CAZyme Information: MGYG000003194_01034

Basic Information

• Species: Paramuribaculum sp900546365
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp900546365
• CAZyme ID: MGYG000003194_01034
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
929		101778.22	4.8608

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003194	2001061	MAG	United States	North America

• Gene Location: Start: 54750; End: 57539 Strand: +

Full Sequence      

MTHRILTLLVGCWAIAASAQVVTTDPAIVQTDSKGIVITYHADQGNKGLEGLTASTPIYA
HTGVITNLSSSQSDWKYAPSWGDNSSKYKLTYVSANTWTLTIPDINSYYGVAAGETVEQL
TFVFRNADGSREGKTSEGGDIFVKVYPAGFQLVLESSVSGQVVTDNTPVTFTAYTTSAAN
ITISVDGTTIGSATNATKATGQHTFTAMGDYTVTAKATTASGTSTTSSLNMVRVSNSAQQ
NYPGGVPKMGAVSNADGTVTFCICAPGKQSMILMPSWNGYHASAATLMKYQDYNGYRYFW
TTVSGLEKGKDYYYYYLADGERAVGDPYANLILDPYSDKYIDSKVFPNLPSYPVADVPYS
VPLAWYNSNMNSYDWKVTDFKGVDKDQLVIYELLIRDFTGTNGQAYGTGTVQGVIDKLDY
IKGLGVNAVELLPIMEFNGNNSWGYNTNFYFAPDKAYGTPDDYRRLIDECHARGLAVILD
IVFNQSDGLHPWYQLYDIAENPFYNGSAPHAYSVLNDWKQENPVVQQQWHDALRHWLTNY
KVDGFRFDLVKGLGDDSSYGTTYYPATNTYATPSDANTNKYNATRVARMKELHKVISEVN
PNAYFINENLAEAQEENEMAQDGELNWANLNSQALTYAIGTVGGSDLNRFYAPDDSRLRG
STVSYAESHDEERLAYAMTTSNAVSALRSSLQRQMLRLGSVAAQMLMSPGAHMIWQFEEL
GADQSTKNADGGNNTDPKKVVWDYLDNEYRAGLKDTYAELCAIRASAPEMFGNESTVTMN
LTSLNWTTPRTIKLTNGNKEIVLVVNGNYTPASRTLDVPASFDASRYKVLAASHGTAPEM
SSAKKVSLAGNCFVVFGTSDISATDNVVADGITAVTVWADENGNIVVNGDYNTMEVYDLS
GRKVRDTSLTKGVYMVRVDSKVHKVAVTR

Enzyme Prediction     

No EC number prediction in MGYG000003194_01034.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	408	728	1.4e-49	0.9464882943143813

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	3.38e-133	373	774	1	390	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 (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.
cd11325	AmyAc_GTHase	1.23e-54	372	724	22	363	Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase
COG0296	GlgB	1.44e-41	248	557	25	312	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	9.55e-41	389	722	1	259	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.
cd11316	AmyAc_bac2_AmyA	8.87e-38	389	721	2	332	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
QCD35300.1	0.0	16	927	18	926
QIM10833.1	3.84e-303	22	927	10	907
QQR08212.1	3.01e-287	17	836	24	759
ANU64421.1	3.01e-287	17	836	24	759
ASB37479.1	3.01e-287	17	836	24	759

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4J7R_A	2.27e-31	319	550	154	419	CrystalStructure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) [Chlamydomonas reinhardtii],4J7R_B Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) [Chlamydomonas reinhardtii],4OKD_A Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) in complex with maltoheptaose [Chlamydomonas reinhardtii],4OKD_B Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) in complex with maltoheptaose [Chlamydomonas reinhardtii]
3M07_A	5.74e-28	250	558	35	295	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
1EH9_A	2.11e-27	385	557	99	261	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	2.11e-27	385	557	99	261	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
1EHA_A	2.11e-27	385	557	99	261	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q55088	1.16e-26	385	557	100	262	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
O22637	1.86e-26	314	577	155	442	Isoamylase SU1, chloroplastic OS=Zea mays OX=4577 GN=SU1 PE=1 SV=1
B9G434	4.21e-26	329	553	197	450	Isoamylase 3, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA3 PE=2 SV=1
P95867	8.78e-26	373	557	90	264	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q9M0S5	1.22e-25	331	553	184	433	Isoamylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000233	0.999154	0.000171	0.000148	0.000141	0.000131

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003194_01034.