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CAZyme Information: MGYG000001338_00028

You are here: Home > Sequence: MGYG000001338_00028

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 Blautia_A wexlerae_A
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A wexlerae_A
CAZyme ID MGYG000001338_00028
CAZy Family CE4
CAZyme Description Peptidoglycan-N-acetylmuramic acid deacetylase PdaA
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
275 MGYG000001338_1|CGC1 31217.29 6.6611
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001338 3930699 Isolate not provided not provided
Gene Location Start: 18958;  End: 19785  Strand: +

Full Sequence      Download help

MHLKYISSTR  IFSSRFTKIF  LLFCACAFIG  SSIGKIVSHN  TARQTAASAQ  SSNWGLSFQE60
EGKRPVGNAT  IEELAQYNAF  FAEDTEEKKI  YLTFDAGFEN  GNTPAILDAL  KKHQAPATFF120
VVGNFISENK  DLIKRMETEG  HIVGNHTMTH  PDMSKISTKE  SFQKELSDVE  KIYREITGKE180
MTKFYRPPQG  IYSTQNLSMA  RELGYHTFFW  SLAYVDWYQD  NQPDPQEAIA  KLTKRIHPGA240
IVLLHSTSST  NAQILDELLD  KWEAMGYSFH  SLNEL275

Enzyme Prediction      help

No EC number prediction in MGYG000001338_00028.

CAZyme Signature Domains help

Created with Snap1327415568829611012313715116517819220622023324726182207CE4
Family Start End Evalue family coverage
CE4 82 207 7.8e-33 0.9307692307692308

CDD Domains      download full data without filtering help

Created with Snap1327415568829611012313715116517819220622023324726153272CE4_BsPdaA_like53275spore_pdaA88260CE4_NodB_like_6s_7s84275CE4_BsYlxY_like84275spore_ybaN_pdaB
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10948 CE4_BsPdaA_like 8.66e-109 53 272 4 223
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.
TIGR02884 spore_pdaA 2.12e-108 53 275 1 223
delta-lactam-biosynthetic de-N-acetylase. Muramic delta-lactam is an unusual constituent of peptidoglycan, found only in bacterial spores in the peptidoglycan wall, or spore cortex. The proteins in this family are PdaA (yfjS), a member of a larger family of polysaccharide deacetylases, and are specificially involved in delta-lactam biosynthesis. PdaA acts immediately after CwlD, an N-acetylmuramoyl-L-alanine amidase and performs a de-N-acetylation. PdaA may also perform the following transpeptidation for lactam ring formation, as heterologous expression in E. coli of CwlD and PdaA together is sufficient for delta-lactam production. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]
cd10917 CE4_NodB_like_6s_7s 1.09e-60 88 260 1 168
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.
cd10950 CE4_BsYlxY_like 3.95e-49 84 275 2 187
Putative catalytic NodB homology domain of uncharacterized protein YlxY from Bacillus subtilis 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 putative polysaccharide deacetylase BsYlxY, encoded by the ylxY gene, which is a member of the carbohydrate esterase 4 (CE4) superfamily. Although its biological function still remains unknown, BsYlxY shows high sequence homology to the catalytic domain of Bacillus subtilis pdaB gene encoding a putative polysaccharide deacetylase (BsPdaB), which is essential for the maintenance of spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. However, disruption of the ylxY gene in B. subtilis did not cause any sporulation defect. Moreover, the Asp residue in the classical His-His-Asp zinc-binding motif of CE4 esterases is mutated to a Val residue in this family. Other catalytically relevant residues of CE4 esterases are also not conserved, which suggest that members of this family may be inactive.
TIGR02764 spore_ybaN_pdaB 6.34e-46 84 275 2 190
polysaccharide deacetylase family sporulation protein PdaB. This model describes the YbaN protein family, also called PdaB and SpoVIE, of Gram-positive bacteria. Although ybaN null mutants have only a mild sporulation defect, ybaN/ytrI double mutants show drastically reducted sporulation efficiencies. This synthetic defect suggests the role of this sigmaE-controlled gene in sporulation had been masked by functional redundancy. Members of this family are homologous to a characterized polysaccharide deacetylase; the exact function this protein family is unknown. [Cellular processes, Sporulation and germination]

CAZyme Hits      help

Created with Snap1327415568829611012313715116517819220622023324726118275CBL24255.1|CE421275QNM09949.1|CE415275QIB56171.1|CE415275QMW81094.1|CE43275QEK18529.1|CE4
Hit ID E-Value Query Start Query End Hit Start Hit End
CBL24255.1 1.33e-125 18 275 12 270
QNM09949.1 1.76e-125 21 275 15 267
QIB56171.1 5.19e-125 15 275 9 268
QMW81094.1 5.19e-125 15 275 9 268
QEK18529.1 7.38e-125 3 275 1 268

PDB Hits      download full data without filtering help

Created with Snap13274155688296110123137151165178192206220233247261362751W1A_1362751W17_A382752J13_A532751NY1_A872756HM9_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
1W1A_1 4.59e-64 36 275 7 246
Structureof Bacillus subtilis PdaA in complex with NAG, a family 4 Carbohydrate esterase. [Bacillus subtilis],1W1A_2 Structure of Bacillus subtilis PdaA in complex with NAG, a family 4 Carbohydrate esterase. [Bacillus subtilis],1W1B_1 Structure of Bacillus subtilis PdaA with Cadmium, a family 4 Carbohydrate esterase. [Bacillus subtilis],1W1B_2 Structure of Bacillus subtilis PdaA with Cadmium, a family 4 Carbohydrate esterase. [Bacillus subtilis]
1W17_A 5.51e-64 36 275 13 252
Structureof Bacillus subtilis PdaA, a family 4 Carbohydrate esterase. [Bacillus subtilis],1W17_B Structure of Bacillus subtilis PdaA, a family 4 Carbohydrate esterase. [Bacillus subtilis]
2J13_A 5.42e-63 38 275 4 241
Structureof a family 4 carbohydrate esterase from Bacillus anthracis [Bacillus anthracis str. Ames]
1NY1_A 1.24e-62 53 275 7 229
CrystalStructure Of B. Subtilis Polysaccharide Deacetylase Northeast Structural Genomics Consortium Target Sr127. [Bacillus subtilis],1NY1_B Crystal Structure Of B. Subtilis Polysaccharide Deacetylase Northeast Structural Genomics Consortium Target Sr127. [Bacillus subtilis]
6HM9_A 2.39e-31 87 275 84 266
Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis]

Swiss-Prot Hits      download full data without filtering help

Created with Snap1327415568829611012313715116517819220622023324726153275sp|Q04729|YFUM2_GEOSE36275sp|O34928|PDAA_BACSU82274sp|Q52845|NODB_RHILO72275sp|Q8DP63|PGDA_STRR688275sp|P04675|NODB_BRASP
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q04729 4.00e-64 53 275 31 253
Uncharacterized 30.6 kDa protein in fumA 3'region OS=Geobacillus stearothermophilus OX=1422 PE=3 SV=1
O34928 3.01e-63 36 275 13 252
Peptidoglycan-N-acetylmuramic acid deacetylase PdaA OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaA PE=1 SV=1
Q52845 1.17e-31 82 274 15 217
Chitooligosaccharide deacetylase OS=Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OX=266835 GN=nodB PE=3 SV=2
Q8DP63 2.46e-29 72 275 253 447
Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1
P04675 3.73e-29 88 275 21 218
Chitooligosaccharide deacetylase OS=Bradyrhizobium sp. (strain ANU 289) OX=186901 GN=nodB PE=3 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
0.471629 0.280736 0.242938 0.001077 0.000857 0.002772

TMHMM  Annotations      download full data without filtering help

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