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Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10436707g0010 |
Family | GH31 |
Protein Properties | Length: 609 Molecular Weight: 67746.7 Isoelectric Point: 6.049 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH31 | 258 | 606 | 0 |
FYFFAGTSPLDVVQQYTALIGRPVAMPYWAFGFHQCRWGYQNVSDITNVVDNYNKSQIPLDVIWNDDDHMDAAKDFTLDPVNYPEHKLRPFLDRIHANGM RYVVLIDPGIGINTSYGTFQRGMADDVFIKHDGVPFMGQVWPGAVYFPDFLNPKTVNFWADEISRFHSMVPVDGLWIDMNEVSNFCSGKCTVPTNRSCPG TGLPWECCLDCTNITATRWXXXXXXXXNITATRWDVPPYKINASGAGAPLGFKTIATSSVHYNGILEYDAHSLYGFSQAIATHKALQNLLNKRPFILTRS TFVGSGSYAAHWTGDNKATWEDLRYSISTILNFGMFGMPMVGADICGFY |
Full Sequence |
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Protein Sequence Length: 609 Download |
MAPLVALFFT CVVCALWPLG HGQQVGYGYH LVSVDQGSDG SMIGSLELLK KTDTYGPDIP 60 HLRLYVKHET QDRVRVHITD AETKRWEVPQ ELLSREQVPA DLKISSRKAK STNSAFGFSE 120 LSGGELIFSF VANPFGFAIK RKSNGDVLFN SSYGSLVFKD QYLELTTGLP STASLYGLGE 180 NTQPEGIKIV PKESYTLYTT DISAINLNTD LYGSHPFYMD VRNGGTSHGV LLMNSNGMDV 240 FYTGNALTYK VIGGVLDFYF FAGTSPLDVV QQYTALIGRP VAMPYWAFGF HQCRWGYQNV 300 SDITNVVDNY NKSQIPLDVI WNDDDHMDAA KDFTLDPVNY PEHKLRPFLD RIHANGMRYV 360 VLIDPGIGIN TSYGTFQRGM ADDVFIKHDG VPFMGQVWPG AVYFPDFLNP KTVNFWADEI 420 SRFHSMVPVD GLWIDMNEVS NFCSGKCTVP TNRSCPGTGL PWECCLDCTN ITATRWXXXX 480 XXXXNITATR WDVPPYKINA SGAGAPLGFK TIATSSVHYN GILEYDAHSL YGFSQAIATH 540 KALQNLLNKR PFILTRSTFV GSGSYAAHWT GDNKATWEDL RYSISTILNF GMFGMPMVGA 600 DICGFYPDT 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01055 | Glyco_hydro_31 | 1.0e-39 | 514 | 609 | 97 | + 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 | 7.0e-49 | 525 | 609 | 85 | + 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). | ||
COG1501 | COG1501 | 5.0e-54 | 41 | 443 | 426 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 6.0e-86 | 259 | 446 | 188 | + 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 | 2.0e-91 | 278 | 442 | 169 | + 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). |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAL40352.1 | 0 | 1 | 609 | 4 | 597 | AF448201_1 putative alpha-xylosidase [Pinus pinaster] |
GenBank | ABR16166.1 | 0 | 1 | 609 | 1 | 594 | unknown [Picea sitchensis] |
RefSeq | XP_002282429.1 | 0 | 4 | 607 | 12 | 603 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002315944.1 | 0 | 24 | 607 | 31 | 607 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531635.1 | 0 | 4 | 608 | 8 | 610 | alpha-glucosidase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3w38_A | 0 | 21 | 609 | 37 | 605 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis D172aE217A MUTANT COMPLEXED WITH LACTO-N- Fucopentaose Ii |
PDB | 3w37_A | 0 | 21 | 609 | 37 | 605 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis D172aE217A MUTANT COMPLEXED WITH LACTO-N- Fucopentaose Ii |
PDB | 3ctt_A | 0 | 27 | 609 | 50 | 579 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis D172aE217A MUTANT COMPLEXED WITH LACTO-N- Fucopentaose Ii |
PDB | 2qmj_A | 0 | 27 | 609 | 50 | 579 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis D172aE217A MUTANT COMPLEXED WITH LACTO-N- Fucopentaose Ii |
PDB | 2qly_A | 0 | 27 | 609 | 50 | 579 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |