CAZyme Information: MGYG000000029_03008

Basic Information

• Species: Bacteroides finegoldii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides finegoldii
• CAZyme ID: MGYG000000029_03008
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
809	MGYG000000029_19|CGC2	92961.4	4.4807

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000029	4415875	Isolate	United Kingdom	Europe

• Gene Location: Start: 9102; End: 11531 Strand: -

Full Sequence      

MKKYLIYILLLLFTAPYISSCSDEWTDSDKLSLLTKAEEEEPIVEDDIDINLLKFGFNLN
PKAETNELPNADEALDIYFYAEGKELAEGEKECPLLGYQEACYLHAGVYSEGTWMYVPAA
WTEDTEKCKMVRVKENVWKITLSPTIRDWFGSGSTPIEQLGLIIRTTDGKKGIEEDTFVD
IEDDKYNSFTPGEIKLESMPSGLQHGINIIDNHTVALVLYEKDKDGNRYYDYAYVMGDFN
NWKRSNDENSQMYYDESAGCWWITLSGLEPTKEYAFQYYLGKKSSVEGEKDTELRIADPY
TEKILDASSDSYIPESTYPSSQRIYPTKGAGVVSTFKIQKDSYSWAHDNFKIADKNNLMI
YELLLRDFTETGDLQGAIQKLDYLERLGITAIELMPVQEFEGNDSWGYNPTFYFALDKAY
GTSEMYKRFIDECHKRGIAVLFDVVYNHATGSNTFARLYWDSKNNRTAENNPWFNVEARH
AFNVFHDFNHESPLVRDFVKRNLKYLINEYHIDGFRFDLTKGFTQNGNKDTDVSGYDESR
ISILRDYYNAIQSVSPEAVMICEHWTDWAEENVLALAGIQCWRKGSNTHDEGYYQSGMGY
SERSSFSNLIQSGGNSIHFGGWVGFMESHDEERVAYKAQVYGNEKIKTDLTTRMNQLAAN
AAFCFTVPGPKMIWQFGELGYDETLGEEDEKTAKKPLHWEYYDEPARKSLYDVYAKLLDL
RKTHANLFGQNATFSWKVETADWTGNTPRTISLKYNDKELVVVGNFGDDTTNYSLDSNIK
YNYMTGDEVSGNITVEPHNFFLGTSFRPE

Enzyme Prediction     

No EC number prediction in MGYG000000029_03008.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	368	680	2.5e-50	0.9968051118210862

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	5.06e-176	343	731	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	6.08e-58	341	724	21	436	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	5.19e-53	235	767	52	559	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	6.29e-36	248	537	57	385	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	2.15e-35	360	679	2	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
BAD50048.1	1.18e-299	67	766	228	905
QRP89046.1	1.68e-299	67	766	228	905
CUA19595.1	4.76e-299	67	766	228	905
AKA52836.1	4.76e-299	67	766	228	905
QUU03841.1	4.76e-299	67	766	228	905

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VGG_A	3.63e-32	294	529	50	263	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	3.63e-32	294	529	50	263	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
1EHA_A	3.63e-32	294	529	50	263	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	1.16e-31	294	529	50	263	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	2.08e-31	294	529	50	263	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	4.61e-33	294	529	51	266	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q55088	2.01e-31	294	529	51	264	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
Q9AJN6	5.65e-27	343	518	85	250	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter ramosus OX=1672 GN=treZ PE=3 SV=1
Q8CZE8	1.83e-25	235	728	51	518	1,4-alpha-glucan branching enzyme GlgB OS=Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831) OX=221109 GN=glgB PE=3 SV=1
Q44316	2.66e-25	342	557	101	294	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000060	1.000019	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000029_03008.