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CAZyme Information: MGYG000002956_00024
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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 | Lactobacillus kalixensis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactobacillus; Lactobacillus kalixensis | |||||||||||
| CAZyme ID | MGYG000002956_00024 | |||||||||||
| CAZy Family | GH31 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 24263; End: 27274 Strand: + | |||||||||||
Full Sequence Download help
| MTQDTQINRH QLGQLTGANK RDNYYELHYA TGEIARLYIL ADGVFRFFID PTKNFNENNS | 60 |
| PLVDLSKFNN HFFEKSEPRA TSDSLIIRSG NYQLIFQQKP ALMSIFDERL HRMRMSQANP | 120 |
| IELGSDQTIE ILKQNKNEFY FGGGLQNGSF SHKGKHISIK CDNLTGDGGV LSQVPFFWSN | 180 |
| AGFGELRNTL KFGEYDFGKL NKDAAIIKHE SPIFDNFYII GNSPSDILSK YYLLTGKPMM | 240 |
| LPKYALDLGY MGNFLTTLWQ PSQASVRNAS QYEDGTYYAR TTNPEDASGK ASLNGEEEYQ | 300 |
| FSARAMIDRY TKLHFPLGWI VPNYGIKDVN QDAMSVFNDY ANTQGVESGI WTNDASSALP | 360 |
| KNTSLIATDN SRSNVLDQDN RNLKANLNRK RPLVLSSNGQ TGSQSKAALF FGDTGGNWEN | 420 |
| IGTQVAGFLG ASLSGEPLVG SGIDGKIGGG NAQIAIRDFE WKTFTPLLFS INDQGLYDKT | 480 |
| PFAFNNKMTR INRAYLALRS HLKNYLYTLI YQTRSGGSIM QPLFMEFPHE QINYTEQVGH | 540 |
| EFMLGSNLLI APITSGREDN NGNSCKDNLY LPNHRTMWID LFTGEKYLGG RVYNRMSYPI | 600 |
| WHLPVFVRGG AIFDLGKRNY VLYPQAKSQV TFYDDNGFTD FAHNHTETTV TSELDSSKLT | 660 |
| VTIDPVKGDY TGMETNSTTT INIVCDTYPD RVTVKINDQI VNLPESGTID AFAHIKEGLY | 720 |
| YNTNYSWLPE FDQYREAKQN ALQIKLASRD ITDSKIEVII QNFNYGSQTL VHSITDSVLC | 780 |
| SPKLPIVDPD KITAHSLSVS WPESTDSVQF EINGILYDGI SGGNFTFHEL EPNTRYIMRM | 840 |
| RYVAGNKVSE WSDPFGAITK KAAIDYAVHD INVDSNYKAN PEHPLSYLTD LKLASEWQTQ | 900 |
| NALTEDNPLT LTFNFNQVED LSRMVFVPRS IDRDANPLEV SLEISTDGIS FKPYGDRINW | 960 |
| KSDSKNKVIG LRNISAKAIR LTVYKATGPI VAAREVMFFR EKD | 1003 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH31 | 380 | 612 | 2.6e-50 | 0.5199063231850117 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd06596 | GH31_CPE1046 | 1.03e-68 | 234 | 584 | 1 | 334 | Clostridium CPE1046-like. CPE1046 is an uncharacterized Clostridium perfringens protein with a glycosyl hydrolase family 31 (GH31) domain. The domain architecture of CPE1046 and its orthologs includes a C-terminal fibronectin type 3 (FN3) domain and a coagulation factor 5/8 type C domain in addition to the GH31 domain. 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 | 3.32e-52 | 28 | 684 | 37 | 753 | Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism]. |
| pfam01055 | Glyco_hydro_31 | 1.00e-47 | 217 | 612 | 1 | 441 | 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 | 1.38e-23 | 383 | 612 | 205 | 425 | 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. |
| cd14752 | GH31_N | 3.86e-18 | 132 | 236 | 14 | 122 | N-terminal domain of glycosyl hydrolase family 31 (GH31). This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). 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 of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QFY04019.1 | 0.0 | 1 | 1003 | 1 | 1003 |
| QFY05230.1 | 0.0 | 1 | 1003 | 1 | 1003 |
| ARD06254.1 | 0.0 | 1 | 1003 | 1 | 1003 |
| QJD72701.1 | 0.0 | 1 | 1002 | 1 | 1002 |
| QFG50650.1 | 0.0 | 1 | 1002 | 1 | 1002 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7F7R_A | 6.09e-168 | 12 | 860 | 37 | 958 | ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100] |
| 6M76_A | 8.56e-168 | 12 | 860 | 37 | 958 | GH31alpha-N-acetylgalactosaminidase from Enterococcus faecalis [Enterococcus faecalis ATCC 10100],6M77_A GH31 alpha-N-acetylgalactosaminidase from Enterococcus faecalis in complex with N-acetylgalactosamine [Enterococcus faecalis ATCC 10100] |
| 7F7Q_A | 8.56e-168 | 12 | 860 | 37 | 958 | ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100] |
| 6JR6_A | 7.00e-18 | 27 | 663 | 55 | 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 | 1.59e-17 | 27 | 663 | 55 | 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
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q9F234 | 7.26e-24 | 383 | 637 | 454 | 699 | Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1 |
| Q9P999 | 1.78e-22 | 387 | 639 | 401 | 660 | Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1 |
| Q94502 | 5.73e-15 | 391 | 618 | 595 | 815 | Neutral alpha-glucosidase AB OS=Dictyostelium discoideum OX=44689 GN=modA PE=3 SV=1 |
| P14410 | 9.66e-15 | 390 | 733 | 581 | 937 | Sucrase-isomaltase, intestinal OS=Homo sapiens OX=9606 GN=SI PE=1 SV=6 |
| Q14697 | 4.51e-13 | 390 | 612 | 595 | 809 | Neutral alpha-glucosidase AB OS=Homo sapiens OX=9606 GN=GANAB PE=1 SV=3 |
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 |
|---|---|---|---|---|---|
| 1.000053 | 0.000010 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |