CAZyme Information: MGYG000000211_01635

Basic Information

• Species: Bacteroides sp900556215
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900556215
• CAZyme ID: MGYG000000211_01635
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
943	MGYG000000211_3|CGC11	104948.67	4.871

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000211	6486320	Isolate	China	Asia

• Gene Location: Start: 564253; End: 567084 Strand: -

Full Sequence      

MKRLYAFFICLLAVLAMQAQIVTTTPDFPTENDEVTIIFDATKGTAGLKGFTGDVYAHTG
VILSTGTSWQYAPTWGDNSAKYKLTSLGNDKWQLKITPNIREYYGVKDGETVKQLAFVFR
SADTSKEGKDTGNKDIFVDVHTAGLTVRFDQPAEKENLITNTALTIKASASVASTLKLYV
GATEIATKANATTISQSYTFSTAGSYTLKAEATANGKTVSATQEVTVLNGTSISEAMPKG
VRPGINYISDTEVTLVLQAPKKKYVYVVGDFNDWTPKSDYQLKQDGEYFWITLSGLIKGE
EYTFQYLVDGSIYIADPYTDKVLDPWNDQYIESTTYPNLKPYPAGKAEGIVSVLQTGQTV
YNWKVKNFERPASEQLVIYEMLVRDFTEEHTFNAAKEKLGYLKNLGVNAIELMPINEFEG
NTSWGYNPSFYFAVDKYYGTKNDLRAFVDECHSQGMAVIIDLVLNHSFGQSPFYLLYKDA
DGKPSADNPWYNQESNIKNPSLSWGYDFNHDSEYTRVLVDSVAGFWMSEYKIDGFRYDFT
KGFSNTPYGVNDWANGPDNARINNLKRMSAAVKERQPGAYVIFEHLAALSEEKQLGDAGI
LLWRNKNEAYCETAMGWSGPKTDFSGLFAGTSSMPAGSLVGYMESHDEERTGFKAWKWGN
TGVIASTTSTNTGMSPATGSNINLSTRTKRLATNAAFFLTVPGPKMIWQFGELGYDFSIN
NNSDGSSYDDQDGYRTDPKPIRWDYFEDADRKGLYETYAALLDFRHSYPELFASNTTFSW
KVGTTNWDNGRTLSATSTDGKSFVVVGNFTLADKNLSVTFPETGTWYEFLKDNEPLSVSG
ATQTIAVPAHEFRLFTNFKPTLTGIETTTPDAEVPLIYYNKAIDTLVLPVGEAKRVEVYS
VNGMLVMTQERCTSVGLSALPVGYYMARVYMEDGKVQVCKIMK

Enzyme Prediction     

No EC number prediction in MGYG000000211_01635.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	386	714	1.6e-46	0.9968051118210862

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	0.0	361	775	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	1.79e-54	361	648	23	318	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	1.48e-51	251	830	36	581	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11313	AmyAc_arch_bac_AmyA	2.77e-36	373	538	2	166	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	7.70e-31	377	713	1	257	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
ALJ58548.1	0.0	1	943	1	942
QUT90345.1	0.0	1	943	1	942
QDO71214.1	0.0	1	943	1	944
QUT75353.1	0.0	1	943	1	937
QIK60226.1	1.81e-289	1	943	1	908

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	1.90e-28	279	538	64	285	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
3VGG_A	2.18e-28	248	538	6	252	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
1EH9_A	2.18e-28	248	538	6	252	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
1EHA_A	2.18e-28	248	538	6	252	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	6.87e-28	248	538	6	252	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P95867	5.14e-29	271	538	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	1.20e-27	248	538	7	253	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
Q2RR72	5.14e-26	257	610	147	501	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
Q9RX51	2.52e-23	337	552	87	283	Malto-oligosyltrehalose trehalohydrolase OS=Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) OX=243230 GN=treZ PE=1 SV=1
Q3SH78	3.08e-23	259	624	155	506	1,4-alpha-glucan branching enzyme GlgB OS=Thiobacillus denitrificans (strain ATCC 25259) OX=292415 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
0.000345	0.998926	0.000212	0.000158	0.000165	0.000164

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000211_01635.