CAZyme Information: MGYG000002484_04165

Basic Information

• Species: Cronobacter malonaticus
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Cronobacter; Cronobacter malonaticus
• CAZyme ID: MGYG000002484_04165
• CAZy Family: CBM48
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
181		19979.58	4.4615

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002484	4470595	Isolate	Czech Republic	Europe

• Gene Location: Start: 555; End: 1100 Strand: -

Full Sequence      

MLLATLLLSPHIPLLFMGEEYGETNPFLFFTDFHGDLAKAVREGRAREFEGHGDWDGDSV
PDPNAQQTFEMSKLDWQKPESEEGRAWLALTRELLTLRREQIVPLLSTAGGHSGRVIDTA
PGFVAVSWTFPKGTLSLALNIGERPQPLPEMPGDTLFAWPQAGDELPANSIQVRLAKGDA
Q

Enzyme Prediction     

EC	3.2.1.141	3.2.1.1

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11325	AmyAc_GTHase	2.65e-38	1	100	339	435	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	1.94e-26	2	149	451	599	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
pfam11941	DUF3459	1.44e-13	90	174	1	92	Domain of unknown function (DUF3459). This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 110 amino acids in length. This domain is found associated with pfam00128, pfam02922.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHB72614.1	1.90e-132	1	181	1	181
ALX80650.1	6.42e-126	2	181	415	594
QWR87126.1	2.07e-124	2	181	415	594
QGG07061.1	2.07e-124	2	181	415	594
ASR82269.1	2.07e-124	2	181	415	594

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	9.47e-76	2	180	440	616	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
2BHY_A	4.30e-24	4	138	427	569	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]
2BHU_A	5.87e-24	4	138	427	569	Crystalstructure of Deinococcus radiodurans maltooligosyltrehalose trehalohydrolase [Deinococcus radiodurans]
1EH9_A	2.47e-14	4	77	402	468	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
1EHA_A	2.47e-14	4	77	402	468	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9RX51	2.35e-23	4	138	425	567	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	5.19e-22	7	175	426	586	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ PE=3 SV=1
O52520	5.32e-20	7	171	419	577	Malto-oligosyltrehalose trehalohydrolase OS=Brevibacterium helvolum OX=1704 GN=treZ PE=3 SV=1
Q44316	5.44e-18	7	145	428	561	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q9AJN6	1.84e-17	4	153	407	547	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter ramosus OX=1672 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
0.807730	0.190528	0.000921	0.000311	0.000184	0.000340

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002484_04165.