CAZyme Information: MGYG000002888_01558

Basic Information

• Species: Corynebacterium kroppenstedtii_A
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium; Corynebacterium kroppenstedtii_A
• CAZyme ID: MGYG000002888_01558
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
371		39857.46	5.1017

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002888	2480296	MAG	United States	North America

• Gene Location: Start: 44; End: 1159 Strand: +

Full Sequence      

MSPVAAGGYGLAGQWCDDVHHAIHSAVSGEHHAYYGDFGSPQVLATALTRAFWHDGRYSQ
FRGRTHGRPIHHATQPASSFVTYTTTHDQTGNRAAGDRPSMNLTPEQQVAKAALVFTSPY
TPMLFEGEEWGASTPFPFFASHESDELNELTKEGRKREFARAGWSDDAVPDPSAQSTFDS
ARLDWDELTEGSHQAIHDAYRKLIAMREDFPLLRSGNFASISVSWHDDSGNPAAAAHGAD
VNASGALSTPPVVDESPGRGRWIRVDRFSPVTNTAVPAGGGNTASAQADGENAISAFINL
ADEPAEVPLPHGSDINDWNVIFRFGASGGKEASSRTDTATAPETSAEDKSAGKDEKTRVT
LAPWETIIVAR

Enzyme Prediction     

No EC number prediction in MGYG000002888_01558.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	3	131	4.8e-41	0.402555910543131

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11325	AmyAc_GTHase	6.63e-87	3	207	234	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
COG0296	GlgB	1.53e-44	3	219	346	560	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11313	AmyAc_arch_bac_AmyA	0.005	81	216	251	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
ACR17526.1	3.70e-256	1	371	357	727
QRP11001.1	3.70e-256	1	371	357	727
QRP15098.1	2.18e-250	1	371	357	727
QRQ66125.1	4.77e-249	1	371	345	715
ALA67617.1	3.58e-93	1	228	316	543

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BHU_A	8.03e-37	11	215	322	529	Crystalstructure of Deinococcus radiodurans maltooligosyltrehalose trehalohydrolase [Deinococcus radiodurans]
2BHY_A	8.03e-37	11	215	322	529	Crystalstructure of Deinococcus radiodurans maltooligosyltrehalose trehalohydrolase in complex with trehalose [Deinococcus radiodurans],2BHZ_A Crystal structure of Deinococcus radiodurans maltooligosyltrehalose trehalohydrolase in complex with maltose [Deinococcus radiodurans R1],2BXY_A Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection [Deinococcus radiodurans],2BXZ_A Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection [Deinococcus radiodurans],2BY0_A Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection [Deinococcus radiodurans],2BY1_A Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection [Deinococcus radiodurans R1],2BY2_A Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection [Deinococcus radiodurans R1],2BY3_A Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection [Deinococcus radiodurans]
1EH9_A	2.66e-36	1	212	292	489	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
1EHA_A	2.66e-36	1	212	292	489	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	2.66e-36	1	212	292	489	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P9WQ22	1.95e-66	7	209	299	501	Malto-oligosyltrehalose trehalohydrolase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treZ PE=3 SV=1
P9WQ23	1.95e-66	7	209	299	501	Malto-oligosyltrehalose trehalohydrolase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treZ PE=1 SV=1
O52520	4.83e-65	3	230	306	533	Malto-oligosyltrehalose trehalohydrolase OS=Brevibacterium helvolum OX=1704 GN=treZ PE=3 SV=1
Q53238	1.14e-63	1	228	311	538	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ PE=3 SV=1
Q44316	1.92e-59	1	228	313	540	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000050	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002888_01558.