y
Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s406_3V6.1 |
Family | GH3 |
Protein Properties | Length: 783 Molecular Weight: 85232 Isoelectric Point: 5.3498 |
Chromosome | Chromosome/Scaffold: 406 Start: 69784 End: 72804 |
Description | beta-D-xylosidase 4 |
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 | 83 | 324 | 0 |
AIPRLSIPAYEWWQEGLHGVAHVSFGGSLPRATSFPLPILTTASFNKDLWNQIGQVVSTEARAFYNDGIAGLTYWSPVINIARDPRWGRIQETSGEDPYT TSAYATHFVQGMQEGDANSKRLKLSACCKHFTAYDVDNWEGIDRYHFDAKANLADTYNPPFQSCVQEGRSASLMCSYNKVNGVPTCANYDFLENTVRRAW GLNGYIVSDCDSVLVMHESTNYAPTTEDAAADALNAGLDLNC |
Full Sequence |
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Protein Sequence Length: 783 Download |
MARKIETLFP LQGRMCWLII ILLLQPFHKG AALEYACNFD KDDNLKSMRF CDTSLSDEIR 60 VFDLVSRLTL EEKVTQLVNT ASAIPRLSIP AYEWWQEGLH GVAHVSFGGS LPRATSFPLP 120 ILTTASFNKD LWNQIGQVVS TEARAFYNDG IAGLTYWSPV INIARDPRWG RIQETSGEDP 180 YTTSAYATHF VQGMQEGDAN SKRLKLSACC KHFTAYDVDN WEGIDRYHFD AKANLADTYN 240 PPFQSCVQEG RSASLMCSYN KVNGVPTCAN YDFLENTVRR AWGLNGYIVS DCDSVLVMHE 300 STNYAPTTED AAADALNAGL DLNCGDYLAS YTEGAVAMGK VNASRVDNAV YNVFLVRMRL 360 GMFDGNPANQ EFGNIGVADV CTPAHQELAV EAARQGIVLL KNDGNILPLS KNINTAVIGP 420 NANATHTMLG NYEGIPCQYI TPLQGLVKFG SGDYHKVWFS EGCVNTACQQ DDQISSAVST 480 AAVADAVVLV VGLSQVQESE ALDRTSLLLP GYQQTLIDEV AGAAAGRPVV LVLMCAGPVD 540 INFAKNDKRI QSILWVGYPG QSGGQAIAEV IFGAHNPGGK LPMSWYPEDY TKISMTNMNM 600 RPDSRSNYPG RTYRFYTGEK IYDFGYGLSY TEYKHSFALA PTTVMTPSIH SQLCDPHQTS 660 AGSSLPCSQA HQETCSSSNF DVHINVENIG AMAGNHTLLL FFTAPSAGKN GTPLKQLAAF 720 DSVYIRSGSQ EKVVLTLNPC QHLGTVAEDG TRMLEAGNHI LSVGDAKHSL SVLFSDTSGA 780 RY* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00933 | Glyco_hydro_3 | 3.0e-52 | 69 | 353 | 315 | + Glycosyl hydrolase family 3 N terminal domain. | ||
pfam01915 | Glyco_hydro_3_C | 1.0e-53 | 397 | 631 | 238 | + 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. | ||
COG1472 | BglX | 6.0e-57 | 42 | 446 | 424 | + Beta-glucosidase-related glycosidases [Carbohydrate transport and metabolism] | ||
PRK15098 | PRK15098 | 8.0e-78 | 61 | 750 | 781 | + beta-D-glucoside glucohydrolase; Provisional | ||
PLN03080 | PLN03080 | 0 | 50 | 772 | 743 | + 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 |
RefSeq | XP_001775759.1 | 0 | 18 | 772 | 3 | 774 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001784462.1 | 0 | 48 | 782 | 1 | 726 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002270249.1 | 0 | 18 | 772 | 11 | 758 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002316021.1 | 0 | 35 | 772 | 28 | 759 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002515300.1 | 0 | 31 | 772 | 23 | 758 | Beta-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 | 3u48_B | 0 | 73 | 771 | 61 | 729 | A Chain A, Pectin Methylesterase Pema From Erwinia Chrysanthemi |
PDB | 3u48_A | 0 | 73 | 771 | 61 | 729 | A Chain A, Pectin Methylesterase Pema From Erwinia Chrysanthemi |
PDB | 3u4a_B | 0 | 73 | 771 | 61 | 729 | A Chain A, Pectin Methylesterase Pema From Erwinia Chrysanthemi |
PDB | 3u4a_A | 0 | 73 | 771 | 61 | 729 | A Chain A, Pectin Methylesterase Pema From Erwinia Chrysanthemi |
PDB | 2x41_A | 6.99949e-42 | 60 | 772 | 3 | 707 | A Chain A, Pectin Methylesterase Pema From Erwinia Chrysanthemi |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
(1,4)-β-xylan degradation | 3.2.1.37-RXN | EC-3.2.1.37 | xylan 1,4-β-xylosidase |