CAZyme Information: MGYG000001270_01005

Basic Information

• Species: Corynebacterium sp902373425
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium; Corynebacterium sp902373425
• CAZyme ID: MGYG000001270_01005
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
727	MGYG000001270_61|CGC1	79394.22	4.8362

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001270	2256923	MAG	Italy	Europe

• Gene Location: Start: 7401; End: 9584 Strand: -

Full Sequence      

MEHTRPAQSTKKMTSTARYFRLWSPDATAARVHVRRPHGQQESSSPGWRNSSALSSSTPA
ESDDITGDADTVIHPLHRTGEWWISDIPAHPGDRYAFSITTDPAVSDDTESGKDSDAIEW
VGPFPDPCSERQPDGVHGFSEIWEPTYEFTCTQWRGRPLEGSVLYELHVGTFTPEGTFDG
LIAKLPYLKDLGVTTVELMPVAPFGGTRNWGYDGTNWFAVQESYGGPDGLRKLVDKAHQH
GLAVCLDVVYNHFGPDGYYGGAFAPYTSGGSTGWGEVVNLVGDHSDTVRRLIMDAIRRWF
TEFRIDALRLDAVHAFNDPGAHPILEQMNDVARDVTARTGIPRTLIAESDQNDPRIVSPV
AAGGYGLAGQWCDDVHHAIHSAVSGEHHAYYGDFGSPQVLATALTRAFWHDGRYSQFRGR
THGRPIHHATQPASSFVTYTTTHDQTGNRAAGDRPSMNLTPEQQVAKAALVFTSPYTPML
FEGEEWGASTPFPFFASHESDELNELTKEGRKREFARAGWSDDAVPDPSAQSTFDSARLD
WDELTEGSHQAIHDAYRKLIAMREDFPLLRSGNFASISVSWHDDSGNPAAAAHGADVNAS
GALSTPPVVDESPGRGRWIRVDRFSPITNTAVPVADSATASAQVTDENGISAFINLADEP
ADVPLPHGSAINDWNVIFRFGASEGEEASLATQTATTLKPSAEDKSAGNEEETRVMLAPW
ETIIVAR

Enzyme Prediction     

EC	3.2.1.141

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	172	487	7.2e-122	0.9968051118210862

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11325	AmyAc_GTHase	0.0	126	563	1	433	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
TIGR02402	trehalose_TreZ	0.0	20	580	3	511	malto-oligosyltrehalose trehalohydrolase. Members of this family are the trehalose biosynthetic enzyme malto-oligosyltrehalose trehalohydrolase, formally known as 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase (EC 3.2.1.141). It is the TreZ protein of the TreYZ pathway for trehalose biosynthesis, and alternative to the OtsAB system. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
COG0296	GlgB	1.48e-140	19	575	39	560	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11350	AmyAc_4	3.71e-55	147	573	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.
cd11313	AmyAc_arch_bac_AmyA	1.91e-36	159	572	2	336	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRQ66125.1	0.0	13	727	1	715
QRP15098.1	0.0	1	727	1	727
ACR17526.1	0.0	1	727	1	727
QRP11001.1	0.0	1	727	1	727
ALA67617.1	5.65e-222	20	584	4	543

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EHA_A	2.12e-119	118	568	60	489	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	2.12e-119	118	568	60	489	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	5.91e-119	118	568	60	489	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	8.31e-119	118	568	60	489	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	1.65e-118	118	568	60	489	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
P9WQ23	5.92e-164	68	565	17	501	Malto-oligosyltrehalose trehalohydrolase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treZ PE=1 SV=1
P9WQ22	5.92e-164	68	565	17	501	Malto-oligosyltrehalose trehalohydrolase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treZ PE=3 SV=1
Q53238	1.26e-152	123	584	75	538	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ PE=3 SV=1
Q44316	2.12e-151	92	584	35	540	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
O52520	6.03e-142	123	586	68	533	Malto-oligosyltrehalose trehalohydrolase OS=Brevibacterium helvolum OX=1704 GN=treZ PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000043	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001270_01005.