CAZyme Information: MGYG000001918_01837

Basic Information

• Species: Prevotellamassilia sp900541575
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia; Prevotellamassilia sp900541575
• CAZyme ID: MGYG000001918_01837
• CAZy Family: GH13
• CAZyme Description: Neopullulanase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
565	MGYG000001918_59|CGC1	64236.12	6.1323

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001918	2523391	MAG	Denmark	Europe

• Gene Location: Start: 511; End: 2208 Strand: -

Full Sequence      

MKPLIYQIFTRLYGNNQHTANIPNGTIEENGCAKLSDFTQQQLKRIADFGFTHVWYTGLL
EHATQTDYSSHGIRQDHPSVVKGRAGSPYAIKDYYDIDPDLATNVENRMKEFEALLRRTH
KAGLKMVIDFVPNHVARQYHSDKCPRGVHDLGADDQTDQAFSPNNNFYYLLGQTLHTDFD
TAHRAPMPYQEYPAKATGNDCFNAWPSRNDWYETVKLNYGVDYMNGRTTHFSPTPSTWKK
MTDILLFWAKKGVDAFRCDMAEMVPAEFWAYATQHVKERFPQVQFIAEVYNPSEYRRYIA
SGFDYLYDKVGLYDTLRAIVCEGRSASCITGCWQAIDDIRAHMLNFLENHDEQRIASAFF
AGEARKALPALVVSATMGTNPFMVYAGQEVGEPGMDAEGFSGSDGRTTIFDYWSVRSLRL
LTATQPEKEMNEEERSLYQYYKKVITLCKSNAALSDGTFYDLQYANYNHDAGYDCDRQYA
FIRQAPSGETLLIVANFSPTPVHCGVKIPAHAFEYLQLRPGIVSTIDLLSGNLQTIEIKP
NKNAFVEIDGFNAIILQIQNSKTNN

Enzyme Prediction     

No EC number prediction in MGYG000001918_01837.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	30	396	4e-179	0.9973333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	3	454	1	456	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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.
cd11313	AmyAc_arch_bac_AmyA	1.91e-50	5	457	7	336	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.
cd11347	AmyAc_1	9.41e-46	3	391	1	347	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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.
cd11316	AmyAc_bac2_AmyA	1.75e-31	89	457	54	403	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.
COG0366	AmyA	2.24e-24	5	502	3	488	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRO26211.1	4.01e-237	2	559	6	564
QJR54587.1	5.69e-237	2	559	6	564
AII70030.1	5.69e-237	2	559	6	564
QJR73493.1	5.69e-237	2	559	6	564
QJR60612.1	5.69e-237	2	559	6	564

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4GKL_A	2.26e-16	4	356	7	262	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	1.43e-14	82	357	61	284	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]
4AEF_A	4.97e-13	89	512	270	631	TheCrystal Structure Of Thermostable Amylase From The Pyrococcus [Pyrococcus furiosus],4AEF_B The Crystal Structure Of Thermostable Amylase From The Pyrococcus [Pyrococcus furiosus]
7JJT_A	6.72e-12	80	498	82	471	ChainA, Alpha-amylase [Ruminococcus bromii]
1JF5_A	3.01e-11	4	496	132	534	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF5_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20845	8.98e-12	89	506	101	488	Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
Q08751	2.88e-10	4	496	132	534	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
O16098	3.04e-10	4	259	87	280	Maltase 1 OS=Drosophila virilis OX=7244 GN=Mal-B1 PE=3 SV=2
P38940	2.03e-09	80	521	198	561	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
Q64319	2.23e-09	89	317	172	359	Neutral and basic amino acid transport protein rBAT OS=Rattus norvegicus OX=10116 GN=Slc3a1 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
1.000043	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001918_01837.