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CAZyme Information: MGYG000002290_03324

You are here: Home > Sequence: MGYG000002290_03324

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 Sellimonas sp002161525
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Sellimonas; Sellimonas sp002161525
CAZyme ID MGYG000002290_03324
CAZy Family CE4
CAZyme Description Peptidoglycan-N-acetylglucosamine deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
480 MGYG000002290_29|CGC1 54243 5.1347
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002290 3837069 Isolate China Asia
Gene Location Start: 13712;  End: 15154  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002290_03324.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE4 272 401 2.1e-28 0.9

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10944 CE4_SmPgdA_like 1.67e-86 274 465 1 188
Catalytic NodB homology domain of Streptococcus mutans polysaccharide deacetylase PgdA, Bacillus subtilis YheN, and similar proteins. This family is represented by a putative polysaccharide deacetylase PgdA from the oral pathogen Streptococcus mutans (SmPgdA) and Bacillus subtilis YheN (BsYheN), which are members of the carbohydrate esterase 4 (CE4) superfamily. SmPgdA is an extracellular metal-dependent polysaccharide deacetylase with a typical CE4 fold, with metal bound to a His-His-Asp triad. It possesses de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. SmPgdA plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin, an essential component of the innate immune system, most likely through deacetylation of an as-yet-unidentified polysaccharide. SmPgdA shows significant homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae (SpPgdA) and Listeria monocytogenes (LmPgdA), both of which are involved in the bacterial defense mechanism against human mucosal lysozyme. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. The biological function of BsYheN is still unknown. This family also includes many uncharacterized polysaccharide deacetylases mainly found in bacteria.
cd10917 CE4_NodB_like_6s_7s 3.61e-48 274 458 1 171
Catalytic NodB homology domain of rhizobial NodB-like proteins. This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.
COG0726 CDA1 1.04e-33 269 465 60 251
Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
cd10951 CE4_ClCDA_like 6.92e-33 276 464 10 194
Catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase and similar proteins. This family is represented by the chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41) from Colletotrichum lindemuthianum (also known as Glomerella lindemuthiana), which is a member of the carbohydrate esterase 4 (CE4) superfamily. ClCDA catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. It consists of a single catalytic domain similar to the deformed (alpha/beta)8 barrel fold adopted by other CE4 esterases, which encompasses a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine), to carry out acid/base catalysis. It possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity. Unlike its bacterial homologs, ClCDA contains two intramolecular disulfide bonds that may add stability to this secreted protein. The family also includes many uncharacterized deacetylases and hypothetical proteins mainly from eukaryotes, which show high sequence similarity to ClCDA.
cd10948 CE4_BsPdaA_like 2.68e-31 272 467 38 223
Catalytic NodB homology domain of Bacillus subtilis polysaccharide deacetylase PdaA, and its bacterial homologs. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by Bacillus subtilis pdaA gene encoding polysaccharide deacetylase BsPdaA, which is a member of the carbohydrate esterase 4 (CE4) superfamily. BsPdaA deacetylates peptidoglycan N-acetylmuramic acid (MurNAc) residues to facilitate the formation of muramic delta-lactam, which is required for recognition of germination lytic enzymes. BsPdaA deficiency leads to the absence of muramic delta-lactam residues in the spore cortex. Like other CE4 esterases, BsPdaA consists of a single catalytic NodB homology domain that appears to adopt a deformed (beta/alpha)8 barrel fold with a putative substrate binding groove harboring the majority of the conserved residues. It utilizes a general acid/base catalytic mechanism involving a tetrahedral transition intermediate, where a water molecule functions as the nucleophile tightly associated to the zinc cofactor.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL27152.1 4.71e-176 42 480 72 512
AMK53201.1 1.79e-148 49 480 41 473
QPS12920.1 1.77e-127 28 480 16 474
QPS12071.1 8.87e-117 60 480 47 475
QUN14574.1 3.04e-113 169 480 3 320

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5JMU_A 4.10e-50 274 480 20 226
ChainA, Peptidoglycan N-acetylglucosamine deacetylase [[Eubacterium] rectale ATCC 33656]
5NC6_A 1.63e-29 274 474 1 196
Crystalstructure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (E)-N-hydroxy-3-(naphthalen-1-yl)prop-2-enamide [Bacillus cereus]
5N1J_A 1.67e-29 274 474 2 197
Crystalstructure of the polysaccharide deacetylase Bc1974 from Bacillus cereus [Bacillus cereus],5N1J_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus [Bacillus cereus],5N1J_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus [Bacillus cereus],5N1J_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus [Bacillus cereus],5N1P_A Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with N-hydroxynaphthalene-1-carboxamide [Bacillus cereus],5N1P_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with N-hydroxynaphthalene-1-carboxamide [Bacillus cereus],5N1P_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with N-hydroxynaphthalene-1-carboxamide [Bacillus cereus],5N1P_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with N-hydroxynaphthalene-1-carboxamide [Bacillus cereus]
5NC9_A 2.43e-29 243 474 1 238
Crystalstructure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NC9_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NC9_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NC9_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NCD_A Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NCD_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NCD_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NCD_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NEK_A Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEK_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEK_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEK_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEL_A Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus],5NEL_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus],5NEL_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus],5NEL_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus]
5NC6_B 4.39e-29 243 474 27 264
Crystalstructure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (E)-N-hydroxy-3-(naphthalen-1-yl)prop-2-enamide [Bacillus cereus],5NC6_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (E)-N-hydroxy-3-(naphthalen-1-yl)prop-2-enamide [Bacillus cereus],5NC6_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (E)-N-hydroxy-3-(naphthalen-1-yl)prop-2-enamide [Bacillus cereus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q81EJ6 2.40e-28 243 474 27 264
Peptidoglycan-N-acetylglucosamine deacetylase BC_1974 OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=BC_1974 PE=1 SV=1
O07596 1.98e-27 273 476 84 281
Putative polysaccharide deacetylase YheN OS=Bacillus subtilis (strain 168) OX=224308 GN=yheN PE=3 SV=1
Q81AF4 1.17e-18 273 477 21 213
Peptidoglycan-N-acetylglucosamine deacetylase BC_3618 OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=BC_3618 PE=1 SV=1
Q8DP63 4.29e-18 52 464 31 441
Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1
P83513 8.29e-15 273 464 401 577
Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.999958 0.000073 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
21 43