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CAZyme Information: MGYG000004015_00378

You are here: Home > Sequence: MGYG000004015_00378

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Psychrobacillus sp012843435
Lineage Bacteria; Firmicutes; Bacilli; Bacillales_A; Planococcaceae; Psychrobacillus; Psychrobacillus sp012843435
CAZyme ID MGYG000004015_00378
CAZy Family GH68
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
637 MGYG000004015_2|CGC1 71658.02 5.2945
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004015 3783055 MAG United Kingdom Europe
Gene Location Start: 36413;  End: 38326  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004015_00378.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH68 78 473 2.4e-113 0.9712230215827338

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08997 GH68 1.96e-163 112 469 1 354
Glycosyl hydrolase family 68, includes levansucrase, beta-fructofuranosidase and inulosucrase. Glycosyl hydrolase family 68 (GH68) consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Levansucrase, also known as beta-D-fructofuranosyl transferase, catalyzes the transfer of the sucrose fructosyl moiety to a growing levan chain. Similarly, inulosucrase catalyzes long inulin-type of fructans, and beta-fructofuranosidases create fructooligosaccharides (FOS). However, in the absence of high fructan/sucrose ratio, some GH68 enzymes can also use fructan as donor substrate. GH68 retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Biotechnological applications of these enzymes include use of inulin in inexpensive production of rich fructose syrups as well as use of FOS as health-promoting pre-biotics.
pfam02435 Glyco_hydro_68 1.33e-94 77 469 3 409
Levansucrase/Invertase. This Pfam family consists of the glycosyl hydrolase 68 family, including several bacterial levansucrase enzymes, and invertase from zymomonas.
cd18609 GH32-like 5.25e-26 108 391 5 255
Glycosyl hydrolase family 32 family protein. The GH32 family contains glycosyl hydrolase family GH32 proteins that cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd08979 GH_J 5.83e-17 113 398 1 235
Glycosyl hydrolase families 32 and 68, which form the clan GH-J. This glycosyl hydrolase family clan J (according to carbohydrate-active enzymes database (CAZY)) includes family 32 (GH32) and 68 (GH68). GH32 enzymes include invertase (EC 3.2.1.26) and other other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). The GH68 family consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10, also known as beta-D-fructofuranosyl transferase), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9). GH32 and GH68 family enzymes are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) and catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd08996 GH32_FFase 1.23e-04 184 277 64 135
Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AOZ74539.1 2.10e-231 2 489 24 516
AOZ78336.1 2.10e-231 2 489 24 516
AJA51172.1 2.10e-231 2 489 24 516
QST00356.1 2.96e-183 54 491 27 471
QHA90839.1 8.30e-139 65 476 22 440

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7BJ4_A 1.99e-128 80 485 13 411
ChainA, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_B Chain B, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_C Chain C, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_D Chain D, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_E Chain E, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_F Chain F, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_G Chain G, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_H Chain H, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_I Chain I, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_J Chain J, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_A Chain A, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_B Chain B, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_C Chain C, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_D Chain D, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_E Chain E, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_F Chain F, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_G Chain G, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_H Chain H, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_I Chain I, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_J Chain J, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_A Chain A, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_B Chain B, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_C Chain C, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_D Chain D, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_E Chain E, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_F Chain F, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_G Chain G, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_H Chain H, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_I Chain I, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_J Chain J, Levansucrase [Halalkalicoccus jeotgali B3]
7EHR_A 1.02e-83 80 477 33 428
ChainA, Levansucrase [Brenneria sp. EniD312]
7EHS_A 2.81e-83 80 477 33 428
ChainA, Levansucrase [Brenneria sp. EniD312]
7FDZ_A 5.53e-83 80 477 33 428
ChainA, Levansucrase [Brenneria sp. EniD312]
7EHT_A 3.01e-82 80 477 33 428
ChainA, Levansucrase [Brenneria sp. EniD312]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O68609 2.63e-79 69 477 16 422
Levansucrase OS=Pseudomonas savastanoi pv. phaseolicola OX=319 GN=lsc PE=3 SV=1
O54435 6.44e-79 72 477 3 406
Levansucrase OS=Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / CIP 78.65) OX=745277 GN=sacB PE=3 SV=1
O52408 1.89e-77 72 477 3 406
Levansucrase OS=Pseudomonas savastanoi pv. glycinea OX=318 GN=lsc PE=3 SV=1
Q46654 2.82e-76 77 477 8 406
Levansucrase OS=Erwinia amylovora OX=552 GN=lsc PE=3 SV=1
P0DJA4 1.44e-75 78 480 7 400
Extracellular sucrase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacC PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000066 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004015_00378.