Basic Information | |
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Species | Setaria italica |
Cazyme ID | Si010565m |
Family | CE11 |
Protein Properties | Length: 333 Molecular Weight: 36113.2 Isoelectric Point: 6.8288 |
Chromosome | Chromosome/Scaffold: 7 Start: 20683789 End: 20691899 |
Description | UDP-3-O-acyl N-acetylglycosamine deacetylase family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE11 | 33 | 317 | 0 |
QQTLAAAVSRSGVGLHSGARVTATLLPTYAGEGRYFQVEGKEEARVAAEVGNAEPRSQLCTTLQRGEGCGPRIRTVEHLLSAMEALGVDNCRVEVIGGDE IPLLDGSAQEWVEAIRSAGLCAAEDTGGQKLEKLAPQIHEPVYLQRDDCFVAAFPSSQIHITYGIDFPKVPAIGCQWFSTFLDANIYSSKIAPARTFCIF KEIEKMRGAGLIKGGSLENAMVCSMSGGWLNPPVRFEDEPCRHKILDLIGDFSLLAQNGNQGFPIAHIIAYKAGHALHTDFLRHL |
Full Sequence |
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Protein Sequence Length: 333 Download |
MSTAATRALK SVSHAVFSWK PRLTLFFQTG RPQQTLAAAV SRSGVGLHSG ARVTATLLPT 60 YAGEGRYFQV EGKEEARVAA EVGNAEPRSQ LCTTLQRGEG CGPRIRTVEH LLSAMEALGV 120 DNCRVEVIGG DEIPLLDGSA QEWVEAIRSA GLCAAEDTGG QKLEKLAPQI HEPVYLQRDD 180 CFVAAFPSSQ IHITYGIDFP KVPAIGCQWF STFLDANIYS SKIAPARTFC IFKEIEKMRG 240 AGLIKGGSLE NAMVCSMSGG WLNPPVRFED EPCRHKILDL IGDFSLLAQN GNQGFPIAHI 300 IAYKAGHALH TDFLRHLCGR ITVDQEEVAR QC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK13188 | PRK13188 | 3.0e-64 | 33 | 331 | 330 | + bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed | ||
TIGR00325 | lpxC | 5.0e-77 | 33 | 315 | 285 | + UDP-3-0-acyl N-acetylglucosamine deacetylase. UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc deacetylase from E. coli , LpxC, was previously designated EnvA. This enzyme is involved in lipid-A precursor biosynthesis. It is essential for cell viability [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]. | ||
pfam03331 | LpxC | 6.0e-92 | 33 | 315 | 291 | + UDP-3-O-acyl N-acetylglycosamine deacetylase. The enzymes in this family catalyze the second step in the biosynthetic pathway for lipid A. | ||
COG0774 | LpxC | 7.0e-94 | 33 | 317 | 292 | + UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell envelope biogenesis, outer membrane] | ||
PRK13186 | lpxC | 1.0e-107 | 33 | 317 | 291 | + UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase; Reviewed |
Gene Ontology | |
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GO Term | Description |
GO:0008759 | UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity |
GO:0009245 | lipid A biosynthetic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAN52736.1 | 0 | 1 | 332 | 1 | 315 | Hypothetical protein [Oryza sativa Japonica Group] |
GenBank | ABF94722.1 | 0 | 1 | 291 | 1 | 280 | UDP-3-0-acyl N-acetylglucosamine deacetylase family protein, expressed [Oryza sativa (japonica cultivar-group)] |
GenBank | EEE58623.1 | 0 | 1 | 332 | 1 | 322 | hypothetical protein OsJ_09977 [Oryza sativa Japonica Group] |
RefSeq | NP_001049426.1 | 0 | 1 | 332 | 1 | 321 | Os03g0223900 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002468246.1 | 0 | 1 | 332 | 1 | 325 | hypothetical protein SORBIDRAFT_01g042410 [Sorghum bicolor] |
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 | 3uhm_A | 1e-37 | 33 | 318 | 4 | 275 | A Chain A, Crystal Structure Of N-Carbamyl-D-Amino Acid Amidohydrolase With A Novel Catalytic Framework Common To Amidohydrolases |
PDB | 3u1y_B | 1e-37 | 33 | 318 | 4 | 275 | A Chain A, Crystal Structure Of N-Carbamyl-D-Amino Acid Amidohydrolase With A Novel Catalytic Framework Common To Amidohydrolases |
PDB | 3u1y_A | 1e-37 | 33 | 318 | 4 | 275 | A Chain A, Crystal Structure Of N-Carbamyl-D-Amino Acid Amidohydrolase With A Novel Catalytic Framework Common To Amidohydrolases |
PDB | 3p3e_A | 1e-37 | 33 | 318 | 4 | 275 | A Chain A, Crystal Structure Of N-Carbamyl-D-Amino Acid Amidohydrolase With A Novel Catalytic Framework Common To Amidohydrolases |
PDB | 2ves_C | 1e-37 | 33 | 318 | 4 | 275 | A Chain A, Crystal Structure Of Lpxc From Pseudomonas Aeruginosa Complexed With The Potent Bb-78485 Inhibitor |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
lipid IVA biosynthesis | UDPACYLGLCNACDEACETYL-RXN | EC-3.5.1.108 | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HX136805 | 267 | 7 | 273 | 0 |
CK207177 | 257 | 7 | 263 | 0 |
CT850072 | 306 | 1 | 306 | 0 |
CA246559 | 204 | 129 | 332 | 0 |
CA238382 | 186 | 129 | 314 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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