logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002135_00207

You are here: Home > Sequence: MGYG000002135_00207

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 Anaeromassilibacillus sp002159845
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Anaeromassilibacillus; Anaeromassilibacillus sp002159845
CAZyme ID MGYG000002135_00207
CAZy Family CE4
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
312 34955.94 8.9719
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002135 2740278 MAG United States North America
Gene Location Start: 157;  End: 1095  Strand: -

Full Sequence      Download help

MKRAKHVRRG  NSGKVVSILT  ILLLFALFSA  TCFPLSHALQ  KVDSPSLSTL  AGQVAIEGAL60
SAKPKIVVES  APVVKTTPQK  QALPNDPYPL  LYTEKISPKE  DDSNEKIAYL  TFDDGPSDLT120
IPLLDVLDRY  QVKATFFLVG  KTGEEDRKAM  REIVKRGHAI  AVHSYSHDYR  EIYASVDAYL180
ADFAKMHDLI  LKETGVDTPL  YRFAGGSINS  YNRDTAKAII  EEMNRRGYTY  FDWNVDSGDA240
TRGTTAQQIY  QHAVNDSKQF  RRPVILFHNT  GTKKMTLEQI  PAIIEALQKE  GYRFDVLKAD300
TPPVRFRIPE  TA312

Enzyme Prediction      help

No EC number prediction in MGYG000002135_00207.

CAZyme Signature Domains help

Created with Snap153146627893109124140156171187202218234249265280296101230CE4
Family Start End Evalue family coverage
CE4 101 230 1.5e-26 0.9230769230769231

CDD Domains      download full data without filtering help

Created with Snap153146627893109124140156171187202218234249265280296106296CE4_SmPgdA_like106288CE4_NodB_like_6s_7s94306CDA1106297CE4_NodB_like_3102231Polysacc_deac_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10944 CE4_SmPgdA_like 1.90e-88 106 296 1 189
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 1.42e-43 106 288 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 1.07e-35 94 306 53 262
Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
cd10959 CE4_NodB_like_3 1.69e-35 106 297 1 187
Catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases. This family includes many uncharacterized bacterial polysaccharide deacetylases. Although their biological function still remains unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Like SpPgdA, this family is a member of the carbohydrate esterase 4 (CE4) superfamily.
pfam01522 Polysacc_deac_1 7.60e-30 102 231 3 124
Polysaccharide deacetylase. This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyzes glucosidic bonds in xylan.

CAZyme Hits      help

Created with Snap15314662789310912414015617118720221823424926528029688309QEY35883.1|CE488310CAB1253925.1|CE4108306QIB68221.1|CE488302QHQ63039.1|CE4106306QAT41967.1|CE4
Hit ID E-Value Query Start Query End Hit Start Hit End
QEY35883.1 2.97e-81 88 309 2 225
CAB1253925.1 1.81e-76 88 310 109 331
QIB68221.1 8.91e-58 108 306 100 298
QHQ63039.1 3.24e-57 88 302 79 294
QAT41967.1 7.81e-56 106 306 98 298

PDB Hits      download full data without filtering help

Created with Snap1531466278931091241401561711872022182342492652802961063085JMU_A893065NC9_A892947FBW_A1063065NC6_A1063065N1J_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
5JMU_A 4.99e-40 106 308 20 224
ChainA, Peptidoglycan N-acetylglucosamine deacetylase [[Eubacterium] rectale ATCC 33656]
5NC9_A 2.44e-22 89 306 25 241
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]
7FBW_A 2.49e-22 89 294 101 293
ChainA, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
5NC6_A 2.70e-22 106 306 1 199
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 2.76e-22 106 306 2 200
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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap153146627893109124140156171187202218234249265280296105304sp|O07596|YHEN_BACSU89306sp|Q81EJ6|PGDA2_BACCR104308sp|P83513|XY11A_PSEXY103294sp|Q81AF4|PGDA3_BACCR101294sp|Q8DP63|PGDA_STRR6
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O07596 1.01e-25 105 304 84 280
Putative polysaccharide deacetylase YheN OS=Bacillus subtilis (strain 168) OX=224308 GN=yheN PE=3 SV=1
Q81EJ6 2.16e-21 89 306 51 267
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
P83513 4.30e-17 104 308 400 597
Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2
Q81AF4 1.13e-16 103 294 19 202
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 2.99e-15 101 294 263 441
Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA 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
0.006033 0.145772 0.847562 0.000221 0.000195 0.000197

TMHMM  Annotations      download full data without filtering help

start end
13 35