CAZyme Information: MGYG000002475_03333

Basic Information

• Species: Lactonifactor longoviformis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lactonifactor; Lactonifactor longoviformis
• CAZyme ID: MGYG000002475_03333
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
245	MGYG000002475_283|CGC1	27869.9	8.6381

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002475	4812037	Isolate	Germany	Europe

• Gene Location: Start: 3678; End: 4415 Strand: +

Full Sequence      

MKRKRRKRHPVRKAVLGLLVIFFCTALGAGTVWGMKGYGMYQEALTEKPLDVRVEEVRNR
EDFTPYSELPQFYIKAAVSVEDHRFFDHWGVDLIAIGRAVWNDIKAMSFVEGGSTITQQL
AKNLLFTQDKKMERKAAEVFAALEIESNYTKEEIFELYANTVYFGSGYYGIGEAARGYFG
KSPLELTDYESAMLAGIPNAPSAYSPDTNKELASRRVNHVLKSMVRHKLITREEAGEIEK
SFPFQ

Enzyme Prediction     

No EC number prediction in MGYG000002475_03333.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	58	225	1e-62	0.943502824858757

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	2.80e-81	48	225	3	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.
TIGR02074	PBP_1a_fam	1.16e-77	59	243	1	184	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]
COG0744	MrcB	1.64e-69	65	235	80	251	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	3.68e-66	10	237	1	243	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	3.03e-44	18	234	8	239	penicillin-binding protein 1a; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYX26381.1	1.39e-101	12	239	4	231
ADL05597.1	2.59e-81	29	245	2	219
ASB42272.1	2.75e-81	6	235	5	234
ANU54501.1	2.75e-81	6	235	5	234
QQR31552.1	2.75e-81	6	235	5	234

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	2.03e-43	63	237	22	196	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	8.08e-43	63	237	22	196	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
4OON_A	7.71e-35	66	226	44	204	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	7.97e-35	67	234	46	213	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]
3UDF_A	2.43e-34	66	234	44	212	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P70997	1.89e-41	63	240	76	253	Penicillin-binding protein 2D OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpG PE=2 SV=3
O87579	2.38e-39	60	237	67	244	Penicillin-binding protein 1A OS=Neisseria lactamica OX=486 GN=mrcA PE=3 SV=1
O86088	4.43e-39	60	237	67	244	Penicillin-binding protein 1A OS=Neisseria cinerea OX=483 GN=mrcA PE=3 SV=1
P38050	4.68e-39	59	235	66	241	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
O66874	4.91e-39	63	237	65	239	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 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
0.950066	0.041541	0.003670	0.000384	0.000191	0.004175

TMHMM  Annotations     

start	end
13	35