CAZyme Information: MGYG000001784_01635

Basic Information

• Species: Mailhella sp003150275
• Lineage: Bacteria; Desulfobacterota; Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae; Mailhella; Mailhella sp003150275
• CAZyme ID: MGYG000001784_01635
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
272		30775.04	11.3114

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001784	3348621	MAG	Denmark	Europe

• Gene Location: Start: 9209; End: 10027 Strand: -

Full Sequence      

MAVFWHGGGSPPEFRLGKRRKRTYSFPVMTADMVRNSARRRGFPARGILLGLALLLALDI
GRYLFWPPVSRLAFINPPFTSMMEYRREQQEARQTEQGKKPHPPAPRQTWVPLKRISPHL
RKAVVISEDDTFWKHSGFNFSTMRDALERNLKKGRLAAGGSTITQQLAKNLWFSPEKSIL
RKVKEAIMACRLELALDKERILELYLNVAEWGSGIYGAEAAARHYFGKSAAALTTYEAAS
MAAVLPAPLKRTPSSPLVRKLAARLVKRMPLY

Enzyme Prediction     

No EC number prediction in MGYG000001784_01635.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	107	255	2.5e-56	0.8361581920903954

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK00056	mtgA	2.92e-81	72	270	30	224	monofunctional biosynthetic peptidoglycan transglycosylase; Provisional
pfam00912	Transgly	3.52e-67	105	269	10	176	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.
TIGR02070	mono_pep_trsgly	5.46e-66	63	269	14	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]
COG0744	MrcB	5.68e-61	63	269	38	240	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
TIGR02074	PBP_1a_fam	1.46e-55	107	248	1	142	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
AAM73242.1	2.11e-65	46	254	5	206
ABM27980.1	2.67e-64	33	269	1	242
ACF45326.1	6.13e-64	48	254	7	207
AAS96769.1	1.07e-63	33	269	1	242
ADP87274.1	1.07e-63	33	269	1	242

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3NB6_A	2.02e-34	110	253	22	165	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
2OQO_A	7.90e-34	110	253	22	165	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]
3UDF_A	3.08e-23	111	253	42	184	ChainA, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDF_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii]
4OON_A	6.57e-22	107	253	38	184	Crystalstructure of PBP1a in complex with compound 17 ((4Z,8S,11E,14S)-5-(2-amino-1,3-thiazol-4-yl)-14-(5,6-dihydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-8-formyl-2-methyl-6-oxo-3,10-dioxa-4,7,11-triazatetradeca-4,11-diene-2,12,14-tricarboxylic acid) [Pseudomonas aeruginosa PAO1]
5U2G_A	9.05e-22	111	253	43	185	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q5P6J8	1.55e-48	76	248	37	202	Biosynthetic peptidoglycan transglycosylase OS=Aromatoleum aromaticum (strain EbN1) OX=76114 GN=mtgA PE=3 SV=2
Q2YBM4	3.09e-48	63	248	21	201	Biosynthetic peptidoglycan transglycosylase OS=Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71) OX=323848 GN=mtgA PE=3 SV=1
Q478U7	1.00e-46	52	270	8	226	Biosynthetic peptidoglycan transglycosylase OS=Dechloromonas aromatica (strain RCB) OX=159087 GN=mtgA PE=3 SV=1
A1K3B8	2.82e-46	76	250	37	204	Biosynthetic peptidoglycan transglycosylase OS=Azoarcus sp. (strain BH72) OX=418699 GN=mtgA PE=3 SV=1
Q3SFZ8	4.09e-46	107	248	61	202	Biosynthetic peptidoglycan transglycosylase OS=Thiobacillus denitrificans (strain ATCC 25259) OX=292415 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
0.999901	0.000092	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
43	65