Q8DI02

PR
Gene name
lpxC
Protein name
UDP-3-O-acyl-N-acetylglucosamine deacetylase
Names
UDP-3-O-acyl-GlcNAc deacetylase, UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
Species
Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
KEGG Pathway
tel:tlr1790
EC number
3.5.1.108: In linear amides
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-46 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8DI02

Entry ID Method Resolution Chain Position Source
AF-Q8DI02-F1 Predicted AlphaFoldDB

No variants for Q8DI02

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8DI02

No associated diseases with Q8DI02

No regional properties for Q8DI02

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q8DI02

Functions

Description
EC Number 3.5.1.108 In linear amides
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity Catalysis of the removal of an acetyl group from the 2-N position of glucosamine in the lipid A precursor UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine.
UDP-3-O-acyl-N-acetylglucosamine deacetylase activity Catalysis of the reaction: UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetylglucosamine(2-) + H2O <=> UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine(1-) + acetate.

1 GO annotations of biological process

Name Definition
lipid A biosynthetic process The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIAASGPTPL VATTQRTLAG TAQWSGVGLH SGQWVALTLQ PAAANTGRQF VRLDLEGQPV
70 80 90 100 110 120
IPARIEAVKS TQLATELVAN GASVRTVEHL LAALAIAGID NVTIQITGPE VPVLDGSAQP
130 140 150 160 170 180
WLEGIQRVGV VPQEAPRPAV ILKEPVTIYE GEAFVSAIPA PELRLTYGID FPYRAIGRQW
190 200 210 220 230 240
CSFTPSELAT EVAPARTFGF AEQVDYLRSQ GLIQGGSLEN ALVCSASGWV NPPLRFADEP
250 260 270 280
VRHKLLDLWG DLALLGTPPI AHYVAYRASH HLHTQLARAI AQQRV