CAZyme Information: MGYG000002534_00643

Basic Information

• Species: Citrobacter_A farmeri
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter_A; Citrobacter_A farmeri
• CAZyme ID: MGYG000002534_00643
• CAZy Family: GH13
• CAZyme Description: Oligo-1,6-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
528	MGYG000002534_1|CGC15	59748.21	4.7025

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002534	5715629	Isolate	Australia	Oceania

• Gene Location: Start: 657943; End: 659529 Strand: +

Full Sequence      

MNKQPWWQACTCYQIYLPSFCDGNGDGMGDFPGLLSKVDYLHELGVGAIWITPFYPSPLV
DNGYDISDYCAVDARFGTLEDFRKVVARCHACGIRVIIDLVINHVSSAHPWFRDAWNNPA
SRYRDYFLFSKQPNNWQSFFSGSAWTAEPDTGEFYYHKFAPEQVDLNWANPDVEREIYRV
VDFWKAQGVDGFRFDVINFLTTDGIGPDNPQVNGEQQHNFDINQPGILETLRRLCRYVRQ
QGENFLIGEIGSEALDVLARYQSPELMDVVFNFNIGSQKTFDIARLCEAINATQAQQSGL
PTLFFSSHDMPRMIGRFGEGSRDTARALAVLVLQLTARGVPFIYQGEELGMPNYSPLTVE
QLFDIQAKTHYQTALQQGANEVQALAQAVEHSRDGSRAPLLWSDAPFAGFSTVAPWMPVC
EDYPLINAERQRQAPTSLWRQYQALIALRAATPALCEGASSELGLTESCVWFTRETVQES
VWVAINFGAPVRNPWWDIPAGVLYGIDGQWLDKNQIVMKRSVHEQTQR

Enzyme Prediction     

No EC number prediction in MGYG000002534_00643.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	29	353	2.2e-105	0.994269340974212

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11333	AmyAc_SI_OligoGlu_DGase	0.0	8	449	1	426	Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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.
TIGR02403	trehalose_treC	1.25e-155	6	489	1	501	alpha,alpha-phosphotrehalase. Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.
cd11330	AmyAc_OligoGlu	1.52e-146	5	468	1	470	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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.
cd11331	AmyAc_OligoGlu_like	6.70e-145	5	458	1	449	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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.
PRK10933	PRK10933	5.07e-132	1	510	2	521	trehalose-6-phosphate hydrolase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AST78186.1	0.0	1	528	1	528
BBS90095.1	0.0	1	528	1	528
BBT69366.1	0.0	1	528	1	528
BBS95117.1	0.0	1	528	1	528
BBR57320.1	0.0	1	528	1	528

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2ZE0_A	3.29e-110	3	518	2	527	Alpha-glucosidaseGSJ [Geobacillus sp. HTA-462]
2PWG_A	4.15e-108	5	493	4	514	ChainA, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWG_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWH_A Chain A, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWH_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila]
1ZJA_A	4.27e-108	5	493	5	515	ChainA, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],1ZJA_B Chain B, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],1ZJB_A Chain A, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],1ZJB_B Chain B, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],2PWD_A Chain A, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWD_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],4H8V_A Crystal structure of the trehalulose synthase MUTB in complex with trehalulose [Rhizobium sp. MX-45],4H8V_B Crystal structure of the trehalulose synthase MUTB in complex with trehalulose [Rhizobium sp. MX-45]
4H2C_A	4.27e-108	5	493	5	515	Trehalulosesynthase MutB R284C mutant [Rhizobium sp. MX-45]
4GO8_A	6.02e-108	5	493	5	515	ChainA, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],4GO8_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29094	5.36e-107	3	504	2	526	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
Q9K8U9	7.34e-107	6	459	5	481	Oligo-1,6-glucosidase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=malL PE=3 SV=1
Q54796	3.04e-105	3	449	2	454	Glucan 1,6-alpha-glucosidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=dexB PE=3 SV=2
P39795	4.98e-104	2	487	4	509	Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2
P28904	5.30e-104	6	495	7	512	Trehalose-6-phosphate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=treC PE=1 SV=3

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
1.000067	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002534_00643.