CAZyme Information: MGYG000003498_01455

Basic Information

• Species: UBA7173 sp900768685
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp900768685
• CAZyme ID: MGYG000003498_01455
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
917	MGYG000003498_35|CGC1	100891.98	5.2269

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003498	2015725	MAG	Fiji	Oceania

• Gene Location: Start: 6817; End: 9570 Strand: +

Full Sequence      

MRKLITLFMMAMLFASFSNAQVITSSPAILQEESQNVVLTFHADQCGVTALQNLPSSTAL
YVHTGVVTDKSNGGWKYVVTDWGTNNSANKLTYVSKNTYTFNVGNIRTFYGVPSGEKILK
LCFIARTAAGDVQTKDLFVEVQESGFQLALNSDATSYVISGTTTINFTVNTSQSANITLS
VDGTQVASASNAMELKKAYTFSNRGYYKVEATATKGTTTLTKSVTVAYPNPSPQANYPGG
VPKMGAVKNADGTVTFCLAAPNKSSVILIPSWDNYETLDKNVMSYQDYKGYRYFWTTVSG
LDNTTAYPYYYLVDGVTKVGDPYAHLVLDPYNDKWMPSDVYPDKPVYPYDKFDDVMLAVY
QGNLDDYKFSKFTIPDHKNLIIYEMLLRDFTGENNADGTGSGTGTLALAMERLDHIFKMG
VNCIELMPIMEFNGNNSWGYNTNFYMAPDKIYGSPKEFKDFVETCHKHGVAVVLDIVFNQ
SDGLHPWYQMYPIASNPFYNENAPHAYSVLNDWNQDNPLVQQQWVDAITYWMTAYNVDGF
RFDLVKGLGDNNSYGSGTDSYNRSRVARMKKLHAAIKAVKPNGIHINENLAGDQEENEMA
ADGQLNWSNINGDCGNYAKVASTGNSSTMSGFFSPYWNRTQFSTVSYAESHDEERIGYTG
STHATLKNKVDFLTRRLGSIAATMLMTPGPKMIWQFAEVGADQSTKNSSGNDTSPKRVLW
DYLDNTYRAALYQNYCELVGIRTCNFDLFSNANLDSRETTYYVRSGFADNMTSARNIVLH
YGSQEIAVLINPALSGNKNITANVSLISSSNSIVLSKSQGVTTTPTYGSGTVTMAVPANS
YVVIGTTNIAGVEDVIADEVGGSKVTVAGGDGEIVINGEYDNCSVYTLSGQRLSSLNVPA
GLYIVKVDGETFKVVVR

Enzyme Prediction     

No EC number prediction in MGYG000003498_01455.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	404	707	2.1e-44	0.9431438127090301

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	1.93e-114	372	751	8	389	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	1.26e-43	375	703	33	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	7.12e-39	243	701	25	472	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	8.22e-35	321	544	108	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.52e-33	381	701	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCD35300.1	2.68e-273	18	917	19	927
QIM10833.1	1.04e-248	23	917	10	908
QQR08212.1	1.43e-205	18	800	24	738
ANU64421.1	1.43e-205	18	800	24	738
ASB37479.1	1.43e-205	18	800	24	738

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	5.98e-23	381	553	138	295	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
1EH9_A	1.85e-22	246	550	3	259	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	1.85e-22	246	550	3	259	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	1.85e-22	246	550	3	259	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
4J7R_A	4.00e-22	378	545	222	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O22637	3.83e-25	348	545	211	419	Isoamylase SU1, chloroplastic OS=Zea mays OX=4577 GN=SU1 PE=1 SV=1
Q9M0S5	1.10e-24	365	548	224	433	Isoamylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA3 PE=1 SV=2
B9G434	2.41e-23	365	548	239	450	Isoamylase 3, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA3 PE=2 SV=1
D0TZF0	5.74e-23	378	545	243	434	Isoamylase 1, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA1 PE=1 SV=1
Q9AJN6	2.69e-22	376	550	96	257	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter ramosus OX=1672 GN=treZ PE=3 SV=1

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
0.000247	0.999063	0.000200	0.000168	0.000151	0.000140

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003498_01455.