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CAZyme Information: MGYG000003514_01516

You are here: Home > Sequence: MGYG000003514_01516

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Fibrobacter_A intestinalis
Lineage Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae; Fibrobacter_A; Fibrobacter_A intestinalis
CAZyme ID MGYG000003514_01516
CAZy Family PL11
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
930 MGYG000003514_62|CGC1 101520.4 4.8738
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003514 2933446 MAG Fiji Oceania
Gene Location Start: 58547;  End: 61339  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003514_01516.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL11 21 605 1.9e-262 0.9653465346534653

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10318 RGL11 0.0 24 587 1 564
Rhamnogalacturonan lyase of the polysaccharide lyase family 11. The rhamnogalacturonan lyase of the polysaccharide lyase family 11 (RGL11) cleaves glycoside bonds in polygalacturonan as well as RG (rhamnogalacturonan) type-I through a beta-elimination reaction. Functionally characterized members of this family, YesW and YesX from Bacillus subtilis, cleave glycoside bonds between rhamnose and galacturonic acid residues in the RG-I region of plant cell wall pectin. YesW and YesX work synergistically, with YesW cleaving the glycoside bond of the RG chain endolytically, and YesX converting the resultant oligosaccharides through an exotype reaction. This domain is sometimes found in architectures with non-catalytic carbohydrate-binding modules (CBMs). There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain through a beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
pfam18370 RGI_lyase 1.76e-45 22 107 1 86
Rhamnogalacturonan I lyases beta-sheet domain. This is the beta-sheet domain found in rhamnogalacturonan (RG) lyases, which are responsible for an initial cleavage of the RG type I (RG-I) region of plant cell wall pectin. Polysaccharide lyase family 11 carrying this domain, such as YesW (EC:4.2.2.23) and YesX (EC:4.2.2.24), cleave glycoside bonds between rhamnose and galacturonic acid residues in RG-I through a beta-elimination reaction. Other family members carrying this domain are hemagglutinin A, lysine gingipain (Kgp) and Chitinase C (EC:3.2.1.14).
cd04082 CBM35_pectate_lyase-like 1.12e-23 722 824 16 120
Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. This family includes carbohydrate binding module family 35 (CBM35) domains that are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. Included in this family are CBM35s of pectate lyases, including pectate lyase 10A from Cellvibrio japonicas, these enzymes release delta-4,5-anhydrogalaturonic acid (delta4,5-GalA) from pectin, thus identifying a signature molecule for plant cell wall degradation. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. Some CBM35s bind their ligands in a calcium-dependent manner, especially those binding uronic acids.
cd04081 CBM35_galactosidase-like 7.95e-06 758 824 55 121
Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases.
cd04083 CBM35_Lmo2446-like 7.90e-05 732 824 30 121
Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADL25062.1 0.0 1 693 1 699
ACX75592.1 0.0 1 693 1 699
QUT73808.1 9.56e-253 25 693 26 710
QLG37185.1 3.42e-240 18 604 38 624
APO48084.1 7.53e-240 18 604 21 607

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2Z8R_A 2.87e-239 20 599 1 580
Crystalstructure of rhamnogalacturonan lyase YesW at 1.40 A resolution [Bacillus subtilis],2Z8R_B Crystal structure of rhamnogalacturonan lyase YesW at 1.40 A resolution [Bacillus subtilis],2Z8S_A Crystal structure of rhamnogalacturonan lyase YesW complexed with digalacturonic acid [Bacillus subtilis],2Z8S_B Crystal structure of rhamnogalacturonan lyase YesW complexed with digalacturonic acid [Bacillus subtilis],2ZUX_A Crystal structure of rhamnogalacturonan lyase YesW complexed with rhamnose [Bacillus subtilis],2ZUX_B Crystal structure of rhamnogalacturonan lyase YesW complexed with rhamnose [Bacillus subtilis]
4CAG_A 1.95e-238 18 592 5 578
Bacilluslicheniformis Rhamnogalacturonan Lyase PL11 [Bacillus licheniformis]
2ZUY_A 5.57e-220 22 604 6 606
Crystalstructure of exotype rhamnogalacturonan lyase YesX [Bacillus subtilis]
2W47_A 6.73e-15 722 824 20 124
ChainA, Lipolytic Enzyme, G-d-s-l [Acetivibrio thermocellus]
2W1W_A 7.08e-15 722 824 20 124
ChainA, LIPOLYTIC ENZYME, G-D-S-L [Acetivibrio thermocellus],2W1W_B Chain B, LIPOLYTIC ENZYME, G-D-S-L [Acetivibrio thermocellus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31526 4.38e-238 20 599 38 617
Rhamnogalacturonan endolyase YesW OS=Bacillus subtilis (strain 168) OX=224308 GN=yesW PE=1 SV=1
O31527 2.31e-219 22 604 6 606
Rhamnogalacturonan exolyase YesX OS=Bacillus subtilis (strain 168) OX=224308 GN=yesX PE=1 SV=1
P23030 2.36e-11 719 837 176 297
Endo-1,4-beta-xylanase B OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=xynB PE=1 SV=2
P23031 2.43e-11 719 837 176 297
Alpha-L-arabinofuranosidase C OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=xynC PE=1 SV=2
Q56F26 7.46e-11 719 825 921 1029
Exo-beta-D-glucosaminidase OS=Amycolatopsis orientalis OX=31958 GN=csxA PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000194 0.999207 0.000157 0.000149 0.000142 0.000129

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003514_01516.