Species | Duncaniella sp001701225 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Duncaniella; Duncaniella sp001701225 | |||||||||||
CAZyme ID | MGYG000001738_00814 | |||||||||||
CAZy Family | PL4 | |||||||||||
CAZyme Description | Rhamnogalacturonate lyase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2186; End: 4069 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL4 | 25 | 568 | 5.7e-127 | 0.9909255898366606 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd10317 | RGL4_C | 1.61e-39 | 418 | 572 | 1 | 161 | C-terminal domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. |
cd10320 | RGL4_N | 1.04e-33 | 26 | 281 | 4 | 259 | N-terminal catalytic domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold; the middle and C-terminal domains are both putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. |
pfam14683 | CBM-like | 2.94e-33 | 417 | 571 | 2 | 157 | Polysaccharide lyase family 4, domain III. CBM-like is domain III of rhamnogalacturonan lyase (RG-lyase). The full-length protein specifically recognizes and cleaves alpha-1,4 glycosidic bonds between l-rhamnose and d-galacturonic acids in the backbone of rhamnogalacturonan-I, a major component of the plant cell wall polysaccharide, pectin. This domain possesses a jelly roll beta-sandwich fold structurally homologous to carbohydrate binding modules (CBMs), and it carries two sulfate ions and a hexa-coordinated calcium ion. |
cd10316 | RGL4_M | 1.87e-17 | 315 | 406 | 1 | 92 | Middle domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle domain represented by this model and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. |
pfam14686 | fn3_3 | 8.58e-09 | 347 | 381 | 20 | 54 | Polysaccharide lyase family 4, domain II. FnIII-like is domain II of rhamnogalacturonan lyase (RG-lyase). The full-length protein specifically recognizes and cleaves alpha-1,4 glycosidic bonds between l-rhamnose and d-galacturonic acids in the backbone of rhamnogalacturonan-I, a major component of the plant cell wall polysaccharide, pectin. This domain displays an immunoglobulin-like or more specifically Fibronectin-III type fold and shows highest structural similarity to the C-terminal beta-sandwich subdomain of the pro-hormone/propeptide processing enzyme carboxypeptidase gp180 from duck. It serves to assist in producing the deep pocket, with domain III, into which the substrate fits. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BBH93641.1 | 2.80e-130 | 14 | 583 | 39 | 591 |
BAV08848.1 | 6.33e-97 | 13 | 574 | 42 | 596 |
APC39134.1 | 5.10e-93 | 29 | 573 | 11 | 563 |
AUH06334.1 | 2.67e-90 | 27 | 576 | 36 | 581 |
AUH02012.1 | 2.67e-90 | 27 | 576 | 36 | 581 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8RJP2 | 5.01e-90 | 26 | 571 | 32 | 573 | Rhamnogalacturonate lyase OS=Dickeya dadantii (strain 3937) OX=198628 GN=rhiE PE=1 SV=1 |
Q2U5P7 | 6.33e-20 | 94 | 573 | 109 | 655 | Probable rhamnogalacturonate lyase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=rglC PE=3 SV=1 |
A5ABH4 | 3.47e-19 | 108 | 553 | 120 | 633 | Probable rhamnogalacturonate lyase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=rglB PE=3 SV=1 |
Q5B5P1 | 1.91e-18 | 179 | 556 | 187 | 630 | Probable rhamnogalacturonate lyase C OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=rglC PE=3 SV=1 |
Q2U0Q1 | 3.87e-09 | 109 | 571 | 99 | 526 | Probable rhamnogalacturonate lyase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=rglA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000550 | 0.998043 | 0.000728 | 0.000235 | 0.000218 | 0.000201 |
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