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CAZyme Information: MGYG000000398_01774

You are here: Home > Sequence: MGYG000000398_01774

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; TF01-11;
CAZyme ID MGYG000000398_01774
CAZy Family GH31
CAZyme Description Alpha-xylosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
787 MGYG000000398_12|CGC1 89399.51 4.671
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000398 2936252 MAG Sweden Europe
Gene Location Start: 16437;  End: 18800  Strand: -

Full Sequence      Download help

MKVADGFWLN  KKGYDVRYAS  QAYQVTTTEN  SIKVIATPYT  VMNRGMTLGG  PNLEITYSST60
SENIIKVHIV  HYKGGLDNIP  QFELNEDTGY  VPQITRTEDK  AELVSGDTKV  VIKIGDDWDV120
QFYHKDKHLT  GGAWRSTSII  NESQFAANAR  MEMQEDDEFF  NYPQDPHRTY  IREQLKTDIG180
ECIYGFGEKF  TPFVKNGQVV  ETWNCDGGTC  SDQSYKNIPF  YISSKGYGVF  VNSSDKVSFE240
VNSDTVSKVT  FTQPGEELEY  FVIGGNNLEE  VLENYTTLTG  KPSLPPAYTF  GLWLSTSFTT300
SYDEDTVMSF  IDGMRDRKIP  LQVFHFDCFW  MKEYEWCNFE  WDKDMFPDPE  GLLKRLHEDK360
GLEVCVWINS  YISQQSKLFD  IGKEKGYFIK  NLDGSVFQAD  LWQPGMAIVD  FTNPEACDWF420
KGMLKELFKM  GVNNIKTDFG  ERIPTKCKYY  NGMDPIKMHN  YYTYLYNKVV  FEALEEYFGK480
DKACLFARSA  TVGGQKFPVH  WGGDCYAEYS  AMAETLRGGL  SLCSSGFGFF  SHDMGGFEAT540
APADVYKRWC  AFGLLSTHSR  LHGSTSYRVP  WVYDKDGDTE  ACDVLRHYTV  LKGRLMPYLW600
AQANKTHQVG  VPMMRSMVIA  FTDDTACKYL  DQQYMLGDNL  CIVPVMNEEG  KAEFYVPDCG660
TWTDIQSGEK  YEGGRYYTRQ  CDYFQTPILA  RPNSIVTYGN  FDAEDKMTVL  YDYLQDAEAV720
IYGLEDGKSA  SAVIYDSESN  KLTQIKAVRN  GNVIDVTYDA  SDRSFKITAE  GKTVDAAAGS780
TNVQITL787

Enzyme Prediction      help

EC 3.2.1.177

CAZyme Signature Domains help

Created with Snap3978118157196236275314354393432472511550590629668708747260696GH31
Family Start End Evalue family coverage
GH31 260 696 3.4e-119 0.9976580796252927

CDD Domains      download full data without filtering help

Created with Snap39781181571962362753143543934324725115505906296687087478769YicI280595GH31_xylosidase_YicI1693PRK10658261696Glyco_hydro_31280589GH31
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1501 YicI 0.0 8 769 1 735
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06593 GH31_xylosidase_YicI 0.0 280 595 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.
PRK10658 PRK10658 0.0 1 693 1 665
putative alpha-glucosidase; Provisional
pfam01055 Glyco_hydro_31 3.59e-153 261 696 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 5.23e-76 280 589 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 Snap39781181571962362753143543934324725115505906296687087471787BAV13089.1|GH311787ADL51183.1|GH311787QAA31782.1|GH311787CBL16634.1|GH311777CCO05987.1|GH31
Hit ID E-Value Query Start Query End Hit Start Hit End
BAV13089.1 0.0 1 787 1 780
ADL51183.1 0.0 1 787 1 780
QAA31782.1 0.0 1 787 1 780
CBL16634.1 0.0 1 787 1 778
CCO05987.1 0.0 1 777 1 769

PDB Hits      download full data without filtering help

Created with Snap397811815719623627531435439343247251155059062966870874717572F2H_A17571XSI_A27571WE5_A1816965F7C_A1727855F7U_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2F2H_A 5.24e-269 1 757 1 726
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 6.22e-269 1 757 1 726
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 9.00e-257 2 757 2 726
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 1.11e-101 181 696 202 715
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 1.86e-65 172 785 239 878
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 Snap39781181571962362753143543934324725115505906296687087471757sp|P31434|XYLS_ECOLI1748sp|Q5AW25|AGDD_EMENI1754sp|P96793|XYLQ_LACPE178771sp|Q9F234|AGL2_BACTQ169743sp|Q9P999|XYLS_SACS2
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P31434 2.77e-268 1 757 1 726
Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2
Q5AW25 1.45e-233 1 748 1 744
Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1
P96793 1.26e-213 1 754 1 728
Alpha-xylosidase XylQ OS=Lactiplantibacillus pentosus OX=1589 GN=xylQ PE=1 SV=1
Q9F234 7.28e-59 178 771 144 743
Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q9P999 1.39e-52 169 743 99 683
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
1.000078 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000398_01774.