CAZyme Information: MGYG000003883_00585

Basic Information

• Species: Kosakonia cowanii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Kosakonia; Kosakonia cowanii
• CAZyme ID: MGYG000003883_00585
• CAZy Family: GH13
• CAZyme Description: Malto-oligosyltrehalose trehalohydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
595	MGYG000003883_16|CGC1	66204.76	4.5506

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003883	4218591	MAG	United States	North America

• Gene Location: Start: 3536; End: 5323 Strand: +

Full Sequence      

MATKTFSKTWGAERLADGAVRFRLWATGQQSVTLRLDGQEKPMTRSEEGWFETTVSRVNA
GAQYQFVLADSMAIPDPASRGQLAEVNGPSLVVDPESYQWQHADWQGRPWEEAVVYELHI
GTFTPQGTFQAAIEKLSYLAELGVTMVEVMPVSQFGGTRGWGYDGVLLYAPHSAYGTPDD
FKAFVDAAHGYGLSVVLDIVLNHFGPEGNYLPLLSPDFFHKERQTPWGAGIAYDVDAARA
YISEAPLYWLHEYNLDGLRFDAIDQIEDTNEPHILVEIAKRIRQEITDRPIHLTTEDSRN
IVSLHPRDESGTATLFTGEWNDDFHNAVHVFATGETHAYYEDFADSPEKWVARVLAEGFA
YQGEVSQHAGEPRGVDSTQQPPVAFVDFIQNHDQVGNRAQGDRLISLAGADRTRVMLATL
LLSPHIPLLFMGEEYGETNPFLFFTDFHGDLAKAVREGRTREFEGHAGHEGEDVPDPNDP
ETFTRSQLDWTRPHSVEGQRWLAFSRELLALRQQHIVPLLRGATRQQGEIIATAPGFIAV
RWALPQGTLSMALNIGTASQPLPELPGETLFAWPEAGAELAQNAIIVRLSQGEAE

Enzyme Prediction     

EC	3.2.1.141	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	123	436	3.1e-129	0.9968051118210862

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02402	trehalose_TreZ	0.0	20	563	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]
cd11325	AmyAc_GTHase	0.0	76	515	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	7.32e-180	6	572	22	607	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11350	AmyAc_4	1.13e-60	98	522	1	388	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	7.90e-36	22	517	23	531	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
APZ06535.1	0.0	1	595	1	595
AST68753.1	0.0	1	595	1	595
QAR46286.1	0.0	1	595	1	595
QNQ20364.1	0.0	1	595	1	595
AZI87651.1	0.0	1	595	1	595

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	0.0	1	593	25	615	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
2BHU_A	4.55e-130	11	552	26	569	Crystalstructure of Deinococcus radiodurans maltooligosyltrehalose trehalohydrolase [Deinococcus radiodurans]
2BHY_A	4.00e-128	11	552	26	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]
1EH9_A	1.17e-124	12	529	3	501	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	1.17e-124	12	529	3	501	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	2.97e-130	11	552	26	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	1.83e-127	12	513	7	518	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ PE=3 SV=1
Q44316	6.77e-125	18	513	15	520	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q55088	6.62e-124	12	529	4	502	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
P95867	9.69e-121	14	536	6	511	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003883_00585.