Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s2_200V6.1 |
Family | CE4 |
Protein Properties | Length: 373 Molecular Weight: 42437.3 Isoelectric Point: 10.4089 |
Chromosome | Chromosome/Scaffold: 2 Start: 1014769 End: 1017943 |
Description | |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE4 | 188 | 314 | 3.7e-27 |
EKLVALTLDDGPHAHITPQLLDILKENNCRATWFLIGNHMARCPLVVDRIIAEGHEVANHMMADVASWTLSKEEFETQLIECDNRLKDYYRNNSSGQAQK WFRPGHGFYNMQIVKTCKKHGYRVALG |
Full Sequence |
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Protein Sequence Length: 373 Download |
MTTFSSYEAT STPPIGTSIT PTNSSSPRWR IIFQRNCKPK TLRSRNSRFR SQQGSGPRLA 60 DHLTSLWQRR PSLDRKDASK PRQIRGSGRD NRQVGAKGWH VSAFGGIDML VNSSLMANVQ 120 ANIVPMAVIV ALGSLIFTII LLLGLAILCH PLWIVKWTQK LQPHVMYLKP TQATRLIFLP 180 WDSGVWLEKL VALTLDDGPH AHITPQLLDI LKENNCRATW FLIGNHMARC PLVVDRIIAE 240 GHEVANHMMA DVASWTLSKE EFETQLIECD NRLKDYYRNN SSGQAQKWFR PGHGFYNMQI 300 VKTCKKHGYR VALGSLYPMD HMFERQAHLL VKILLWRVLR LLLPELRKRG YRVVSLSELE 360 ESVSNPEVKQ AD* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10954 | CE4_CtAXE_like | 5.0e-25 | 189 | 297 | 109 | + Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs. This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan, as a consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases. | ||
cd10959 | CE4_NodB_like_3 | 6.0e-31 | 189 | 320 | 132 | + 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 | 7.0e-32 | 188 | 312 | 125 | + 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 hydrolyses glucosidic bonds in xylan. | ||
cd10917 | CE4_NodB_like_6s_7s | 1.0e-35 | 189 | 320 | 132 | + 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. | ||
cd10958 | CE4_NodB_like_2 | 5.0e-69 | 189 | 325 | 137 | + Catalytic NodB homology domain of uncharacterized chitin deacetylases and hypothetical proteins. This family includes some uncharacterized chitin deacetylases and hypothetical proteins, mainly from eukaryotes. Although their biological function is unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41), which catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. Like ClCDA, this family is a member the carbohydrate esterase 4 (CE4) superfamily. |
Gene Ontology | |
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GO Term | Description |
GO:0005975 | carbohydrate metabolic process |
GO:0016810 | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_001751919.1 | 0 | 1 | 361 | 1 | 416 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | YP_001801874.1 | 2e-34 | 153 | 359 | 32 | 247 | polysaccharide deacetylase [Cyanothece sp. ATCC 51142] |
RefSeq | YP_002373904.1 | 7e-33 | 153 | 361 | 27 | 252 | polysaccharide deacetylase [Cyanothece sp. PCC 8801] |
RefSeq | ZP_01729594.1 | 1e-39 | 139 | 359 | 18 | 247 | Peptidoglycan N-acetylglucosamine deacetylase [Cyanothece sp. CCY0110] |
RefSeq | ZP_05037305.1 | 8e-31 | 140 | 361 | 22 | 247 | Polysaccharide deacetylase domain protein [Synechococcus sp. PCC 7335] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2c79_A | 0.00000000000006 | 189 | 359 | 5 | 188 | A Chain A, Crystal Structure Of Wild-Type E.Coli Gs In Complex With Adp And Glucose(Wtgsb) |
PDB | 2c71_A | 0.00000000000006 | 189 | 359 | 5 | 188 | A Chain A, The Structure Of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum In Complex With A Magnesium Ion. |
PDB | 1w1b_2 | 0.00000000000007 | 188 | 359 | 59 | 246 | A Chain A, The Structure Of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum In Complex With A Magnesium Ion. |
PDB | 1w1b_1 | 0.00000000000007 | 188 | 359 | 59 | 246 | A Chain A, The Structure Of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum In Complex With A Magnesium Ion. |
PDB | 1w1a_2 | 0.00000000000007 | 188 | 359 | 59 | 246 | 1 Chain 1, Structure Of Bacillus Subtilis Pdaa In Complex With Nag, A Family 4 Carbohydrate Esterase. |
Transmembrane Domains | |||||
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Start | End | ||||
126 | 148 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FC369235 | 291 | 38 | 328 | 0 |
EX927815 | 238 | 91 | 323 | 0 |
BY975899 | 104 | 1 | 104 | 0 |
FD775771 | 158 | 144 | 301 | 2.94273e-44 |
EX930510 | 213 | 67 | 277 | 2e-40 |
Orthologous Group | |||||
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Species | ID | ||||
Selaginella moellendorffii | 96774 |
Sequence Alignments (This image is cropped. Click for full image.) |
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