| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01037959001 |
| Family | GH31 |
| Protein Properties | Length: 1761 Molecular Weight: 196718 Isoelectric Point: 7.4824 |
| Chromosome | Chromosome/Scaffold: 10 Start: 11627282 End: 11642515 |
| Description | Glycosyl hydrolases family 31 protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH31 | 254 | 722 | 0 |
| FYFFSGPTPEMVVQQYTELIGHPAPMPYWSFGFHQCRYGYTNVSDVEGVVAGYAKAGIPLEVMWTDIDYMDAYKDFTLDPINFPLDKIKKLVDTLHQNGQ KYVLILDPGISVNQTYRTYKRGMEADIFIKRDGIPYLGSVWPGPVYFPDFVNPATEIFWGGEIKIFRDSLPIDGLWLDMNEISNFITSPPTPLSTLDDPP YKINNAGVRRPINNRTVPATSLHFGNITEYNAHNLYGILESKATNAALTKLTGKRPFILTRSTFVGSGKYAAHWTGDNAATWDDLAYSIPAVLNFGLFGI PMVGADICGFSGDTNEELCRRWIQLGAFYPFARDHSAKFTIRQELYVWDSVAATAKKVLGLRYRLLPYFYTLMYEAHTKGVPIARPLFFSFPQDPETYGI NFQFLIGKGVMVSPVLKPGEVSVKAYFPSGNWFDLFNYSNAVSAGSGKYTTLDAPPDHINVHVREGNIL | |||
| GH31 | 1148 | 1616 | 0 |
| FYFFSGPTPEMVMQQYTELIGRPAPMPYWSFGFHQCRYGYMNVSDVGGVVAGYAKAGIPLEVMWTDIDYMDAYKDFTLDPINFPLDKMKKLVDTLHQNGQ KYVLILDPGISVNKTYGTYKRGMEADIFIKRDGIPYLGSVWPGPVYFPDFVNPATEIFWGGEIKIFRDSLAIDGLWLDMNELSNFITSPPTPSSTLDDPP YKINNVGVRRPINNNTVPATSLHFGNITEYNAHNLYGHLESKATNAALTKLTGKRPFILTRSTFVGSGKYAAHWTGDNAATWDDLAYSIPAVLNFGLFGI PMVGADICGFSGNTNEELCRRWIQLGAFYPFARDHSEKFTIRQELYVWDSVAATAKKVLGLRYRLLPYFYTLMYEAHTKGVPIARPLFFSFPQDPGTYGI NSQFLIGKGVMVSPVLKPGEVSVKAYFPSGNWFDLFNYSNAVSAGSGKYTTLDAPPDHINVHVREGNIL | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1761 Download |
| MGRKRPQPPL HFHHLLLAFL FCCSFSNAKN EEDLVGYGYR VRSVSFDPSG NSLTAHLDLI 60 KPSPVFGPDV RNLILVASLE TNDRLRIRIT DSEHQRWEIP REILPRYTQL HLRSDLVFTL 120 RRTTPFGFIV SRRSTGDILF DASSDASEAG TFLVFKDQYL QVSSALPILR SSLYGLGEHT 180 KKTFKLAQNQ TLTLWNTDIH SSNLDVNLYG LTDNRGKVPM GTTHGVLLLN SNGMDIVYTG 240 DRITYKAIGG VLDFYFFSGP TPEMVVQQYT ELIGHPAPMP YWSFGFHQCR YGYTNVSDVE 300 GVVAGYAKAG IPLEVMWTDI DYMDAYKDFT LDPINFPLDK IKKLVDTLHQ NGQKYVLILD 360 PGISVNQTYR TYKRGMEADI FIKRDGIPYL GSVWPGPVYF PDFVNPATEI FWGGEIKIFR 420 DSLPIDGLWL DMNEISNFIT SPPTPLSTLD DPPYKINNAG VRRPINNRTV PATSLHFGNI 480 TEYNAHNLYG ILESKATNAA LTKLTGKRPF ILTRSTFVGS GKYAAHWTGD NAATWDDLAY 540 SIPAVLNFGL FGIPMVGADI CGFSGDTNEE LCRRWIQLGA FYPFARDHSA KFTIRQELYV 600 WDSVAATAKK VLGLRYRLLP YFYTLMYEAH TKGVPIARPL FFSFPQDPET YGINFQFLIG 660 KGVMVSPVLK PGEVSVKAYF PSGNWFDLFN YSNAVSAGSG KYTTLDAPPD HINVHVREGN 720 ILVMQGEAMT TKAARKTPFQ LLVVLSSSGI STGEVFLDDG EEVEMGGGGK NWSLVKFYAW 780 VEDKKAIVGS EVMNRGFALS QKWIIDRVTL IGLTKAQGKR FKGFEVYTNE GTKTIGDSSL 840 KVDLDGNRKF VVMEIKKLSP NRKGPNSYIE LHILYWAIKL ITFYKQFSDS NKGAQIEESE 900 AFLFCCSFSV LCFSNAKNEE DPVGYGYRVR SVSFDPSGKS LTAHLDLIKT SPVFGPDVRN 960 LNLVASLETN DRLRIRITDS EHQRWEIPQE ILPLSDPKSD LVFTLRKTTP FGFIVSRRST 1020 GDILFDASSD ISDADTFLVF KDQYLQVSSA LPILRSSLYG LGEHTKKTFK LAQNQTLTLW 1080 NADIGSANLD VNLYGSHPFY MDVRLTDNRG KVPMGTTHGV LLLNSNGMDI VYTGDRITYK 1140 AIGGVLDFYF FSGPTPEMVM QQYTELIGRP APMPYWSFGF HQCRYGYMNV SDVGGVVAGY 1200 AKAGIPLEVM WTDIDYMDAY KDFTLDPINF PLDKMKKLVD TLHQNGQKYV LILDPGISVN 1260 KTYGTYKRGM EADIFIKRDG IPYLGSVWPG PVYFPDFVNP ATEIFWGGEI KIFRDSLAID 1320 GLWLDMNELS NFITSPPTPS STLDDPPYKI NNVGVRRPIN NNTVPATSLH FGNITEYNAH 1380 NLYGHLESKA TNAALTKLTG KRPFILTRST FVGSGKYAAH WTGDNAATWD DLAYSIPAVL 1440 NFGLFGIPMV GADICGFSGN TNEELCRRWI QLGAFYPFAR DHSEKFTIRQ ELYVWDSVAA 1500 TAKKVLGLRY RLLPYFYTLM YEAHTKGVPI ARPLFFSFPQ DPGTYGINSQ FLIGKGVMVS 1560 PVLKPGEVSV KAYFPSGNWF DLFNYSNAVS AGSGKYTTLD APPDHINVHV REGNILAMQG 1620 EAMTTKAARK TPFQLLVVLS SSGISTGEVF LDDGEDIEMG GGGKNWSLVK FYARVEDKKV 1680 IVGSEVINGG FALSQQWIID RVTLIGFTKA QAKRFKGFEV CTNVGTKTLG DSGNRKFVVM 1740 ETEKLSLPIG KEFQLKLNLT * 1800 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd06604 | GH31_glucosidase_II_MalA | 2.0e-125 | 274 | 633 | 366 | + Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This family also includes the MalA alpha-glucosidase from Sulfolobus sulfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source. | ||
| pfam01055 | Glyco_hydro_31 | 0 | 255 | 722 | 472 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
| pfam01055 | Glyco_hydro_31 | 0 | 1149 | 1616 | 472 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
| cd06602 | GH31_MGAM_SI_GAA | 0 | 274 | 651 | 383 | + This family includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII). | ||
| cd06602 | GH31_MGAM_SI_GAA | 0 | 1168 | 1545 | 383 | + This family includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII). | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN60336.1 | 0 | 1 | 859 | 1 | 877 | hypothetical protein [Vitis vinifera] |
| EMBL | CAN60336.1 | 0 | 901 | 1760 | 18 | 891 | hypothetical protein [Vitis vinifera] |
| EMBL | CAN66951.1 | 0 | 11 | 858 | 5 | 884 | hypothetical protein [Vitis vinifera] |
| EMBL | CAN66951.1 | 0 | 896 | 1760 | 3 | 899 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI39013.1 | 0 | 1 | 1760 | 1 | 1760 | unnamed protein product [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3w38_A | 0 | 902 | 1759 | 20 | 908 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum (Apo Form) |
| PDB | 3w38_A | 0 | 15 | 858 | 16 | 894 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum (Apo Form) |
| PDB | 3w37_A | 0 | 902 | 1759 | 20 | 908 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum (Apo Form) |
| PDB | 3w37_A | 0 | 15 | 858 | 16 | 894 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum (Apo Form) |
| PDB | 3ctt_A | 0 | 937 | 1655 | 61 | 774 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum (Apo Form) |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-2141 | EC-3.2.1.20 | α-glucosidase |
