CAZyme Information: MGYG000001093_00041

Basic Information

• Species: Flavobacterium lindanitolerans
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Flavobacteriaceae; Flavobacterium; Flavobacterium lindanitolerans
• CAZyme ID: MGYG000001093_00041
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
967	MGYG000001093_8|CGC1	107746.17	5.2718

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001093	3659018	MAG	Sweden	Europe

• Gene Location: Start: 2914; End: 5817 Strand: -

Full Sequence      

MKKITLLFLLIASYAWSQQQTVTYSVTPATFEENQSITLTFNGSSINEATWGVAGNALYI
WAWSFDLNDQNNADCPTNGDWGNSNEANRLTYNSANDTYSISFVPTAFYNRTGIGRIGFL
IKAKNGNGDKKSQDILLRVGTFQVNLTAPAQNSSTMLASGSNFTITANNTGGNASYVLKS
NGSTINTNASTASYSYVHTGITSNQNYSLEVTQGATTITKNFAVVINPGVISAAMPAGMG
DGINYNPSDPTKATLVLNVPNKDFVYVAGSFNNWQPTGAYAMKKDPATGKFWLELSGLTS
GTAYTYQYWVCDQTNLPANSPALVKTADPFSTLVLSPYDDPEIASLGVYPNLPTYPAGQE
REVTVLQTGPNAFYNYNWSAATTNFVKPSKKDLVIYEVLVRDFDANRTYQNLIDRIDYFK
NLKINAIQLMPVMEFEGNESWGYNTVYHLALDKRYGTEAKLKEFIDLCHQNGIAVIFDIA
LNHVYGRSPLERMWMTDTDNDGWANGVTTENPYCNQNAMHSYSVGRDLNHFNEPNNLTGY
YVQRTIQRWMNDFKIDGFRWDLTKGFTQNCPYTGSSSAQESCTNNYQADRVAKLKYYADM
QWAIDPNFYVIFEHLGAGGSYNEEVEWANYRKTGDADGISKGIMQWRKMTDAYANFLKGN
SANLAGVADATDRFIGYAESHDEERVIYKALTESGQTNGNLPKALARMSAMGALHLLVPG
PKMIYHFGDLGYNSSIFTCNNGTVNTPNDATSGDCKLDTKPQPQWANNWLGDVARKKIYD
DWAKMIEFKKRENVFENGTHAWNFSQTGRPRLDIWTSTSQTAELSYVFVLTNATNTVYNA
TAGFPYTGTWYNLMDGTPITVTDANMTIPIEVDGFRVFGNKQALLERNDFNTTAIALYPN
PSKGIFNISKDTKQVSIYSITGQLVKEFKGEFSNEHQYSVENLNQGMYIVKVIDSEDKEA
TLKLMKQ

Enzyme Prediction     

No EC number prediction in MGYG000001093_00041.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	403	731	9.2e-34	0.9331103678929766

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	1.20e-134	376	795	1	386	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.
COG0296	GlgB	1.94e-36	242	561	27	303	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11325	AmyAc_GTHase	2.79e-35	376	724	23	353	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
cd00551	AmyAc_family	1.13e-27	394	730	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.
cd11341	AmyAc_Pullulanase_LD-like	7.99e-22	392	562	2	198	Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. 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
QBZ97475.1	0.0	1	967	1	967
QIH39266.1	0.0	1	967	1	965
QZK89354.1	0.0	1	966	1	961
QKJ61638.1	0.0	1	967	1	963
AOC94343.1	0.0	1	966	1	956

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VGG_A	2.93e-25	369	737	80	426	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	3.90e-25	369	737	80	426	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	6.90e-25	369	737	80	426	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGD_A	2.16e-24	369	737	80	426	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	3.81e-24	369	737	80	426	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
Q55088	3.80e-24	369	737	81	427	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
P95867	9.05e-24	384	683	96	381	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q9RX51	8.97e-16	356	569	97	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
Q2RR72	1.99e-15	257	561	147	414	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
Q21M30	5.89e-15	260	561	143	409	1,4-alpha-glucan branching enzyme GlgB OS=Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) OX=203122 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
0.000457	0.998695	0.000229	0.000215	0.000202	0.000197

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001093_00041.