Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10435316g0010 |
Family | GH31 |
Protein Properties | Length: 949 Molecular Weight: 107248 Isoelectric Point: 8.0864 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH31 | 451 | 925 | 0 |
HGCSPTELIERYTETIGRMPELPKWILSGAVVGMQGGTESVQHVWGQLKKYNVPISAFWLQDWVGQRRTSIGSQLWWNWEVDTIHYPGWKQLVEELHSNG ILTMTYCNPCLVPTDEKANRKRNLFEEANKLGLFVKNKSGSTYMIPNTTFNVGMLDLTNPAARSWFKGILHEMVETGIKGWMADFGEGLPLDACLFSGED PISAHNRYPSLWAEVNREFVEEWKAKQQENLRKVETVNEGLDEEQLVFFMRAGFRETPKWATLFWEGDQMTSWQRNDGIKSAIVGLLSGGLSGFALNHSD IGGYCAINLPFSPYRRSEELLLRWMEMNSFTTIFRTHEGNSPSANKQFYSNDRTLSHFARFAKVYKAWEFFRIQLVKEAASKGLPVVRHLFLHYPHDKYV QKLTFQQFLVGSEVLVVPVVDKGRNQVKAYFPAGEDWQHIWTGRIFSPPMSSGMEAWIYAPLGYPAVFVKVGSLI |
Full Sequence |
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Protein Sequence Length: 949 Download |
MPNNIRVSRR DDRRLNNPFP RCPRGIGFIK GNLFITEHQI RPLQAFDIGT NFVLKCELNN 60 GGTGFVSVFH RSEPARSLWS TVPGVAFISA ALSSPFVEES RGSVAIHDKV RTLCSHQTVE 120 NISVIYPSKT SNEFGEQSEN EICPLLAGTQ SRNGFLKGVH LGNLVGPIVV LTGCLYSTSK 180 VAREQLEVFL DNKNQSEGPF YTSKSAEEGC CCPCFFKSRP VGVRYYLSFV EKSDHDLGFT 240 VNLEDPILLS SEIPCYSHIE TSKNGLKTAL NETQSTPHGI SVHSDTGPDF RTNNVLRKRA 300 SSLLKKARRQ LNKIQMFEGT NTQKFPGKKK LKCVPAFNRI ALTIFSERDE KFYGFGEQFS 360 YMDMKGKRVP ILVQEQGLGR GDQPITAAAN LVAYRSGGDW STTYAPSPFY ITSSMKCLYL 420 EGHDHSVFDL IMDDRVQIQM YGTSMQGRIL HGCSPTELIE RYTETIGRMP ELPKWILSGA 480 VVGMQGGTES VQHVWGQLKK YNVPISAFWL QDWVGQRRTS IGSQLWWNWE VDTIHYPGWK 540 QLVEELHSNG ILTMTYCNPC LVPTDEKANR KRNLFEEANK LGLFVKNKSG STYMIPNTTF 600 NVGMLDLTNP AARSWFKGIL HEMVETGIKG WMADFGEGLP LDACLFSGED PISAHNRYPS 660 LWAEVNREFV EEWKAKQQEN LRKVETVNEG LDEEQLVFFM RAGFRETPKW ATLFWEGDQM 720 TSWQRNDGIK SAIVGLLSGG LSGFALNHSD IGGYCAINLP FSPYRRSEEL LLRWMEMNSF 780 TTIFRTHEGN SPSANKQFYS NDRTLSHFAR FAKVYKAWEF FRIQLVKEAA SKGLPVVRHL 840 FLHYPHDKYV QKLTFQQFLV GSEVLVVPVV DKGRNQVKAY FPAGEDWQHI WTGRIFSPPM 900 SSGMEAWIYA PLGYPAVFVK VGSLIGTTFM QNLLDLGVCM MFPPPAEDN |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
cd06589 | GH31 | 3.0e-29 | 467 | 809 | 351 | + The enzymes of glycosyl hydrolase family 31 (GH31) 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. |
pfam01055 | Glyco_hydro_31 | 2.0e-66 | 452 | 925 | 490 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. |
COG1501 | COG1501 | 9.0e-72 | 336 | 925 | 612 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] |
cd06594 | GH31_glucosidase_YihQ | 1.0e-158 | 467 | 809 | 344 | + YihQ is a bacterial alpha-glucosidase with a conserved glycosyl hydrolase family 31 (GH31) domain that catalyzes the release of an alpha-glucosyl residue from the non-reducing end of alpha-glucoside substrates such as alpha-glucosyl fluoride. Orthologs of YihQ that have not yet been functionally characterized are present in plants and fungi. YihQ has sequence similarity to other GH31 enzymes such as CtsZ, a 6-alpha-glucosyltransferase from Bacillus globisporus, and YicI, an alpha-xylosidase from Echerichia coli. In bacteria, YihQ (along with YihO) is important for bacterial O-antigen capsule assembly and translocation. |
PRK10426 | PRK10426 | 0 | 338 | 923 | 589 | + alpha-glucosidase; Provisional |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAD81144.1 | 0 | 6 | 938 | 15 | 931 | alpha-glucosidase -like [Oryza sativa Japonica Group] |
EMBL | CBI30134.1 | 0 | 5 | 938 | 38 | 904 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002266626.1 | 0 | 5 | 938 | 4 | 870 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002308887.1 | 0 | 5 | 938 | 4 | 874 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002522166.1 | 0 | 5 | 938 | 4 | 873 | alpha-xylosidase, 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 | 4kmq_A | 3e-31 | 338 | 925 | 257 | 823 | A Chain A, X-Ray Crystal Structure Of The Endo-Beta-N- Acetylglucosaminidase From Arthrobacter Protophormiae E173q Mutant Reveals A Tim Barrel Catalytic Domain And Two Ancillary Domains |
PDB | 1we5_F | 5e-29 | 337 | 891 | 151 | 639 | A Chain A, Crystal Structure Of Alpha-Xylosidase From Escherichia Coli |
PDB | 1we5_E | 5e-29 | 337 | 891 | 151 | 639 | A Chain A, Crystal Structure Of Alpha-Xylosidase From Escherichia Coli |
PDB | 1we5_D | 5e-29 | 337 | 891 | 151 | 639 | A Chain A, Crystal Structure Of Alpha-Xylosidase From Escherichia Coli |
PDB | 1we5_C | 5e-29 | 337 | 891 | 151 | 639 | A Chain A, Crystal Structure Of Alpha-Xylosidase From Escherichia Coli |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EX420945 | 228 | 722 | 949 | 0 |
DY975686 | 288 | 536 | 823 | 0 |
CO467346 | 270 | 395 | 663 | 0 |
JG471720 | 275 | 437 | 711 | 0 |
CN524335 | 246 | 437 | 682 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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