CAZyme Information: MGYG000003814_01542

Basic Information

• Species: Prevotella sp900548585
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900548585
• CAZyme ID: MGYG000003814_01542
• CAZy Family: GT51
• CAZyme Description: Biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
233	MGYG000003814_67|CGC1	26279.53	10.2663

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003814	1857523	MAG	Canada	North America

• Gene Location: Start: 2578; End: 3279 Strand: -

Full Sequence      

MAVVAFFVSTILSVVVYRFVPVYVTPLMVIRCVGQVIDGHSPRVEHKWVRLGDISPSMPV
AVMGSEDARFLLHHGFDFRQIEQAAKHNASGGRKVGASTISQQTAKNVFLFPDRTWLRKG
LEAYFTVLIELMWSKQRIMEVYLNSIETGDGIYGVEAVARLHFGKSASELTRSECALIAA
TLPNPRKYSSLEPSKYVRSRRARIEANMKFIPKFPAENEDIDKRTVKGGIYKR

Enzyme Prediction     

No EC number prediction in MGYG000003814_01542.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	44	209	5e-52	0.9378531073446328

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK00056	mtgA	2.92e-111	2	208	15	223	monofunctional biosynthetic peptidoglycan transglycosylase; Provisional
TIGR02070	mono_pep_trsgly	1.01e-88	2	208	10	218	monofunctional biosynthetic peptidoglycan transglycosylase. This family is one of the transglycosylases involved in the late stages of peptidoglycan biosynthesis. Members tend to be small, about 240 amino acids in length, and consist almost entirely of a domain described by pfam00912 for transglycosylases. Species with this protein will have several other transglycosylases as well. All species with this protein are Proteobacteria that produce murein (peptidoglycan). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
pfam00912	Transgly	1.27e-68	43	209	10	177	Transglycosylase. The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.
COG0744	MrcB	7.30e-67	1	209	29	241	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
TIGR02074	PBP_1a_fam	1.48e-48	48	208	4	165	penicillin-binding protein, 1A family. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALO48142.1	4.63e-106	6	233	15	242
QNT65514.1	9.32e-106	3	229	14	240
QYR10254.1	2.41e-104	3	231	15	243
AGB29041.1	2.85e-102	6	232	9	233
QUB46829.1	1.97e-100	2	220	11	230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	3.55e-27	48	189	22	164	Crystalstructure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis [Aquifex aeolicus VF5],3D3H_A Crystal structure of a complex of the peptidoglycan glycosyltransferase domain from Aquifex aeolicus and neryl moenomycin A [Aquifex aeolicus],3NB7_A Crystal structure of Aquifex Aeolicus Peptidoglycan Glycosyltransferase in complex with Decarboxylated Neryl Moenomycin [Aquifex aeolicus]
3NB6_A	1.38e-26	48	189	22	164	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
5U2G_A	4.81e-26	31	201	30	196	2.6Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20],5U2G_B 2.6 Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20]
3DWK_A	4.27e-24	34	233	15	216	ChainA, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_B Chain B, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_C Chain C, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_D Chain D, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL]
2OLU_A	6.96e-23	34	201	24	192	StructuralInsight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Apoenzyme [Staphylococcus aureus],2OLV_A Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex [Staphylococcus aureus],2OLV_B Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex [Staphylococcus aureus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8A8H2	1.13e-84	6	227	21	243	Biosynthetic peptidoglycan transglycosylase OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=mtgA PE=3 SV=1
Q3V7G2	3.02e-82	6	233	17	240	Biosynthetic peptidoglycan transglycosylase OS=Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow) OX=272559 GN=mtgA PE=3 SV=1
Q3V815	3.02e-82	6	233	17	240	Biosynthetic peptidoglycan transglycosylase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=mtgA PE=3 SV=1
Q3V7R3	9.79e-69	2	204	15	217	Biosynthetic peptidoglycan transglycosylase OS=Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100) OX=264462 GN=mtgA PE=3 SV=1
B6IWJ6	1.42e-66	17	211	29	218	Biosynthetic peptidoglycan transglycosylase OS=Rhodospirillum centenum (strain ATCC 51521 / SW) OX=414684 GN=mtgA 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
0.995559	0.004412	0.000022	0.000014	0.000007	0.000016

TMHMM  Annotations     

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