CAZyme Information: MGYG000003423_01283

Basic Information

• Species: W3P20-009 sp900766825
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; W3P20-009; W3P20-009; W3P20-009 sp900766825
• CAZyme ID: MGYG000003423_01283
• CAZy Family: CE11
• CAZyme Description: UDP-3-O-acyl-N-acetylglucosamine deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
306		33543.33	5.2298

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003423	2824109	MAG	Fiji	Oceania

• Gene Location: Start: 42865; End: 43785 Strand: +

Full Sequence      

MEKQTTIASQASFEGKGLHTGAYVHLTIKPAPVDFGFQFCRTDLEGRPTFAALATSVNFT
QRGTVLAGPNGEKVSTIEHLMSALRALGVDNCLIELDGPEVPILDGSAKPFVEALRAMGP
LVEQDAERRYMVVTHKVVYEEKEKGLRIIALPEDYFAATVNIAFDGSRCLGNQWAQLEDL
TSEYNDVYDCRTFVFLHEVQPLLQMGLIKGGDLDNAIVFVEGELTPEQREALAKQLGKTD
ITIHPSGVLNDRDLKYANEAARHKLLDLVGDLALVGRPIKGRILATRSGHGSNTAFARML
MSEFPA

Enzyme Prediction     

No EC number prediction in MGYG000003423_01283.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE11	4	225	9.1e-67	0.8007380073800738

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK13188	PRK13188	8.72e-143	1	300	2	298	bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed
pfam03331	LpxC	4.35e-118	4	302	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.
PRK13186	lpxC	1.03e-115	1	303	1	275	UDP-3-O-acyl-N-acetylglucosamine deacetylase.
COG0774	LpxC	9.18e-99	1	302	1	277	UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis].
TIGR00325	lpxC	7.09e-59	3	306	2	277	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]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASB49507.1	3.33e-99	2	303	3	302
AVV53596.1	4.17e-96	1	303	1	300
AOH39727.1	4.17e-96	1	303	1	300
AEV32817.1	2.65e-95	1	303	1	300
BCG53338.1	4.50e-93	2	300	3	297

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4J3D_A	3.12e-53	1	303	1	277	Pseudomonasaeruginosa LpxC in complex with a hydroxamate inhibitor [Pseudomonas aeruginosa PAO1],4J3D_B Pseudomonas aeruginosa LpxC in complex with a hydroxamate inhibitor [Pseudomonas aeruginosa PAO1]
5U3B_A	3.30e-53	1	303	1	277	Pseudomonasaeruginosa LpxC in complex with NVS-LPXC-01 [Pseudomonas aeruginosa PAO1],5U3B_B Pseudomonas aeruginosa LpxC in complex with NVS-LPXC-01 [Pseudomonas aeruginosa PAO1],6MAE_A CHAIN A. UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase PA-LPXC Complexed with (R)-3-((S)-3-(4-(cyclopropylethynyl)phenyl)-2-oxooxazolidin-5-yl)-N-hydroxy-2-methyl-2-(methylsulfonyl)propenamide [Pseudomonas aeruginosa PAO1]
7K99_A	3.68e-53	1	303	1	277	CrystalStructure of P. aeruginosa LpxC with N-Hydroxyformamide inhibitor 19 [Pseudomonas aeruginosa PAO1],7K99_C Crystal Structure of P. aeruginosa LpxC with N-Hydroxyformamide inhibitor 19 [Pseudomonas aeruginosa PAO1],7K9A_A Crystal Structure of P. aeruginosa LpxC with N-Hydroxyformamide inhibitor [Pseudomonas aeruginosa PAO1],7K9A_C Crystal Structure of P. aeruginosa LpxC with N-Hydroxyformamide inhibitor [Pseudomonas aeruginosa PAO1]
5UPG_A	3.78e-53	1	303	2	278	Crystalstructure of LpxC from Pseudomonas aeruginosa in complex with PF-5081090 [Pseudomonas aeruginosa PAO1],6C9C_A Crystal structure of LpxC from Pseudomonas aeruginosa in complex with racemic ligand PT803 [Pseudomonas aeruginosa UCBPP-PA14],6CAX_A Crystal structure of LpxC from Pseudomonas aeruginosa in complex with PT805 [Pseudomonas aeruginosa],6DUI_A Crystal structure of LpxC from Pseudomonas aeruginosa in complex with PT801 [Pseudomonas aeruginosa LESB58],6E54_A Crystal structure of LpxC from Pseudomonas aeruginosa in complex with ligand PT802 [Pseudomonas aeruginosa PAO1]
5U39_A	5.87e-53	3	303	5	279	Pseudomonasaeruginosa LpxC in complex with CHIR-090 [Pseudomonas aeruginosa PAO1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8A015	9.69e-90	1	303	1	300	Bifunctional enzyme LpxC/FabZ OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=lpxC/fabZ PE=3 SV=1
Q7MXT8	2.81e-89	1	303	1	300	Bifunctional enzyme LpxC/FabZ OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=lpxC/fabZ PE=3 SV=1
Q8KBX0	3.92e-78	4	300	5	301	Bifunctional enzyme LpxC/FabZ OS=Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) OX=194439 GN=lpxC/fabZ PE=3 SV=1
B4RFF2	2.57e-60	4	303	3	276	UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Phenylobacterium zucineum (strain HLK1) OX=450851 GN=lpxC PE=3 SV=1
Q2S9Z8	4.62e-57	1	303	1	277	UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Hahella chejuensis (strain KCTC 2396) OX=349521 GN=lpxC PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000049	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003423_01283.