CAZyme Information: MGYG000000534_02157

Basic Information

• Species: Prevotella sp900543975
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900543975
• CAZyme ID: MGYG000000534_02157
• CAZy Family: CE11
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
463		51834.04	6.6888

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000534	3142227	MAG	Fiji	Oceania

• Gene Location: Start: 10436; End: 11827 Strand: +

Full Sequence      

MNTHKQKSLKGSFSLCGKGLHTGLSLTVTFNPAPENYGYKIQRIDLEGMPIIDAVAEHVV
DTQRGTVLGKGDVRVSTVEHGLAALYALGIDNCLIQVNGPEFPILDGSAAMYITKIEEVG
IEELNAPKDWYIIRKKIEVKDEETGSCITILPDEEFSLTAMCSFNSKFINSQFATLDKMD
AFPTEIAQARTFVFVRDIEPLLKANLIKGGDLDNAIVIYEKQTTQERLDQLADFLKVPHM
DATKLGYIQHKPLVWENECTRHKLLDIIGDMALIGKPIKGRIIATRPGHTINNKFARQMR
REIRKHEIQAPIYDPNDAPVMDNVRIRELLPHRYPMQLVDKVIALGATSIVGVKNITANE
PFFQGHFPQEPVMPGVLQIEAMAQCGGLLVLNNLEEPERWSTYFLKIDDVKFRQKVVPGD
TLMFKVDLLAPVRHGISSMKGYVFVGDHVVSEATFTAQIVKNK

Enzyme Prediction     

No EC number prediction in MGYG000000534_02157.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE11	6	299	3.3e-89	0.988929889298893

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK13188	PRK13188	0.0	5	463	4	463	bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed
pfam03331	LpxC	3.05e-116	6	298	1	268	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	2.71e-105	5	298	3	271	UDP-3-O-acyl-N-acetylglucosamine deacetylase.
COG0774	LpxC	4.46e-88	5	297	3	273	UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis].
TIGR00325	lpxC	4.10e-74	5	308	2	280	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
QVJ82182.1	6.73e-304	1	463	1	463
ADE83477.1	7.00e-303	5	463	2	460
QYR10872.1	7.27e-303	5	463	3	461
ALO48551.1	8.10e-300	5	463	3	461
QUB46881.1	1.90e-298	5	463	3	461

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4MDT_A	2.41e-51	5	295	3	271	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	2.94e-51	5	295	3	271	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	3.37e-51	5	295	3	271	CrystalStructure of the Escherichia coli LpxC/LPC-138 complex [Escherichia coli]
6MOO_A	1.36e-49	3	299	7	280	Co-Crystalstructure of P. aeruginosa LpxC-achn975 complex [Pseudomonas aeruginosa]
3NZK_A	1.60e-49	5	295	8	276	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8A015	4.96e-258	5	463	3	461	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	4.81e-209	5	463	3	461	Bifunctional enzyme LpxC/FabZ OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=lpxC/fabZ PE=3 SV=1
Q8KBX0	1.53e-120	6	463	5	466	Bifunctional enzyme LpxC/FabZ OS=Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) OX=194439 GN=lpxC/fabZ PE=3 SV=1
Q1D2K0	2.38e-60	2	308	4	285	UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Myxococcus xanthus (strain DK1622) OX=246197 GN=lpxC PE=3 SV=1
Q2IPK1	1.47e-55	1	321	1	293	UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Anaeromyxobacter dehalogenans (strain 2CP-C) OX=290397 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
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000534_02157.