CAZyme Information: MGYG000001661_00892

Basic Information

• Species: Bacteroides gallinarum
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides gallinarum
• CAZyme ID: MGYG000001661_00892
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
786	MGYG000001661_5|CGC2	90115.65	4.3889

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001661	3951783	MAG	United States	North America

• Gene Location: Start: 164642; End: 167002 Strand: +

Full Sequence      

MKKYIIYLLYLLLALPCFTACSDDDKPFLLTREPEEENQDGSVDENFDESKLVDGFNFNP
MQEVAAIPDADKQLDIYFKANEESALYGHTEDCYLHAGIIVDGTWTCVPAAWDENLDKCK
MSLITSNVWKISLTPSIREWFDSGDTPIEELGLLIRSADGTMKGLEEDYFTETSDSKFSG
FTPGEVVEATMPNGLEYGINIIDDSTVALVLYEKDKNGNRKDYAYVMGDFNDWKLANDET
SRMYRDEAAGCWWILLNGLDRTKEYAFQYYLGDKNEEMRIADPYSEKILDSGNDSYIPSS
TYPESMRQYPEKGAGVVSVFKIAKDNFAWKNDDFRIEDKNNLMIYELLLRDFSETGDLNG
AMAKLDYLEDLGVNAIELMPVQEFDGNDSWGYNPCFYFAMDKAYGTQEMYKKFIDECHGR
GIAVILDVVYNHATGSHPFARLYWDSKNNQTADNNPWFNVTAPHPYNVFHDFNHEEPMVR
QFVKRNLEFLLNEYHIDGFRFDLTKGFTQNKSDEGSASNYDASRINILKDYYNTIQSVRQ
DAVMIIEHFCNEDEENVLSAAGILPWCQMNDAYCQSGMGYQERSGFENRRFKEGWVGFME
SHDEERTAFKAKAYGNGAVGQNLKYRMNSMAANAAFCFMQPGSKMLWQFGEMGYDISIED
GGRTGKKPLHWEYLDNPYRKELHDVYTKLLNLRQVKPDLFRSNYIVEKKISEYNWWGGRG
LKIENGSDKIVVIGNFTPQTINNYSEISLDGVHYNYITGEPKPAVVSVPAHGFVIYTSFE
PATLSD

Enzyme Prediction     

No EC number prediction in MGYG000001661_00892.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	352	573	2.2e-48	0.645367412140575

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	2.25e-176	327	703	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	6.85e-51	327	504	23	190	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	9.31e-44	226	738	52	561	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11316	AmyAc_bac2_AmyA	2.54e-34	345	547	4	225	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.
COG1523	PulA	8.44e-32	274	503	100	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADD61516.1	0.0	52	779	136	859
QUU03841.1	0.0	32	779	196	953
AKA52836.1	0.0	32	779	196	953
ADV44995.1	0.0	52	779	134	859
CBW23644.1	0.0	32	779	196	953

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EHA_A	8.12e-32	278	502	50	252	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	8.12e-32	278	502	50	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	8.12e-32	278	502	50	252	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
3VGD_A	2.60e-31	278	502	50	252	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	4.65e-31	278	500	50	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	1.38e-32	276	552	49	291	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q55088	4.49e-31	278	502	51	253	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
Q9AJN6	2.22e-26	327	697	85	505	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter ramosus OX=1672 GN=treZ PE=3 SV=1
Q44316	2.43e-24	327	502	102	267	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q6LHN1	1.99e-23	226	745	139	653	1,4-alpha-glucan branching enzyme GlgB OS=Photobacterium profundum (strain SS9) OX=298386 GN=glgB 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	0.000179	0.999860	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001661_00892.