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CAZyme Information: MGYG000000687_00138

You are here: Home > Sequence: MGYG000000687_00138

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; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerostipes;
CAZyme ID MGYG000000687_00138
CAZy Family GH31
CAZyme Description Alpha-xylosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
777 MGYG000000687_2|CGC1 88805.67 4.9374
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000687 2211452 MAG Kazakhstan Asia
Gene Location Start: 33057;  End: 35390  Strand: -

Full Sequence      Download help

MKFGNGCWLQ  KEGYECFPPQ  QIYFTKIEPK  KVTLCAPTSR  IFHRGDTLGG  INLTLEITSP60
MPEVLRVKTY  HHLGIRKTGP  DFELETQENV  ELEIEDSDEK  ICIKRGSLSL  TITKENFSME120
YARDGEVISK  CNGRDRAFMK  TDWKGYAYDK  GSKDAYMRQQ  LSLSVGELVY  GMGERFTPFV180
KNGQTVDIWN  EDGGTSTYQS  YKNIPFYLTN  KGYGVFVNNP  GDVSFEVATE  QVSKVQFSVS240
GECLDYFFIN  GPTMKEVLAH  YTGITGKPSL  PAQWTFGLWL  STSFTTNYDE  ETVMSFINGM300
EERGIPLQVF  HFDCFWMKDF  HWCDFTWDNR  VFPDPEGMLQ  RIKAKGLKIC  VWINPYIAQE360
SPLFLEGMEK  GYFIKRTNGD  VWQWDMWQPG  MAIVDFTNPQ  ACQWFKDKLA  VLVDMGVDCF420
KTDFGERIPT  EDVVYYDGAD  PVKMHNYYTY  LYNKVVYELL  EEKKGKEEAV  LFARSASVGG480
QKFPVHWGGD  CWSTYEAMAE  SLRGGLSLTM  SRFGFWSHDI  GGFENTSTAD  VYKRWAAFGL540
LSTHSRLHGS  TSYRVPWAYD  DKAVDVVRYF  TKLKMQLLPY  NIYSNAAYTA  KTGVPTMRSM600
VLEFEKDPTC  AYLDRQYMLG  GNILTAPIFR  EDGIANYYLP  AGTWTNYLTG  ETREGGVWVE660
EHHDYLSIPL  WVRENSIIPV  CNQMERNDDA  YDKNLQLKVY  ELKEEASTCV  TQNGSQVLSI720
EIKKDGEAIT  CKAETENAYE  IRFVNCKLTS  ADNAELVVDG  NDTIVKVSDP  KAVVVCR777

Enzyme Prediction      help

EC 3.2.1.177

CAZyme Signature Domains help

Created with Snap3877116155194233271310349388427466505543582621660699738246678GH31
Family Start End Evalue family coverage
GH31 246 678 1.2e-126 0.9976580796252927

CDD Domains      download full data without filtering help

Created with Snap3877116155194233271310349388427466505543582621660699738266577GH31_xylosidase_YicI8730YicI1675PRK10658247678Glyco_hydro_31266571GH31
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06593 GH31_xylosidase_YicI 0.0 266 577 1 308
alpha-xylosidase YicI-like. YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) enzyme that catalyzes the release of an alpha-xylosyl residue from the non-reducing end of alpha-xyloside substrates such as alpha-xylosyl fluoride and isoprimeverose. YicI forms a homohexamer (a trimer of dimers). 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. The YicI family corresponds to subgroup 4 in the Ernst et al classification of GH31 enzymes.
COG1501 YicI 0.0 8 730 1 734
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
PRK10658 PRK10658 0.0 1 675 1 665
putative alpha-glucosidase; Provisional
pfam01055 Glyco_hydro_31 6.35e-178 247 678 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.
cd06589 GH31 4.83e-80 266 571 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

Created with Snap38771161551942332713103493884274665055435826216606997381774QJU17220.1|GH311774QQQ94732.1|GH311774ANU77154.1|GH311774ASU29953.1|GH311769BBF45281.1|GH31
Hit ID E-Value Query Start Query End Hit Start Hit End
QJU17220.1 0.0 1 774 1 773
QQQ94732.1 0.0 1 774 1 773
ANU77154.1 0.0 1 774 1 773
ASU29953.1 0.0 1 774 1 773
BBF45281.1 0.0 1 769 1 772

PDB Hits      download full data without filtering help

Created with Snap387711615519423327131034938842746650554358262166069973817302F2H_A17301XSI_A27301WE5_A1676995F7C_A947255F7U_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2F2H_A 1.08e-293 1 730 1 724
Structureof the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_B Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_C Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_D Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_E Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_F Structure of the YicI thiosugar Michaelis complex [Escherichia coli]
1XSI_A 1.29e-293 1 730 1 724
Structureof a Family 31 alpha glycosidase [Escherichia coli],1XSI_B Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_C Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_D Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_E Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_F Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_A Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_B Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_C Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_D Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_E Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_F Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSK_A Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_B Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_C Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_D Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_E Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_F Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli]
1WE5_A 5.52e-281 2 730 2 724
CrystalStructure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_B Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_C Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_D Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_E Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_F Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli]
5F7C_A 1.88e-113 167 699 202 738
Crystalstructure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_B Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_C Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_D Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5F7U_A 4.64e-70 94 725 180 857
Cycloalternan-formingenzyme from Listeria monocytogenes in complex with pentasaccharide substrate [Listeria monocytogenes EGD-e]

Swiss-Prot Hits      download full data without filtering help

Created with Snap38771161551942332713103493884274665055435826216606997381730sp|P31434|XYLS_ECOLI1764sp|P96793|XYLQ_LACPE1768sp|Q5AW25|AGDD_EMENI88762sp|Q9F234|AGL2_BACTQ52700sp|Q9P999|XYLS_SACS2
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P31434 5.71e-293 1 730 1 724
Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2
P96793 4.09e-247 1 764 1 749
Alpha-xylosidase XylQ OS=Lactiplantibacillus pentosus OX=1589 GN=xylQ PE=1 SV=1
Q5AW25 8.64e-238 1 768 1 772
Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1
Q9F234 3.75e-71 88 762 80 770
Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q9P999 9.42e-61 52 700 5 644
Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 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
1.000096 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000687_00138.