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CAZyme Information: MGYG000001375_01895

You are here: Home > Sequence: MGYG000001375_01895

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 Ruminococcus_F champanellensis
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_F; Ruminococcus_F champanellensis
CAZyme ID MGYG000001375_01895
CAZy Family CE12
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
996 MGYG000001375_1|CGC27 107224.58 4.6273
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001375 2513436 Isolate not provided not provided
Gene Location Start: 2048271;  End: 2051261  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.1.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE12 773 982 6.2e-65 0.9904761904761905
CE12 189 380 4.5e-47 0.9904761904761905
CBM35 627 748 9.7e-24 0.9915966386554622
CBM13 397 560 8.4e-20 0.7872340425531915

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd01821 Rhamnogalacturan_acetylesterase_like 1.65e-65 772 983 1 198
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
cd04082 CBM35_pectate_lyase-like 6.98e-49 626 748 2 124
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.
cd01821 Rhamnogalacturan_acetylesterase_like 3.22e-44 188 379 1 196
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
cd04083 CBM35_Lmo2446-like 4.24e-20 625 748 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.
COG2755 TesA 3.56e-18 772 991 9 216
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL17979.1 0.0 1 996 1 996
ADU21040.1 1.36e-263 4 996 2 1020
AEV69827.1 8.13e-223 34 996 27 843
ABN54336.1 6.94e-221 34 988 28 822
ANV75445.1 7.78e-220 34 988 28 822

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2O14_A 5.51e-115 35 381 10 359
X-RayCrystal Structure of Protein YXIM_BACsu from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR595 [Bacillus subtilis]
2W47_A 8.46e-30 627 748 7 128
ChainA, Lipolytic Enzyme, G-d-s-l [Acetivibrio thermocellus]
2W1W_A 8.98e-30 627 748 7 128
ChainA, LIPOLYTIC ENZYME, G-D-S-L [Acetivibrio thermocellus],2W1W_B Chain B, LIPOLYTIC ENZYME, G-D-S-L [Acetivibrio thermocellus]
2VZP_A 4.94e-25 627 748 6 127
AtomicResolution Structure of the C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis],2VZP_B Atomic Resolution Structure of the C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis],2VZQ_A C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA in complex with digalacturonic acid [Amycolatopsis orientalis],2VZQ_B C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA in complex with digalacturonic acid [Amycolatopsis orientalis],2VZR_A C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA in complex with glucuronic acid [Amycolatopsis orientalis],2VZR_B C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA in complex with glucuronic acid [Amycolatopsis orientalis]
2VZU_A 1.68e-21 627 748 911 1032
Complexof Amycolatopsis orientalis exo-chitosanase CsxA D469A with PNP-beta-D-glucosamine [Amycolatopsis orientalis],2VZU_B Complex of Amycolatopsis orientalis exo-chitosanase CsxA D469A with PNP-beta-D-glucosamine [Amycolatopsis orientalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P42304 5.46e-119 21 381 16 374
Uncharacterized esterase YxiM OS=Bacillus subtilis (strain 168) OX=224308 GN=yxiM PE=1 SV=2
O31528 7.35e-46 774 995 5 213
Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
O31523 3.93e-28 774 994 8 222
Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
Q56F26 9.22e-21 627 748 911 1032
Exo-beta-D-glucosaminidase OS=Amycolatopsis orientalis OX=31958 GN=csxA PE=1 SV=2
Q00017 3.01e-20 767 983 13 229
Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 PE=1 SV=1

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
0.000884 0.630549 0.367556 0.000393 0.000318 0.000266

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001375_01895.