Q7MXT8

PR
Gene name
lpxC/fabZ (PG_0071)
Protein name
Bifunctional enzyme LpxC/FabZ
Names
Species
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
KEGG Pathway
pgi:PG_0071
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)

274-344 (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 Q7MXT8

Entry ID Method Resolution Chain Position Source
AF-Q7MXT8-F1 Predicted AlphaFoldDB

No variants for Q7MXT8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7MXT8

No associated diseases with Q7MXT8

No regional properties for Q7MXT8

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q7MXT8

Functions

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

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

7 GO annotations of molecular function

Name Definition
(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity Catalysis of the reaction: (3R)-3-hydroxytetradecanoyl-
3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity Catalysis of the reaction: (3R)-3-hydroxydecanoyl-
3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Catalysis of the reaction: (3R)-3-hydroxyoctanoyl-
3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Catalysis of the reaction: (3R)-3-hydroxypalmitoyl-
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.

2 GO annotations of biological process

Name Definition
fatty acid biosynthetic process The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
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
MQKQQTLKDK FCLQGKGLHT GLDIHITFCP APEESGYKIK RVDLEGQPVI DAIADNVHST
70 80 90 100 110 120
RRGTVLKKGE VSVSTIEHAM AALYALGVDN CLIEVDAPEF PILDGSAEPY VSEIKRVGLV
130 140 150 160 170 180
EQETPRDYYI IKKRMEVSDP ESNSKLILLP DDEFTVDVHI AFPSKVLSNQ FASLETLSDF
190 200 210 220 230 240
EEQIAGARTF VFVREVQMLL EANLIKGGDL DNALVIYDEP LAQDRLDALS DMMGVERKQV
250 260 270 280 290 300
NELGYINNKP LIYDNEPARH KLLDVLGDLA LIGKYIRGRI IATCPGHSIN NKMARLIRKE
310 320 330 340 350 360
IKQNEAQAPV YNPNKEPIMD INRIKELLPH RYPFLLVDKI IEVGPDYIVG VKSVSGNEPF
370 380 390 400 410 420
FPGHFPGEPV MPGVLQVEAM AQVGGLLVLN TLTEPSSYST YFLMIDKVKF RRKVVPGDTL
430 440 450 460
VFKLRMISEI RRGVANMRGL AFVGEQLACE AEFMAQIIQN KE