CAZyme Information: MGYG000000470_00459

Basic Information

• Species: Brachyspira pilosicoli
• Lineage: Bacteria; Spirochaetota; Brachyspirae; Brachyspirales; Brachyspiraceae; Brachyspira; Brachyspira pilosicoli
• CAZyme ID: MGYG000000470_00459
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
452		53165.02	4.4712

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000470	2694868	MAG	Fiji	Oceania

• Gene Location: Start: 18965; End: 20323 Strand: -

Full Sequence      

MNTSIYNLFPPLLGHISNWYKHIDRIKYMGFEWIYINPITYPGFSGSLYAAKDYYKYNEN
FFSSAEANIAEKELKDFLKYCKKNNIKVMIDLVINHSSKDSVLVDEHFEWYLLDDEGKLK
SPGAWDNGVWIEWGDLASFNNEKPEDGDNPIWSYWKELILHNLSLGFDGFRCDAAYKVNK
DLWIYLIDIAKTKKKDTVFFAESLGCSMEDTLSLIEAGFDYVASSAKWWDYESEWFIEQY
DLAREKSKQIAFPSNHDTLRLINEYNGNIWQVMQRFLFTAIVCDMWMITLGDEYGFYNRC
DVVKGNEFENISYDLSEFIKDIGNYIKNNDILANCGKIVSIDLQEKKLIEELKKKLENSQ
EENNINNDNEEEEKKNPLKRFYKYSLDEKDVVLIVINTSEDKETLEIDKYNIIEDISFNN
RVNNFESGVVEFLPYQLKIFKVVKTISYNLEG

Enzyme Prediction     

No EC number prediction in MGYG000000470_00459.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	20	236	3.5e-44	0.9857142857142858

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11313	AmyAc_arch_bac_AmyA	9.14e-36	21	334	26	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	1.31e-22	5	280	2	238	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.
COG0366	AmyA	1.93e-14	20	294	32	314	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	1.20e-11	22	181	9	180	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.
cd11316	AmyAc_bac2_AmyA	7.39e-11	22	175	28	186	Alpha amylase catalytic domain found in 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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
AFR70162.1	0.0	1	452	1	452
CCG57319.1	3.36e-317	1	452	1	452
ADK30554.1	1.68e-296	29	452	1	424
AGA65413.1	8.87e-292	29	452	1	424
AEM21212.1	1.25e-208	1	440	1	473

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	6.46e-16	2	275	12	303	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]
4GKL_A	1.38e-13	21	184	29	180	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]
6SAV_A	1.38e-10	21	343	45	363	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Rhizomucor pusillus]
6SAV_B	1.84e-10	21	343	45	363	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Rhizomucor pusillus]
1LWH_A	3.61e-06	23	267	29	288	CrystalStructure Of T. Maritima 4-Alpha-Glucanotransferase [Thermotoga maritima],1LWH_B Crystal Structure Of T. Maritima 4-Alpha-Glucanotransferase [Thermotoga maritima],1LWJ_A Crystal Structure Of T. Maritima 4-Alpha- GlucanotransferaseACARBOSE COMPLEX [Thermotoga maritima],1LWJ_B Crystal Structure Of T. Maritima 4-Alpha- GlucanotransferaseACARBOSE COMPLEX [Thermotoga maritima]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q63T93	7.42e-15	4	295	10	298	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Burkholderia pseudomallei (strain K96243) OX=272560 GN=glgE PE=3 SV=2
Q6L2Z8	2.77e-07	4	203	190	395	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828) OX=263820 GN=glgE PE=3 SV=1
P38939	8.16e-07	14	212	450	667	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P38536	8.42e-07	23	332	461	826	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P16950	7.44e-06	23	212	459	668	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu 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
1.000059	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000470_00459.