CAZyme Information: MGYG000000413_02559

Basic Information

• Lineage: Bacteria; Firmicutes_B; Peptococcia; Peptococcales; Peptococcaceae; UBA7185
• CAZyme ID: MGYG000000413_02559
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
236	MGYG000000413_214|CGC1	26813.88	4.7121

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000413	2856126	MAG	Sweden	Europe

• Gene Location: Start: 441; End: 1151 Strand: +

Full Sequence      

MIKRLFGLFRRIVLLLVICAVAAGGFLVYEGYQVYEEALLETPVEQVMAEIQNQPHYTTL
EQIPQIYIDAVISTEDHRFYVHSGLDVIAIARALWHDIQAGKMVEGGSTITQQLAKNQFF
TQKKELTRKIAEVFMVRQIEKLYEKDEILELYINSIYYGEGYYCIYDASMGYFGKEPAAL
NAQECTLLAGIPNAPSVYAPTANPDLALQRQRQVVQDMVTWGYLTREEAVAILPQS

Enzyme Prediction     

No EC number prediction in MGYG000000413_02559.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	46	219	5.9e-62	0.9830508474576272

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	2.54e-77	46	219	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	1.79e-73	57	231	4	178	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	6.50e-69	1	231	9	253	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	1.49e-63	2	229	5	241	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	3.56e-47	9	228	3	239	penicillin-binding protein 1a; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUO38940.1	3.37e-90	11	233	10	232
QHB22227.1	3.46e-82	10	226	5	221
QEI32894.1	3.46e-82	10	226	5	221
QRT31378.1	3.46e-82	10	226	5	221
QJU22158.1	1.18e-81	30	230	28	228

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	3.77e-47	57	228	22	193	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	1.51e-46	57	228	22	193	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
4OON_A	1.70e-35	63	235	47	219	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]
3UDF_A	1.36e-34	61	228	45	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]
5U2G_A	3.84e-34	60	235	45	220	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
Q07259	1.80e-43	3	228	2	219	Putative transglycosylase H16_A0665 OS=Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) OX=381666 GN=H16_A0665 PE=3 SV=2
O66874	1.86e-42	57	228	65	236	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
P38050	5.74e-41	8	230	9	242	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
P02918	1.25e-38	9	228	3	239	Penicillin-binding protein 1A OS=Escherichia coli (strain K12) OX=83333 GN=mrcA PE=1 SV=1
O87626	1.39e-37	52	228	65	241	Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA 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
0.982753	0.008734	0.006106	0.000076	0.000039	0.002320

TMHMM  Annotations     

start	end
7	29