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CAZyme Information: MGYG000002407_02532

You are here: Home > Sequence: MGYG000002407_02532

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 Cohnella sp900169535
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Cohnella; Cohnella sp900169535
CAZyme ID MGYG000002407_02532
CAZy Family CBM35
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2135 MGYG000002407_18|CGC11 225772.34 4.6151
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002407 6325359 Isolate not provided not provided
Gene Location Start: 692711;  End: 699118  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002407_02532.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH87 973 1521 7.8e-166 0.8375209380234506
CBM35 876 998 3.4e-19 0.9831932773109243

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14490 CBM6-CBM35-CBM36_like_1 8.73e-59 1008 1161 1 155
uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily. Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules.
cd04083 CBM35_Lmo2446-like 9.85e-21 873 998 1 125
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.
cd04082 CBM35_pectate_lyase-like 9.82e-15 875 998 3 124
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.
pfam12708 Pectate_lyase_3 1.41e-10 1175 1291 1 135
Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.
cd04081 CBM35_galactosidase-like 4.64e-10 874 998 2 125
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AYQ75285.1 0.0 55 2127 178 2082
QGG57009.1 1.36e-298 37 2131 34 2085
ASS66060.2 4.19e-296 5 2135 4 2072
QJC52623.1 4.13e-279 46 2131 39 2079
QJD83813.1 2.01e-278 49 2133 179 2210

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7C7D_A 4.33e-78 1008 1535 54 569
Crystalstructure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3 [Streptomyces thermodiastaticus],7C7D_B Crystal structure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3 [Streptomyces thermodiastaticus]
5ZRU_A 9.59e-56 1000 1452 5 481
ChainA, Alpha-1,3-glucanase [Niallia circulans],5ZRU_C Chain C, Alpha-1,3-glucanase [Niallia circulans]
6K0M_A 7.95e-34 1007 1411 13 417
Catalyticdomain of GH87 alpha-1,3-glucanase from Paenibacillus glycanilyticus FH11 [Paenibacillus glycanilyticus],6K0N_A Catalytic domain of GH87 alpha-1,3-glucanase in complex with nigerose [Paenibacillus glycanilyticus]
6K0P_A 8.09e-33 1007 1411 13 417
Catalyticdomain of GH87 alpha-1,3-glucanase D1045A in complex with nigerose [Paenibacillus glycanilyticus]
6K0S_A 8.09e-33 1007 1411 13 417
Catalyticdomain of GH87 alpha-1,3-glucanase D1069A in complex with nigerose [Paenibacillus glycanilyticus],6K0V_A Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_B Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_C Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_D Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P38536 1.13e-21 1949 2127 1680 1855
Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P38535 2.54e-21 1944 2131 901 1085
Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
C6CRV0 7.74e-20 1908 2126 1242 1458
Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P19424 7.98e-12 1951 2127 41 214
Endoglucanase OS=Bacillus sp. (strain KSM-635) OX=1415 PE=1 SV=1
P36917 4.37e-09 1951 2051 1056 1154
Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000407 0.159051 0.839852 0.000367 0.000200 0.000107

TMHMM  Annotations      download full data without filtering help

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