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CAZyme Information: MGYG000000119_02596

You are here: Home > Sequence: MGYG000000119_02596

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 Blautia sp000432195
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp000432195
CAZyme ID MGYG000000119_02596
CAZy Family GH31
CAZyme Description Alpha-xylosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
748 MGYG000000119_19|CGC1 84342.78 4.992
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000119 3510293 Isolate Canada North America
Gene Location Start: 9318;  End: 11564  Strand: -

Full Sequence      Download help

MKFTNGYWLL  KDEMKAVYAV  EYASHRVKGK  EVTVYLPSGH  IADRGNCLNL  PMLTLTLSSP60
MEGVIKVSAV  HHAGALYKGP  FAEIQNENPE  VVIEDTEEAL  IYRSGSLKAV  LDKTPGAYKL120
AFYEGDTLLT  ESSFRNLAYM  QNTRTGKNYM  LEQLAIDVDE  YIYGLGERFT  PFVKNGQVVE180
MWNEDGGTAS  EIAYKNIPFY  ITNKGYGVLV  DHEGDVSYEI  ASEKVERIQF  SVEGERLDYY240
FISGKTPIGT  VEKYTELTGK  PALPPAWSFG  LWLTTSFTTN  YDEETTSSFI  QGMADRNIPL300
HVFHFDCYWM  EAYEWCNFVW  DPATFPDPKG  MLQRYHEKGL  KICVWINPYI  GQKSPLFQEG360
MEHGYLIKKK  DGSVWQTDLW  QAGMGLVDFT  NPEAVIWYQE  KLKTLLDMGV  DCFKTDFGER420
IPVKDIAYFD  GSDPVKMHNY  YTYLYNKAVF  ELLERERGKG  EAVLFARSAT  VGGQKFPAHW480
GGDCSATYPS  MAETLRGGLS  LALSGFGFWS  HDISGFESTA  PADIYKRWCQ  FGLLSSHSRL540
HGSSSYRVPW  LFDEEACVIL  KEFVNLKCRL  MPYLYGQAVK  AHVKGTPMLR  PMFLDFPQDK600
ACDTLDRQYM  FGDSLLVAPV  FKENGEVQYY  LPEGTWYNLI  TGSKAEGGKW  QKETHDYHSL660
PLMVRPNTIL  PMGNNEVDAA  YDFADGVTLV  LSEFSEGAKA  EAEIPDLQGN  IVMKACAQRH720
GEEIFVSVEG  GNGNFSVKNM  GSGTVVVK748

Enzyme Prediction      help

EC 3.2.1.177

CAZyme Signature Domains help

Created with Snap3774112149187224261299336374411448486523561598635673710239670GH31
Family Start End Evalue family coverage
GH31 239 670 5.4e-136 0.9976580796252927

CDD Domains      download full data without filtering help

Created with Snap37741121491872242612993363744114484865235615986356737101667PRK10658259570GH31_xylosidase_YicI240670Glyco_hydro_3129701YicI259564GH31
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10658 PRK10658 0.0 1 667 1 665
putative alpha-glucosidase; Provisional
cd06593 GH31_xylosidase_YicI 0.0 259 570 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.
pfam01055 Glyco_hydro_31 0.0 240 670 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.
COG1501 YicI 0.0 29 701 22 701
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06589 GH31 8.81e-86 259 564 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 Snap37741121491872242612993363744114484865235615986356737101740QBE96561.1|GH311740QIB57061.1|GH311740QMW80162.1|GH311744QJU17439.1|GH311744ASU29736.1|GH31
Hit ID E-Value Query Start Query End Hit Start Hit End
QBE96561.1 0.0 1 740 1 740
QIB57061.1 0.0 1 740 1 740
QMW80162.1 0.0 1 740 1 740
QJU17439.1 0.0 1 744 1 744
ASU29736.1 0.0 1 744 1 744

PDB Hits      download full data without filtering help

Created with Snap377411214918722426129933637441144848652356159863567371017372F2H_A17371XSI_A27371WE5_A1596915F7C_A936725F7U_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2F2H_A 2.38e-312 1 737 1 736
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 2.84e-312 1 737 1 736
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 5.09e-299 2 737 2 736
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 3.00e-115 159 691 201 736
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 1.79e-81 93 672 180 804
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 Snap37741121491872242612993363744114484865235615986356737101737sp|P31434|XYLS_ECOLI1737sp|P96793|XYLQ_LACPE1734sp|Q5AW25|AGDD_EMENI87744sp|Q9F234|AGL2_BACTQ62689sp|Q9P999|XYLS_SACS2
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P31434 1.26e-311 1 737 1 736
Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2
P96793 1.02e-260 1 737 1 740
Alpha-xylosidase XylQ OS=Lactiplantibacillus pentosus OX=1589 GN=xylQ PE=1 SV=1
Q5AW25 7.63e-260 1 734 1 765
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 2.75e-77 87 744 80 744
Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q9P999 6.76e-67 62 689 15 641
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
1.000064 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000119_02596.