y
Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s252_60V6.1 |
Family | GH28 |
Protein Properties | Length: 478 Molecular Weight: 52235.4 Isoelectric Point: 7.0528 |
Chromosome | Chromosome/Scaffold: 252 Start: 390906 End: 393595 |
Description | Pectin lyase-like superfamily protein |
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 |
GH28 | 114 | 460 | 0 |
ANGGAQLYIPVGLWLTGSITLISHLTLFLENGATILGSEDFFDYPVIPGLPSYGRGRELPGPRFSSLINGNGLEDVIITGDNATIDGQGAVWWSAFRKKT LNYTRGHMLELIESKNILISNLTFKNSPFWTIHPVYCKNVVVKSLTILNPFDAPNTDGIDPDSSQHVCIEDCYISVGDDAISIKSGWDQFGTSFAMPSKH IKVQRILAFSRSSAGISFGSEMSGGISDVKVDGMVVTGARWGVRIKTAVGRGGYVRGISVKNIVLHSIRTAIAVMGNYGEHPDENWNRTAYPLIEDIRMK NIVGENINQAGLFLGLQESPFRDIHLANIALQVNTTKQIWNCSDVAG |
Full Sequence |
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Protein Sequence Length: 478 Download |
MTGSPGYQSL QFLLLLLSCI GSGKFWHTCM GGHSVTDDDH FATNEVLNPM SPMDLHKSIF 60 GKGKSKDRCA HTVNAWEGRP HSVSITDFGA VGDGKTLNTH AFENAIFYLR SYAANGGAQL 120 YIPVGLWLTG SITLISHLTL FLENGATILG SEDFFDYPVI PGLPSYGRGR ELPGPRFSSL 180 INGNGLEDVI ITGDNATIDG QGAVWWSAFR KKTLNYTRGH MLELIESKNI LISNLTFKNS 240 PFWTIHPVYC KNVVVKSLTI LNPFDAPNTD GIDPDSSQHV CIEDCYISVG DDAISIKSGW 300 DQFGTSFAMP SKHIKVQRIL AFSRSSAGIS FGSEMSGGIS DVKVDGMVVT GARWGVRIKT 360 AVGRGGYVRG ISVKNIVLHS IRTAIAVMGN YGEHPDENWN RTAYPLIEDI RMKNIVGENI 420 NQAGLFLGLQ ESPFRDIHLA NIALQVNTTK QIWNCSDVAG SYIFVFPQPC VEFTRKT* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN03003 | PLN03003 | 4.0e-23 | 81 | 449 | 376 | + Probable polygalacturonase At3g15720 | ||
PLN02188 | PLN02188 | 1.0e-23 | 81 | 470 | 409 | + polygalacturonase/glycoside hydrolase family protein | ||
PLN02218 | PLN02218 | 2.0e-30 | 80 | 421 | 357 | + polygalacturonase ADPG | ||
pfam00295 | Glyco_hydro_28 | 7.0e-34 | 188 | 458 | 283 | + Glycosyl hydrolases family 28. Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism. | ||
COG5434 | PGU1 | 9.0e-58 | 41 | 395 | 382 | + Endopygalactorunase [Cell envelope biogenesis, outer membrane] |
Gene Ontology | |
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GO Term | Description |
GO:0004650 | polygalacturonase activity |
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_001755533.1 | 0 | 79 | 470 | 1 | 393 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001756010.1 | 0 | 61 | 476 | 9 | 419 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001775589.1 | 0 | 1 | 476 | 4 | 479 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001779181.1 | 0 | 79 | 470 | 1 | 392 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001781065.1 | 0 | 69 | 476 | 35 | 442 | predicted protein [Physcomitrella patens subsp. patens] |
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 | 3jur_D | 2e-40 | 81 | 445 | 26 | 411 | A Chain A, The Crystal Structure Of A Hyperthermoactive Exopolygalacturonase From Thermotoga Maritima |
PDB | 3jur_C | 2e-40 | 81 | 445 | 26 | 411 | A Chain A, The Crystal Structure Of A Hyperthermoactive Exopolygalacturonase From Thermotoga Maritima |
PDB | 3jur_B | 2e-40 | 81 | 445 | 26 | 411 | A Chain A, The Crystal Structure Of A Hyperthermoactive Exopolygalacturonase From Thermotoga Maritima |
PDB | 3jur_A | 2e-40 | 81 | 445 | 26 | 411 | A Chain A, The Crystal Structure Of A Hyperthermoactive Exopolygalacturonase From Thermotoga Maritima |
PDB | 2uvf_B | 3e-20 | 78 | 419 | 152 | 531 | A Chain A, The Crystal Structure Of A Hyperthermoactive Exopolygalacturonase From Thermotoga Maritima |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
homogalacturonan degradation | RXN-2103 | EC-3.2.1.15 | polygalacturonase |