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CAZyme Information: MGYG000004430_01484

You are here: Home > Sequence: MGYG000004430_01484

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485;
CAZyme ID MGYG000004430_01484
CAZy Family GH31
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1147 MGYG000004430_12|CGC1 131604.27 6.3618
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004430 3945500 MAG Israel Asia
Gene Location Start: 43017;  End: 46460  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004430_01484.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 203 629 5.2e-115 0.9976580796252927

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06595 GH31_u1 7.08e-151 222 529 1 304
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup. This family represents an uncharacterized GH31 enzyme subgroup found in bacteria and eukaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.
pfam01055 Glyco_hydro_31 5.46e-112 204 629 1 442
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
cd09083 EEP-1 2.32e-111 872 1145 4 252
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1. This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins.
COG1501 YicI 3.98e-98 140 680 168 722
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06589 GH31 1.60e-55 223 519 1 265
glycosyl hydrolase family 31 (GH31). GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QIU93240.1 2.33e-313 29 846 29 842
QNL39798.1 5.51e-312 29 846 28 841
CBK67137.1 2.13e-311 29 846 17 830
QUT31493.1 3.13e-311 29 846 28 841
QRM99741.1 3.13e-311 29 846 28 841

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7WJ9_A 7.89e-125 30 630 34 612
ChainA, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_B Chain B, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_C Chain C, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_D Chain D, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_E Chain E, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_F Chain F, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJA_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJB_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_B Chain B, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_C Chain C, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_D Chain D, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_E Chain E, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_F Chain F, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363]
7WJC_A 1.13e-123 30 630 34 612
ChainA, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJD_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJE_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJF_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363]
4C1R_A 3.37e-104 868 1141 2 278
Bacteroidesthetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482],4C1R_B Bacteroides thetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482],4C1R_C Bacteroides thetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482],4C1R_D Bacteroides thetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482]
3MPR_A 6.31e-102 868 1141 7 283
CrystalStructure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron],3MPR_B Crystal Structure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron],3MPR_C Crystal Structure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron],3MPR_D Crystal Structure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron]
3G6S_A 2.09e-57 868 1127 4 260
ChainA, Putative endonuclease/exonuclease/phosphatase family protein [Phocaeicola vulgatus ATCC 8482]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9P999 1.88e-53 172 691 155 684
Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
B3PEE6 1.65e-45 27 707 34 754
Oligosaccharide 4-alpha-D-glucosyltransferase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agd31B PE=1 SV=1
Q9F234 6.61e-40 198 735 228 777
Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q9BE70 2.90e-36 176 756 166 767
Neutral alpha-glucosidase C (Fragment) OS=Macaca fascicularis OX=9541 GN=GANC PE=2 SV=2
Q5AW25 2.93e-35 145 630 199 697
Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000434 0.282968 0.716078 0.000175 0.000197 0.000151

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004430_01484.