CAZyme Information: MGYG000000305_00040

Basic Information

• Species: RF16 sp900542355
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae; RF16; RF16 sp900542355
• CAZyme ID: MGYG000000305_00040
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
895		99518	4.8781

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000305	2446714	MAG	Sweden	Europe

• Gene Location: Start: 48492; End: 51179 Strand: -

Full Sequence      

MRKTFFRTSLRFACLNLFLLGVALLQAQVSTIPAIIQKGYKGEITIIFNPNKGNQGMAKA
TACYAHIGLITSESKTASDWKYATDWQKTDPAMTLVDGKWQLLITPDIYTYYGCPETEEI
QKMVFVFNDGKSGGAEGKTAEGGDIFVDLAEAGLAASIQTDLPEIASVGTAVSLRCHASQ
TAELSLSLNGKEVQSATGTEMTYTATLPAEGNYAFQLVAKTATEEAVAEAFTCVPAAPRK
ADRPAGVLNGIYYDAADPTKVTLCTYAASKTEPAQHVFVVGDFNDWTISNDYQLAQATDS
AYFWITLSDLTPKQEYAMQYVVVRADGVVKYISDLYSEKLLHPDDQYEPRKIDPTLMDYP
AKGRDYVTVIQTAKEPFAWSDATLRFQRPDKNNLIIYELWVYDHTPFRNIEGLMERLDYL
HNLGVNAVELMPVNEFDGNQNWGYSPNHYFALDKAYGTPEQLKTFIDECHKRGIAVILDM
VFNHATGLNPMNKLYPYGTDLKNNPWFNVSAPHPDNVYEDWNHDFAPAHSMFTRALQYWL
TEYKIDGYRLDLSHGICGPKYNAVDNLKDYYAKGVQAVSEDAYMILEHWGSSMASDRPQL
IKAGMLCWQNTCNAFEQTAMGWLKDGDSFAEANQDGYVSYPESHDEERAFFKAKQWGDGD
MKTDEAVRVGRVPLNMAFATLLNGSHMFYHFAELGYDNSKFQNAAGQWGTDGKDAYGITA
QVQEEVKMQAKMRPESAGWFREGSVRMAAYQKTAQAIQLRTRLLPEVFEGNPTAVQVGSG
KAVRTIQWGNDVFVVGNFSASAAQTATLPSGTWYDYYAGGTASGTITLQPGELKIYTGTP
QALPEVPAYYDFAEGIGQTITDNGVTTPAHKVLIDGVVYIVRNGVWYDLMGRKVK

Enzyme Prediction     

No EC number prediction in MGYG000000305_00040.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	410	598	6.4e-47	0.5750798722044729

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	5.77e-117	379	706	1	349	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	2.14e-50	377	589	23	225	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	3.26e-42	273	556	46	308	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.21e-37	395	694	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.
COG1523	PulA	9.74e-33	246	552	31	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADQ81138.1	4.33e-164	15	868	41	889
QUT75353.1	2.00e-135	29	889	23	892
AEW21359.1	1.53e-134	11	703	3	620
BAR52001.1	1.53e-134	11	703	3	620
QDO71214.1	3.71e-133	19	815	11	829

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EH9_A	2.46e-33	299	561	39	264	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	2.46e-33	299	561	39	264	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	2.46e-33	299	561	39	264	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	7.89e-33	299	561	39	264	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	1.41e-32	299	561	39	264	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	1.36e-32	299	561	40	265	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
P95867	4.62e-30	299	561	40	267	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q44316	4.56e-27	365	580	88	294	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q9AJN6	5.01e-25	377	556	85	255	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter ramosus OX=1672 GN=treZ PE=3 SV=1
Q53238	2.34e-24	379	556	102	270	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ 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
0.000943	0.998238	0.000211	0.000211	0.000179	0.000175

TMHMM  Annotations     

start	end
13	35