CAZyme Information: MGYG000001537_03530

Basic Information

• Species: Cellulomonas timonensis
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Cellulomonadaceae; Cellulomonas; Cellulomonas timonensis
• CAZyme ID: MGYG000001537_03530
• CAZy Family: GH13
• CAZyme Description: Malto-oligosyltrehalose trehalohydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
597	MGYG000001537_13|CGC9	65213.88	5.2455

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001537	4057828	Isolate	not provided	not provided

• Gene Location: Start: 873728; End: 875521 Strand: +

Full Sequence      

MRPRVWAPRAREVALDLPREGRRVPLRQAGDGWWEADLDLAPGVRHAYAVDGAPPHADPR
AERLPEGVHGPAEAFDATAFAWTDTGWLGLDARGAILYELHVGTFTERGTLDAAIEHLDD
LVALGVDMVELMPLASFNGEHGWGYDGVSLYSVHEPYGGPRALQRFVDAAHAHGMGVCLD
VVHNHLGPSGNYLGAFGPYLTDAHHTPWGAAVNLDQDGSHEVRRWICDSALRWLRDFHVD
ALRLDAVHALVDDSPQHLLAQLSVEVADLAAELGRPLSLIAESDLNDPVAILPVAQGGWG
MTAQWADDVHHAIHALVTGERHGYYVDFGSPQTLRKALTQVFVHDGGWSAFRGRHWGRPL
PPGTDGHQFVVSASNHDQVGNRALGDRPSARLDPGALAVEAALVLLSPFTPMLFMGEEWG
ARTPWLYFTDHPEPELADAVRSGRRGEFGGHGWEELYGGVVEPPDPQARSTFEASRLDRG
ELRDAGHARLLDWHRQLIALRRAEPELSAGDLTATRVRFEDAPADQASSGWQGWLVVERG
GARVVVNLAEEERRVPLQSSRPLEVRAAWSPVRVEPPAADDESGHVVLPGRSVVVLA

Enzyme Prediction     

EC	3.2.1.141

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	105	420	8.2e-129	0.9968051118210862

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02402	trehalose_TreZ	0.0	2	556	2	544	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	0.0	58	504	1	436	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	1.08e-132	4	579	41	622	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11350	AmyAc_4	8.10e-41	80	511	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.
cd00551	AmyAc_family	3.34e-27	96	414	1	252	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QVI64512.1	1.12e-306	1	597	1	592
QVI64192.1	1.89e-299	1	596	1	596
QCB93755.1	8.54e-298	3	597	5	615
QGQ19482.1	3.46e-297	3	597	5	615
QWC17591.1	1.52e-296	3	597	5	598

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EHA_A	2.82e-126	5	477	15	465	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	2.82e-126	5	477	15	465	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	7.93e-126	5	477	15	465	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	1.12e-125	5	477	15	465	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	2.23e-125	5	477	15	465	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
Q9AJN6	2.47e-195	5	579	7	569	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter ramosus OX=1672 GN=treZ PE=3 SV=1
Q53238	8.08e-181	5	562	19	565	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ PE=3 SV=1
Q44316	4.91e-180	5	551	21	560	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
P9WQ22	2.48e-178	4	572	5	558	Malto-oligosyltrehalose trehalohydrolase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treZ PE=3 SV=1
P9WQ23	2.48e-178	4	572	5	558	Malto-oligosyltrehalose trehalohydrolase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treZ PE=1 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
1.000048	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001537_03530.