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CAZyme Information: MGYG000003288_00615

You are here: Home > Sequence: MGYG000003288_00615

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 Duodenibacillus sp900544255
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Duodenibacillus; Duodenibacillus sp900544255
CAZyme ID MGYG000003288_00615
CAZy Family CE11
CAZyme Description UDP-3-O-acyl-N-acetylglucosamine deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
313 MGYG000003288_33|CGC1 34162.39 8.088
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003288 2215926 MAG Mongolia Asia
Gene Location Start: 7499;  End: 8440  Strand: -

Full Sequence      Download help

MTDASPLLRQ  CTIARTISTV  GIGLHSGRRV  RLTMKPAAPD  TGIIFRRVDM  TPPVEMPAKP60
TSVNDTRMAT  TLNEGKVVIS  TIEHIMSALN  GMGVDNVYVD  VDAPEIPIMD  GSGATFVYLI120
RSAGLMQQSA  PKKFVRVLKP  VKVTDGDKWA  QLEPYKGLVL  QFGINFGHPA  IDNTVQNATV180
DFSRETYEDA  VSRARTFGFV  TDVEMLRSMG  LAQGGTMENA  IVMDEFRVLN  VGGLRSPDEF240
VKHKILDAMG  DLYVLGHKLL  ARYSAYKSGH  GLNNKLLRAL  IADPTSWEYT  TLARAESPFR300
PVHAEALLSP  AAG313

Enzyme Prediction      help

EC 3.5.1.-

CAZyme Signature Domains help

Created with Snap15314662789310912514015617218720321923425026628129710281CE11
Family Start End Evalue family coverage
CE11 10 281 4.9e-110 0.992619926199262

CDD Domains      download full data without filtering help

Created with Snap1531466278931091251401561721872032192342502662812979298lpxC10282LpxC7312LpxC8298lpxC7281PRK13188
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK13186 lpxC 3.58e-175 9 298 3 290
UDP-3-O-acyl-N-acetylglucosamine deacetylase.
pfam03331 LpxC 3.49e-163 10 282 1 271
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 3.04e-156 7 312 1 300
UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis].
TIGR00325 lpxC 4.38e-129 8 298 1 290
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]
PRK13188 PRK13188 1.41e-77 7 281 2 299
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed

CAZyme Hits      help

Created with Snap15314662789310912514015617218720321923425026628129710296QQS89336.1|CE117296QDA55074.1|CE117299QQQ95905.1|CE119287BBF22511.1|CE117296QDZ28935.1|CE11
Hit ID E-Value Query Start Query End Hit Start Hit End
QQS89336.1 8.43e-137 10 296 4 290
QDA55074.1 5.45e-134 7 296 1 290
QQQ95905.1 3.75e-133 7 299 1 296
BBF22511.1 1.87e-132 9 287 5 283
QDZ28935.1 9.58e-128 7 296 1 294

PDB Hits      download full data without filtering help

Created with Snap15314662789310912514015617218720321923425026628129772914MDT_A72913P3G_A72914MQY_A72983NZK_A42974FW3_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
4MDT_A 6.18e-109 7 291 1 286
Structureof LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine [Escherichia coli],4MDT_B Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine [Escherichia coli],4MDT_C Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine [Escherichia coli],4MDT_D Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine [Escherichia coli]
3P3G_A 7.41e-109 7 291 1 286
CrystalStructure of the Escherichia coli LpxC/LPC-009 complex [Escherichia coli IHE3034],3PS1_A Crystal structure of the Escherichia Coli LPXC/LPC-011 complex [Escherichia coli IHE3034],3PS2_A Crystal structure of the Escherichia Coli LPXC/LPC-012 complex [Escherichia coli IHE3034],3PS3_A Crystal structure of the Escherichia Coli LPXC/LPC-053 complex [Escherichia coli IHE3034],4IS9_A Crystal Structure of the Escherichia coli LpxC/L-161,240 complex [Escherichia coli IHE3034],4IS9_B Crystal Structure of the Escherichia coli LpxC/L-161,240 complex [Escherichia coli IHE3034],4ISA_A Crystal Structure of the Escherichia coli LpxC/BB-78485 complex [Escherichia coli IHE3034]
4MQY_A 8.76e-109 7 291 1 286
CrystalStructure of the Escherichia coli LpxC/LPC-138 complex [Escherichia coli]
3NZK_A 1.07e-108 7 298 6 299
Structureof LpxC from Yersinia enterocolitica Complexed with CHIR090 Inhibitor [Yersinia enterocolitica],3NZK_B Structure of LpxC from Yersinia enterocolitica Complexed with CHIR090 Inhibitor [Yersinia enterocolitica]
4FW3_A 3.20e-108 4 297 1 294
CrystalStructure of the LpxC in complex with N-[(2S)-3-AMINO-1-(HYDROXYAMINO)-1-OXOPROPAN-2-YL]-4-(4-PHENYLBUTA-1,3-DIYN-1-YL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW3_B Crystal Structure of the LpxC in complex with N-[(2S)-3-AMINO-1-(HYDROXYAMINO)-1-OXOPROPAN-2-YL]-4-(4-PHENYLBUTA-1,3-DIYN-1-YL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW3_C Crystal Structure of the LpxC in complex with N-[(2S)-3-AMINO-1-(HYDROXYAMINO)-1-OXOPROPAN-2-YL]-4-(4-PHENYLBUTA-1,3-DIYN-1-YL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW3_D Crystal Structure of the LpxC in complex with N-[(2S)-3-AMINO-1-(HYDROXYAMINO)-1-OXOPROPAN-2-YL]-4-(4-PHENYLBUTA-1,3-DIYN-1-YL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW4_A Crystal Structure of the LpxC in complex with N-[(1S,2R)-2-HYDROXY-1-(HYDROXYCARBAMOYL)PROPYL]-4-(4-PHENYLBUTA-1,3-DIYN-1-YL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW4_B Crystal Structure of the LpxC in complex with N-[(1S,2R)-2-HYDROXY-1-(HYDROXYCARBAMOYL)PROPYL]-4-(4-PHENYLBUTA-1,3-DIYN-1-YL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW4_C Crystal Structure of the LpxC in complex with N-[(1S,2R)-2-HYDROXY-1-(HYDROXYCARBAMOYL)PROPYL]-4-(4-PHENYLBUTA-1,3-DIYN-1-YL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW4_D Crystal Structure of the LpxC in complex with N-[(1S,2R)-2-HYDROXY-1-(HYDROXYCARBAMOYL)PROPYL]-4-(4-PHENYLBUTA-1,3-DIYN-1-YL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW5_A Crystal Structure of the LpxC in complex with 4'-BROMO-N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]BIPHENYL-4-CARBOXAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW5_B Crystal Structure of the LpxC in complex with 4'-BROMO-N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]BIPHENYL-4-CARBOXAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW5_C Crystal Structure of the LpxC in complex with 4'-BROMO-N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]BIPHENYL-4-CARBOXAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW5_D Crystal Structure of the LpxC in complex with 4'-BROMO-N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]BIPHENYL-4-CARBOXAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW6_A Crystal Structure of the LpxC in complex with N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]-4-(PHENYLETHYNYL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW6_B Crystal Structure of the LpxC in complex with N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]-4-(PHENYLETHYNYL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW6_C Crystal Structure of the LpxC in complex with N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]-4-(PHENYLETHYNYL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW6_D Crystal Structure of the LpxC in complex with N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]-4-(PHENYLETHYNYL)BENZAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW7_A Crystal Structure of the LpxC in complex with N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]BIPHENYL-4-CARBOXAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW7_B Crystal Structure of the LpxC in complex with N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]BIPHENYL-4-CARBOXAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW7_C Crystal Structure of the LpxC in complex with N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]BIPHENYL-4-CARBOXAMIDE inhibitor [Pseudomonas aeruginosa PAO1],4FW7_D Crystal Structure of the LpxC in complex with N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]BIPHENYL-4-CARBOXAMIDE inhibitor [Pseudomonas aeruginosa PAO1]

Swiss-Prot Hits      download full data without filtering help

Created with Snap1531466278931091251401561721872032192342502662812977298sp|Q2KVH1|LPXC_BORA17298sp|Q7VUQ9|LPXC_BORPE7298sp|Q7WFS8|LPXC_BORBR7298sp|Q7W4C0|LPXC_BORPA7291sp|Q39JW3|LPXC_BURL3
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q2KVH1 1.48e-124 7 298 1 297
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Bordetella avium (strain 197N) OX=360910 GN=lpxC PE=3 SV=1
Q7VUQ9 8.52e-124 7 298 1 297
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) OX=257313 GN=lpxC PE=3 SV=1
Q7WFS8 8.52e-124 7 298 1 297
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) OX=257310 GN=lpxC PE=3 SV=1
Q7W4C0 8.52e-124 7 298 1 297
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253) OX=257311 GN=lpxC PE=3 SV=1
Q39JW3 2.27e-123 7 291 1 285
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383) OX=482957 GN=lpxC PE=3 SV=1

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
1.000036 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003288_00615.