Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr1g087240.1 |
Family | GH3 |
Protein Properties | Length: 766 Molecular Weight: 82340.9 Isoelectric Point: 8.7682 |
Chromosome | Chromosome/Scaffold: 1 Start: 23440530 End: 23444010 |
Description | beta-xylosidase 2 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH3 | 69 | 316 | 0 |
AAVPRVGIKGYEWWSEALHGVSNVGPGTKFAGQFPAATSFPQVITTVASFNASLWEAIGRVASDEARAMYNGGTAGLTYWSPNVNIFRDPRWGRGQETPG EDPILAGKYAASYVRGLQGTDSSRLKVAASCKHFTAYDLDNWNGVDRFHFNAKVSKQDMEDTFNVPFRMCVKEGNVASVMCSYNQVNGVPTCADPNLLKR TIRGQWHLDGYIVSDCDSVGVFYTNQHYTSTPEEAAADAIKAGLDLDC |
Full Sequence |
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Protein Sequence Length: 766 Download |
MDSILITIVF LLLLMSSEAR DPFACDPKNT STNNFPFCKA SLPIPTRVND LIGRLTLQEK 60 VSMLVNNAAA VPRVGIKGYE WWSEALHGVS NVGPGTKFAG QFPAATSFPQ VITTVASFNA 120 SLWEAIGRVA SDEARAMYNG GTAGLTYWSP NVNIFRDPRW GRGQETPGED PILAGKYAAS 180 YVRGLQGTDS SRLKVAASCK HFTAYDLDNW NGVDRFHFNA KVSKQDMEDT FNVPFRMCVK 240 EGNVASVMCS YNQVNGVPTC ADPNLLKRTI RGQWHLDGYI VSDCDSVGVF YTNQHYTSTP 300 EEAAADAIKA GLDLDCGPFL AQHTQNAVKK GLLTETDVNG ALANTLTVQM RLGMFDGEPS 360 AQPYGNLGPT DVCTPTHQEL ALDAARQGIV LLKNTGPSLP LSTKNHQTVA VIGPNSNATV 420 TMIGNYAGIA CGYTSPLQGI GKYARTIHEP GCANVACNDD KQFGSALNAA RQADATVLVM 480 GLDQSIEAEM VDRTGLLLPG HQQDLVSKVA AASRGPTILV LMSGGPIDIT FAKNDPRIMG 540 ILWAGYPGQA GGAAIADILF GTTNPGAKLP MTWYPQGYLK NLAMTNMAMR PSSSTGYPGR 600 TYRFYNGPVV YPFGYGLSYT NFVHTLASAP KVVSVPVDGH RRGNSSNKAA IRVTHARCGK 660 LSIRLDIDVK NVGSKDGTNT LLVFSVPPTG NGHWAPQKQL VAFEKVYVPA KAQQRVRINI 720 HVCKLLSVVD KSGTRRIPMG AHSIHIGDVK HFVSLQEQKL GIIKT* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG1472 | BglX | 1.0e-53 | 66 | 452 | 393 | + Beta-glucosidase-related glycosidases [Carbohydrate transport and metabolism] | ||
pfam01915 | Glyco_hydro_3_C | 2.0e-60 | 389 | 620 | 239 | + Glycosyl hydrolase family 3 C-terminal domain. This domain is involved in catalysis and may be involved in binding beta-glucan. This domain is found associated with pfam00933. | ||
pfam00933 | Glyco_hydro_3 | 1.0e-61 | 51 | 348 | 305 | + Glycosyl hydrolase family 3 N terminal domain. | ||
PRK15098 | PRK15098 | 8.0e-83 | 106 | 720 | 673 | + beta-D-glucoside glucohydrolase; Provisional | ||
PLN03080 | PLN03080 | 0 | 1 | 756 | 782 | + Probable beta-xylosidase; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
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 | AAG10624.1 | 0 | 3 | 765 | 2 | 763 | AC022521_2 Similar to xylosidase [Arabidopsis thaliana] |
RefSeq | NP_563659.1 | 0 | 3 | 765 | 7 | 768 | BXL2 (BETA-XYLOSIDASE 2); hydrolase, hydrolyzing O-glycosyl compounds [Arabidopsis thaliana] |
RefSeq | XP_002270249.1 | 0 | 3 | 765 | 9 | 768 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002515300.1 | 0 | 16 | 765 | 21 | 768 | Beta-glucosidase, putative [Ricinus communis] |
RefSeq | XP_002519194.1 | 0 | 18 | 756 | 37 | 774 | Periplasmic beta-glucosidase precursor, 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 | 3u48_B | 0 | 106 | 720 | 91 | 696 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
PDB | 3u48_A | 0 | 106 | 720 | 91 | 696 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
PDB | 3u4a_B | 0 | 106 | 720 | 91 | 696 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
PDB | 3u4a_A | 0 | 106 | 720 | 91 | 696 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
PDB | 2x41_A | 9.99995e-41 | 47 | 746 | 3 | 705 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |