91	1	517	1	528	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]
3P0B_A	3.78e-79	5	522	24	535	Thermusthermophilus family GH57 branching enzyme: crystal structure, mechanism of action and products formed [Thermus thermophilus]
1UFA_A	3.68e-77	5	522	4	515	Crystalstructure of TT1467 from Thermus thermophilus HB8 [Thermus thermophilus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q5JDJ7	1.69e-89	1	517	1	526	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	1.25e-78	5	522	4	515	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	2.02e-39	3	485	10	485	Probable 1,4-alpha-glucan branching enzyme MT3115 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3115 PE=3 SV=1
P9WQ27	2.02e-39	3	485	10	485	Probable 1,4-alpha-glucan branching enzyme Rv3031 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv3031 PE=1 SV=1
P09961	8.67e-07	130	226	69	165	Alpha-amylase 1 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyA PE=1 SV=2

SignalP and Lipop Annotations help

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 download full data without filtering help

start	end
455	477