y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma09g00850.1 |
Family | PL1 |
Protein Properties | Length: 398 Molecular Weight: 43586.5 Isoelectric Point: 6.2371 |
Chromosome | Chromosome/Scaffold: 09 Start: 461753 End: 463683 |
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 |
PL1 | 119 | 318 | 0 |
ITFAKDMVIRLKNELMVNSYKTIDGRGAKVEIANGACITIQGVCHVIVHGISIHDCEPGKGGMVRSSPEHVGYREGSDGDAISIFASSNVWIDHCFLARC TDGLIDVIHASTAVTISNNYFTQHDKVMLLGHSDEYTADKVMRVTVAFNRFASGLIERMPRVRFGYAHVVNNLYDEWLMYAIGGSADPTIFSEGNYFTAS |
Full Sequence |
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Protein Sequence Length: 398 Download |
MATLTTLLVT LYFIVPALAS TPNRDSTKEF NALSPISSYI NKTPEDVVIM NTIDSCWRAK 60 TNWASNRKAL ADCAIGFGKE AIGGKFGDIY EVTDPSDDPV DPKPGTLRYG AIQTEPLWIT 120 FAKDMVIRLK NELMVNSYKT IDGRGAKVEI ANGACITIQG VCHVIVHGIS IHDCEPGKGG 180 MVRSSPEHVG YREGSDGDAI SIFASSNVWI DHCFLARCTD GLIDVIHAST AVTISNNYFT 240 QHDKVMLLGH SDEYTADKVM RVTVAFNRFA SGLIERMPRV RFGYAHVVNN LYDEWLMYAI 300 GGSADPTIFS EGNYFTASND SAAKQVTKRE SSEKWNNWKW RSFRDEFING AYFVPSGYGS 360 CTPIYSAAQS FIAAQASMVP LLTLNAGPLN CVVDKAC* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06358 | PBP1_NHase | 0.008 | 264 | 329 | 68 | + Type I periplasmic-binding protein of the nitrile hydratase (NHase) system that selectively converts nitriles to corresponding amides. This group includes the type I periplasmic-binding protein of the nitrile hydratase (NHase) system that selectively converts nitriles to corresponding amides, which are subsequently converted by amidases to yield free carboxylic acids and ammonia. NHases from bacteria and fungi have been purified and characterized. In Rhodococcus sp., the nitrile hydratase operon consists of six genes encoding NHase regulator 2, NHase regulator 1, amidase, NHase alpha subunit, NHase beta subunit, and NHase activator. The operon produces a constitutive hydratase that has a broad substrate spectrum: aliphatic and aromatic nitriles, mononitriles and dinitriles, hydroxynitriles and amino-nitriles, and a constitutive amidase of equally low substrate specificity. NHases are metalloenzymes containing either cobalt or iron, and therefore can be classified into two subgroups: ferric NHases and cobalt NHases. | ||
COG3866 | PelB | 4.0e-29 | 130 | 315 | 198 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
pfam00544 | Pec_lyase_C | 1.0e-67 | 130 | 315 | 208 | + Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue. | ||
smart00656 | Amb_all | 1.0e-82 | 124 | 319 | 207 | + Amb_all domain. |
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 | NP_193939.1 | 0 | 1 | 397 | 3 | 393 | pectate lyase family protein [Arabidopsis thaliana] |
RefSeq | XP_002263615.1 | 0 | 2 | 397 | 5 | 397 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002317128.1 | 0 | 8 | 397 | 7 | 382 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317132.1 | 0 | 1 | 397 | 1 | 393 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002518442.1 | 0 | 35 | 397 | 30 | 390 | Pectate lyase 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 | 1pxz_B | 0 | 51 | 387 | 2 | 343 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 1pxz_A | 0 | 51 | 387 | 2 | 343 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 3zsc_A | 6e-21 | 125 | 317 | 56 | 248 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1vbl_A | 8e-19 | 128 | 316 | 121 | 331 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
PDB | 1pcl_A | 1e-18 | 128 | 379 | 71 | 346 | A Chain A, Unusual Structural Features In The Parallel Beta-Helix In Pectate Lyases |