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CAZyme Information: MGYG000003671_00623

You are here: Home > Sequence: MGYG000003671_00623

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 HGM10818 sp900772445
Lineage Bacteria; Firmicutes; Bacilli; RF39; UBA660; HGM10818; HGM10818 sp900772445
CAZyme ID MGYG000003671_00623
CAZy Family GH31
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
785 92197.89 8.9111
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003671 1177326 MAG Peru South America
Gene Location Start: 8039;  End: 10396  Strand: -

Full Sequence      Download help

MSNLSGYFIK  DNNNLISKKE  CVLTGNKYRF  TVLTDRLIRL  EYSPNGVFED  RASQNIINRL60
FERPIFVVNE  SDTLLQISTK  YFVLSYVKNA  KFDSGKLTPG  SNLKVLLKDT  DKTWYYNHPE120
ARNFGTINYS  LDDFVGKLKL  DKGMYSTDGF  CVLDDSKTLV  LNPDGEYVAR  NDNNIDLYLF180
MYKRDFGLCL  KDYFDITGYP  SFLPRYAFGN  WWYKNDKYTN  KDINNVIKKF  KENEIPLSVI240
MLGDKWHNDI  NNYSFDNTLI  DPHKLISLLN  TNNIKLGLTV  DPRLKVSEKS  INYDKLSNYI300
KEKDISFIPL  SMTKLTLYFN  LFIRELSNMG  VDIFNIDYDN  ILDKNTLGLF  NHFHFVENLI360
KNKRGIILSR  NSKIATHRYP  ITFTGRTIVD  WNTLSYLPLY  TMSASNSGVS  FIAHAIGGYY420
KGIEQEELYM  RYIQLGTFSP  FLILAGDSSK  YCKREPWKWN  FLRLSVIREY  MQLRNKLVPY480
IYTESYNYYK  KCLPLVQPLY  YKYPQVYDEP  LYINEYFFGS  EMLICPITKK  KNTLINRVVQ540
RIFVPSGIWF  DFKTGKKYPG  DKYYMCFYKD  DEYPAFCKSG  AIIPLSLNDN  TNNPTDMEVQ600
IFPLSDNTYT  IYEDDGISNN  YLKDDCMLTH  INYKYQKDNY  SLMITNSKKI  GIVQSRNYKI660
RFKNTQNITD  VNVLYNDKPY  NASVYYDKND  FVVSVDNVIS  GGTLFINIRG  NNILLEAIQL720
INEDIKEILN  DLEIETFLKD  KIDNILFSDI  SVRRKRIEIK  KLKKYKLDPK  FINMFIKLLE780
YISNV785

Enzyme Prediction      help

No EC number prediction in MGYG000003671_00623.

CAZyme Signature Domains help

Created with Snap3978117157196235274314353392431471510549588628667706745178583GH31
Family Start End Evalue family coverage
GH31 178 583 1.2e-76 0.9976580796252927

CDD Domains      download full data without filtering help

Created with Snap3978117157196235274314353392431471510549588628667706745197481GH31_u1173677YicI190583Glyco_hydro_31198585GH31_GANC_GANAB_alpha198461GH31
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06595 GH31_u1 3.68e-102 197 481 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.
COG1501 YicI 2.89e-70 173 677 232 771
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
pfam01055 Glyco_hydro_31 1.84e-66 190 583 12 442
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
cd06603 GH31_GANC_GANAB_alpha 4.00e-37 198 585 1 428
neutral alpha-glucosidase C, neutral alpha-glucosidase AB. This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.
cd06589 GH31 6.07e-32 198 461 1 253
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 Snap397811715719623527431435339243147151054958862866770674520742QVK18410.1|GH3117749BCN31488.1|GH3116696AMC08870.1|GH3111748QES75740.1|GH3116742QBE99217.1|GH31
Hit ID E-Value Query Start Query End Hit Start Hit End
QVK18410.1 3.85e-148 20 742 20 752
BCN31488.1 3.46e-130 17 749 13 766
AMC08870.1 9.34e-130 16 696 16 715
QES75740.1 1.08e-127 11 748 14 765
QBE99217.1 5.17e-127 16 742 13 756

PDB Hits      download full data without filtering help

Created with Snap3978117157196235274314353392431471510549588628667706745126167WJC_A126167WJ9_A1905855F7C_A1776446JR6_A1776446JR8_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
7WJC_A 5.73e-99 12 616 31 646
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]
7WJ9_A 8.00e-99 12 616 31 646
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]
5F7C_A 1.03e-29 190 585 294 717
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]
6JR6_A 2.49e-27 177 644 237 755
Flavobacteriumjohnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR7_A Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101]
6JR8_A 5.75e-27 177 644 237 755
Flavobacteriumjohnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101]

Swiss-Prot Hits      download full data without filtering help

Created with Snap3978117157196235274314353392431471510549588628667706745175651sp|Q9P999|XYLS_SACS2175635sp|Q9F234|AGL2_BACTQ191622sp|Q8BVW0|GANC_MOUSE191622sp|Q8TET4|GANC_HUMAN190596sp|Q5AW25|AGDD_EMENI
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9P999 1.94e-37 175 651 190 689
Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
Q9F234 3.83e-31 175 635 230 730
Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q8BVW0 4.91e-27 191 622 330 808
Neutral alpha-glucosidase C OS=Mus musculus OX=10090 GN=Ganc PE=1 SV=2
Q8TET4 4.64e-26 191 622 346 824
Neutral alpha-glucosidase C OS=Homo sapiens OX=9606 GN=GANC PE=2 SV=3
Q5AW25 8.02e-25 190 596 269 711
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 OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000032 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003671_00623.