CAZyme Information: MGYG000002291_00137

Basic Information

• Species: OM05-12 sp003438995
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OM05-12; OM05-12 sp003438995
• CAZyme ID: MGYG000002291_00137
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
915		101707.13	4.917

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002291	4475595	Isolate	China	Asia

• Gene Location: Start: 181260; End: 184007 Strand: -

Full Sequence      

MKKGFIYILSFLFCLSSHAQILTTEPDFVTESGSIKVVFDASQGSKGLMNYNGDVYAHTG
VITGSNDSRWEYASTWGVNSDKYKMASLGNNKWELTLSPDIRTYYGVPAGTPIKKLVFVF
RSGAKSGNDYLTGKETGDKDIYLSVYESGLNVKLDSPAKDMVVEKGTSLTLTASSSVAAD
LQLSVNETVVATKNRATDISASYVFSSPGTYTVKATATLDGAIGSATRLVSILEPSVSAP
LPDGVRPGINYVSPTEVTLVLQAPGKTSVYAIGDFNAWNPLPDYQLKKDGEYFWITLQGL
TPKQEYAFQYLVDGAIRIADPYTDKVLDPWNDGDITATTYPGLMAYPTGKTEGIVSVLQT
DQTPYTWKSVGFDKPAKEKLIIYELLLRDFTEEHTFSSAREKISYLKGLGVNAVELMPVN
EFEGNSSWGYNPSFYFAPDKYYGTKDDMKAFVDECHRNGIAVIMDLVLNHSYGQSPFYLL
YRDADGTPSADNPWYNRQSNIANPSLSWGYDFNHDSPYTRALVDSVAAYWMNEYRVDGFR
YDFTKGFSNTIYSNANDYASAYDASRIANLKRMASEVWKRNPDAYVICEHLADNTEEKEL
SSAGLMLWGNMNNNACEGAMGFTENSKSDISGAVYKKRTWSAPNLVGYMESHDEERMAYK
LKTYGNAAGGYDTKDHTTSMNRLKMSGCLFFLIPGPKMIWQFGELGYDYSIDYNDRVGEK
PVCWNYLEDADRKSVYNTWAQLFAMKTQYPVFSTSDITYKLSDACKYLVLKSSDMNAVIV
ANYGVTQGNVAVTFPATGTWYNYFSKTTEQITSASNTITLAPGEYRLYTDKEMIISTSLS
EFPESSVSVYPNPVSDILNVSGEDVSRISVYSLHGVLLKEVRDSNAVSVQELAKGVYLVR
IRTGSSEIITKFVKQ

Enzyme Prediction     

No EC number prediction in MGYG000002291_00137.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	390	615	7.1e-45	0.645367412140575

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	0.0	365	756	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	3.17e-57	360	704	18	361	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	1.60e-52	255	589	36	356	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	6.08e-37	236	542	23	359	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11322	AmyAc_Glg_BE	2.31e-35	373	589	29	250	Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1,4-alpha-glucan branching enzyme). The glycogen branching enzyme catalyzes the third step of glycogen biosynthesis by the cleavage of an alpha-(1,4)-glucosidic linkage and the formation a new alpha-(1,6)-branch by subsequent transfer of cleaved oligosaccharide. They are part of a group called branching enzymes which catalyze the formation of alpha-1,6 branch points in either glycogen or starch. This group includes proteins from bacteria, eukaryotes, and archaea. 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
ALJ58548.1	0.0	1	900	1	927
QUT90345.1	0.0	1	900	1	927
QDO71214.1	0.0	1	901	1	930
QUT75353.1	0.0	1	908	1	930
QIK60226.1	0.0	1	915	1	909

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	1.89e-31	283	542	64	285	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
1EHA_A	2.75e-28	284	542	33	252	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	2.75e-28	284	542	33	252	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	2.75e-28	284	542	33	252	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
3VGE_A	8.67e-28	284	540	33	250	Crystalstructure of glycosyltrehalose trehalohydrolase (D252S) [Saccharolobus solfataricus],3VGF_A Crystal structure of glycosyltrehalose trehalohydrolase (D252S) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P95867	8.67e-28	275	542	14	255	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q55088	1.52e-27	284	542	34	253	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
Q7MG90	1.94e-26	257	589	127	449	1,4-alpha-glucan branching enzyme GlgB OS=Vibrio vulnificus (strain YJ016) OX=196600 GN=glgB PE=3 SV=2
Q2RR72	4.83e-26	223	589	118	467	1,4-alpha-glucan branching enzyme GlgB OS=Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1) OX=269796 GN=glgB PE=3 SV=1
Q5DZB8	1.37e-25	257	589	127	449	1,4-alpha-glucan branching enzyme GlgB OS=Aliivibrio fischeri (strain ATCC 700601 / ES114) OX=312309 GN=glgB 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
0.000363	0.998641	0.000474	0.000179	0.000165	0.000160

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002291_00137.