Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; | |||||||||||
CAZyme ID | MGYG000004043_00348 | |||||||||||
CAZy Family | PL4 | |||||||||||
CAZyme Description | Rhamnogalacturonate lyase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 19897; End: 21786 Strand: - |
Family | Start | End | Evalue | family coverage |
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PL4 | 34 | 571 | 1.1e-126 | 0.9800362976406534 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd10317 | RGL4_C | 3.70e-33 | 421 | 575 | 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 | 3.80e-33 | 31 | 283 | 6 | 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 | 1.25e-27 | 420 | 574 | 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 | 3.27e-17 | 316 | 408 | 1 | 91 | 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 | 4.39e-09 | 352 | 398 | 23 | 67 | 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 | 8.54e-110 | 16 | 575 | 39 | 580 |
BAV08848.1 | 1.52e-94 | 1 | 577 | 29 | 596 |
APC39134.1 | 1.80e-94 | 71 | 577 | 59 | 564 |
AYH46991.1 | 3.99e-87 | 36 | 579 | 37 | 575 |
AIR69111.1 | 7.14e-86 | 36 | 579 | 31 | 569 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8RJP2 | 2.60e-85 | 36 | 579 | 39 | 577 | Rhamnogalacturonate lyase OS=Dickeya dadantii (strain 3937) OX=198628 GN=rhiE PE=1 SV=1 |
Q0C7K7 | 3.22e-19 | 32 | 492 | 27 | 526 | Probable rhamnogalacturonate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=rglB PE=3 SV=1 |
Q2U5P7 | 9.87e-18 | 87 | 558 | 92 | 635 | Probable rhamnogalacturonate lyase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=rglC PE=3 SV=1 |
Q5AZ85 | 1.15e-16 | 165 | 498 | 175 | 555 | Rhamnogalacturonate lyase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=rglB PE=2 SV=2 |
Q5B5P1 | 1.62e-16 | 7 | 558 | 4 | 631 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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0.000307 | 0.998954 | 0.000196 | 0.000179 | 0.000173 | 0.000157 |
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