CAZyme Information: MGYG000002500_02511

Basic Information

• Species: Enterobacter cloacae
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter cloacae
• CAZyme ID: MGYG000002500_02511
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
594	MGYG000002500_2|CGC36	66201.52	5.2382

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002500	5087499	Isolate	not provided	not provided

• Gene Location: Start: 2476998; End: 2478782 Strand: -

Full Sequence      

MEFRTFQKQWGAEFISSDVVRFRVWAEGQQQLTLRLAERDLPMTAVGNGWFQIDVPGVTH
GTEYQFVLQDGMAVPDPASRAQKGDVNGPSVVIDPGRYQPINPDWAGRPWEETVIYELHI
GTFTPQGTFRAAIDKLPYLAELGITQLEVMPVSQFGGSRGWGYDGVLLYAPHSAYGTPED
FHAFIDAAHGLGLSVVLDIVLNHFGPEGNYLPLLSPAFFDAQRMTPWGNGIAYEREPVRH
YILDAPLFWLTEYRLDGLRFDAIDQIKDTASKHILQQIAETIREALPDRHIHLTTEDSRN
VIFLHPRDEKGATPLFTAEWNDDFHNAAHVFATGETHAYYQDFAFEPEKKFARALAEGFV
YQGEVSLQTGHSRGVECHTQPPTFFVDFIQNHDQTGNRAQGERLITLAGADKTRVLLAAL
LLSPHIPLLFMGEEYGETNPFLFFTDFHGDLAKAVREGRAKEFTGHSGHDGDVPDPNDEQ
TFARSKLDWHNVTTAQGKSWLRFTRSLLVLRHRYLVPLLRPGGTVEGKIVKTAPGMVAVS
WSFPTGTLSLALNIGNKPVDVPALAGETLFSWPEAAEVLAPNSIVVRFADGDAS

Enzyme Prediction     

EC	3.2.1.141	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	123	436	7.3e-128	0.9968051118210862

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11325	AmyAc_GTHase	0.0	76	513	1	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
TIGR02402	trehalose_TreZ	0.0	20	562	1	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]
COG0296	GlgB	1.79e-172	1	586	17	625	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11350	AmyAc_4	3.85e-55	102	514	5	383	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.
TIGR02104	pulA_typeI	1.54e-38	22	438	23	487	pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASQ18114.1	0.0	1	594	1	594
QLA64818.1	0.0	1	594	1	594
ADF61501.1	0.0	1	594	1	594
AVL18808.1	0.0	1	594	1	594
QUG52508.1	0.0	1	594	1	594

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	1.01e-316	1	594	25	617	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
2BHU_A	5.34e-125	21	512	37	522	Crystalstructure of Deinococcus radiodurans maltooligosyltrehalose trehalohydrolase [Deinococcus radiodurans]
2BHY_A	6.57e-123	21	512	37	522	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]
1EHA_A	3.96e-122	15	489	6	467	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGG_A	5.59e-122	15	489	6	467	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9RX51	1.76e-125	21	512	37	520	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
Q55088	3.15e-121	15	489	7	468	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
P95867	4.59e-118	15	514	7	490	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q53238	2.93e-112	21	578	16	579	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ PE=3 SV=1
P9WQ23	3.69e-112	22	590	4	578	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
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002500_02511.