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ECOBD:C6EAV9

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Species (Taxon ID) Escherichia coli (strain B / BL21-DE3). (469008)
Gene Name(s) No Information Provided.
Protein Name(s) UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase (ECO:0000256 with HAMAP-Rule:MF_00388, ECO:0000256 with SAAS:SAAS00041388)

UDP-3-O-acyl-GlcNAc deacetylase (ECO:0000256 with HAMAP-Rule:MF_00388)

External Links
UniProt C6EAV9
EMBL CP001665
CP001509
AM946981
RefSeq YP_002997963.1
YP_003037705.1
YP_003052769.1
ProteinModelPortal C6EAV9
SMR C6EAV9
STRING 469008.ECBD_3521
BindingDB C6EAV9
EnsemblBacteria ACT30520
ACT41998
CAQ30613
GeneID 8113174
8158251
8181503
KEGG ebd:ECBD_3521
ebe:B21_00096
ebl:ECD_00097
eggNOG COG0774
HOGENOM HOG000256663
KO K02535
OMA KAYKSGH
Proteomes UP000001509
UP000002032
UP000009074
GO GO:0008759
GO:0009245
Gene3D 3.30.1700.10
3.30.230.20
HAMAP MF_00388
InterPro IPR020568
IPR004463
IPR011334
IPR015870
Pfam PF03331
SUPFAM SSF54211
TIGRFAMs TIGR00325

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008759

UDP-3-O-(3-hydroxymyristoyl) N-acetylglucosamine deacetylase activity

PMID:20709752[1]

ECO:0000314

F

Native LpxC activity varies with metal supplementation in the growth medium. E. coli BL21(DE3) cells (without LpxC expression plasmid) were grown in minimal medium with and without 20 μm metal supplementation, lysed, and assayed for deacetylase activity as described under “Materials and Methods” either anaerobically (black bars) or after exposure to room oxygen for 2.5 h (gray bars).

complete

enables

GO:0008759

UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004463
InterPro:IPR011334
InterPro:IPR015870

F

Seeded From UniProt

complete

involved_in

GO:0009245

lipid A biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004463
InterPro:IPR011334
InterPro:IPR015870

P

Seeded From UniProt

complete

enables

GO:0008759

UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.5.1.108

F

Seeded From UniProt

complete

enables

GO:0103117

UDP-3-O-acyl-N-acetylglucosamine deacetylase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.5.1.108

F

Seeded From UniProt

complete

involved_in

GO:0009245

lipid A biosynthetic process

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0441

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0006629

lipid metabolic process

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0443

P

Seeded From UniProt

complete

enables

GO:0008759

UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000036436

F

Seeded From UniProt

complete

involved_in

GO:0009245

lipid A biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000036436

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Gattis, SG et al. (2010) Active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions. J. Biol. Chem. 285 33788-96 PubMed GONUTS page