CAZyme Information: MGYG000002885_02097

Basic Information

• Species: Pseudomonas_E juntendi
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E juntendi
• CAZyme ID: MGYG000002885_02097
• CAZy Family: GH13
• CAZyme Description: Malto-oligosyltrehalose trehalohydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
373		42040.03	5.3135

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002885	3148284	MAG	United States	North America

• Gene Location: Start: 2812; End: 3933 Strand: +

Full Sequence      

MHRHGAHLLDATSARFALWAPDARSVSVELEQQPAIALQPDEDGWFSGVAPCRAGDRYHF
RIDDELQVADPASRYQPTGVHGPSQVVDVASYPWQHPWLGRPWHEAVIQELHVGLLDGYQ
GVTRQLPKLAALGISAIELMPLGQFPGERNWGYDGVLPYAPQHTYGSPEQLCALVDQAHG
EKLMVLVDVVYNHFGPDGNYLHQYASPFFREDRQTPWGAAIDFRRPQVREYFIQNALMWL
CDYRCDGLRLDAVHAIDQPDFLVELAERVRAAVEPGRHVWLVLENEHNQATLLQQGFDAQ
WNDDGHNALHVLLTGETEGYYADYKDRPIDQLARCLAEGFVFQGQANRHGTPRGEPSAHL
PPSAFVLFLQNHA

Enzyme Prediction     

EC	3.2.1.141

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	118	372	7.8e-114	0.8402555910543131

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02402	trehalose_TreZ	0.0	15	372	2	374	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]
cd11325	AmyAc_GTHase	2.79e-155	70	372	1	316	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	7.50e-119	2	372	24	423	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd02853	E_set_MTHase_like_N	1.87e-35	5	87	1	84	N-terminal Early set domain associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (also called Glycosyltrehalose trehalohydrolase) and similar proteins. E or "early" set domains are associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (MTHase) and similar proteins at the N-terminal end. This subfamily also includes bacterial alpha amylases and 1,4-alpha-glucan branching enzymes which are highly similar to MTHase. Maltooligosyl trehalose synthase (MTSase) and MTHase work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The N-terminal domain of MTHase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.
PRK12313	PRK12313	7.95e-35	2	253	25	311	1,4-alpha-glucan branching protein GlgB.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEQ88863.1	2.03e-289	1	372	1	372
QOH69050.1	2.89e-289	1	372	1	372
QDR69141.1	2.89e-289	1	372	1	372
QKL02808.1	2.75e-287	1	372	1	372
AHD15355.1	6.20e-270	1	372	1	372

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	1.47e-105	5	372	35	416	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
1EH9_A	4.13e-86	6	372	3	376	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
1EHA_A	4.13e-86	6	372	3	376	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGG_A	1.15e-85	6	372	3	376	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	1.62e-85	6	372	3	376	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q55088	2.32e-85	6	372	4	377	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
P95867	2.28e-78	9	372	7	379	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q44316	1.14e-76	14	372	17	399	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q9RX51	1.80e-75	8	372	30	399	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
Q53238	6.85e-74	13	372	14	397	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000031	0.000026	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002885_02097.