Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s3023_2V6.1 |
Family | CE9 |
Protein Properties | Length: 263 Molecular Weight: 28329.3 Isoelectric Point: 6.0359 |
Chromosome | Chromosome/Scaffold: 3023 Start: 2297 End: 3085 |
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 |
CE9 | 2 | 257 | 0 |
EGVHLEGPFFSPKWPGAQNPEHIILPDVTWLEAWEKQYPGLIRQVTLAPEREGALEVISWLREQRITAALGHTDATYEEVERAVESGLHHAVHTFNAMTP LHHRLPGAAGAVLSDPRISAEVIADGIHVHPAAISILAQLKQHNDQLVLITDAMSAAGLDDGEYKIGDLPVIVKHGEARLKDGGALAGSTLTMIRGFRYL VQEVGLSLNAASRAASLTPARLLGIDHRTGSLAQGKQADIVLLNAELDIEGVWVKG |
Full Sequence |
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Protein Sequence Length: 263 Download |
LEGVHLEGPF FSPKWPGAQN PEHIILPDVT WLEAWEKQYP GLIRQVTLAP EREGALEVIS 60 WLREQRITAA LGHTDATYEE VERAVESGLH HAVHTFNAMT PLHHRLPGAA GAVLSDPRIS 120 AEVIADGIHV HPAAISILAQ LKQHNDQLVL ITDAMSAAGL DDGEYKIGDL PVIVKHGEAR 180 LKDGGALAGS TLTMIRGFRY LVQEVGLSLN AASRAASLTP ARLLGIDHRT GSLAQGKQAD 240 IVLLNAELDI EGVWVKGRRI GE* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK10657 | PRK10657 | 2.0e-9 | 188 | 258 | 71 | + isoaspartyl dipeptidase; Provisional | ||
PRK11170 | nagA | 1.0e-52 | 3 | 257 | 255 | + N-acetylglucosamine-6-phosphate deacetylase; Provisional | ||
TIGR00221 | nagA | 5.0e-70 | 3 | 258 | 256 | + N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]. | ||
COG1820 | NagA | 3.0e-96 | 3 | 260 | 258 | + N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism] | ||
cd00854 | NagA | 6.0e-108 | 3 | 257 | 255 | + N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling. |
Gene Ontology | |
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GO Term | Description |
GO:0016787 | hydrolase activity |
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_001786594.1 | 0 | 3 | 262 | 1 | 260 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | YP_003013173.1 | 0 | 1 | 260 | 130 | 388 | N-acetylglucosamine-6-phosphate deacetylase [Paenibacillus sp. JDR-2] |
RefSeq | YP_003241562.1 | 0 | 1 | 259 | 135 | 393 | N-acetylglucosamine-6-phosphate deacetylase [Geobacillus sp. Y412MC10] |
RefSeq | ZP_02326251.1 | 0 | 1 | 260 | 128 | 387 | N-acetylglucosamine-6-phosphate deacetylase [Paenibacillus larvae subsp. larvae BRL-230010] |
RefSeq | ZP_04852977.1 | 0 | 1 | 258 | 133 | 390 | N-acetylglucosamine-6-phosphate deacetylase [Paenibacillus sp. oral taxon 786 str. D14] |
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 | 2vhl_B | 0 | 1 | 250 | 130 | 377 | A Chain A, The Three-Dimensional Structure Of The N-Acetylglucosamine- 6-Phosphate Deacetylase From Bacillus Subtilis |
PDB | 2vhl_A | 0 | 1 | 250 | 130 | 377 | A Chain A, The Three-Dimensional Structure Of The N-Acetylglucosamine- 6-Phosphate Deacetylase From Bacillus Subtilis |
PDB | 2p50_D | 7.00649e-44 | 3 | 260 | 127 | 379 | A Chain A, The Three-Dimensional Structure Of The N-Acetylglucosamine- 6-Phosphate Deacetylase From Bacillus Subtilis |
PDB | 2p50_C | 7.00649e-44 | 3 | 260 | 127 | 379 | A Chain A, The Three-Dimensional Structure Of The N-Acetylglucosamine- 6-Phosphate Deacetylase From Bacillus Subtilis |
PDB | 2p50_B | 7.00649e-44 | 3 | 260 | 127 | 379 | A Chain A, The Three-Dimensional Structure Of The N-Acetylglucosamine- 6-Phosphate Deacetylase From Bacillus Subtilis |