CAZyme Information: MGYG000001081_02546

Basic Information

• Species: Acutalibacter sp900755895
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Acutalibacter; Acutalibacter sp900755895
• CAZyme ID: MGYG000001081_02546
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
234	MGYG000001081_173|CGC2	26209.97	4.3834

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001081	3715652	MAG	Sweden	Europe

• Gene Location: Start: 144225; End: 144929 Strand: -

Full Sequence      

MKVLRIVRNIVLWALALCLCAVAALALLGWEMYTQALEAMPLDQRVEQVRAQESYTAFED
LPDTYVEAVLAAEDHRFYQHNGMDVIALGRALVNDIKAMSFVEGGSTITQQLAKNLFFTQ
EKRLTRKVAEMFMAFHIEANYSKEEIFELYVNSIYFGSGCYDVASASQTYFGVEPSAMDA
DQCTLLAGIPNAPSVYDPTVNPDLSQQRQRQVVELMVKYEYLTANEASTILTAA

Enzyme Prediction     

No EC number prediction in MGYG000001081_02546.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	50	217	2.1e-61	0.943502824858757

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	3.71e-79	41	217	4	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	6.75e-73	55	229	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	3.25e-66	58	229	81	253	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	5.07e-64	55	227	69	241	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK13481	PRK13481	1.56e-41	32	232	26	230	glycosyltransferase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASB42272.1	1.27e-98	2	230	9	237
ANU54501.1	1.27e-98	2	230	9	237
QQR31552.1	1.27e-98	2	230	9	237
QUO38940.1	1.32e-79	1	231	1	232
QRP41835.1	1.46e-79	1	227	1	227

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	1.80e-44	55	226	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	7.19e-44	55	226	22	193	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
4OON_A	5.30e-37	58	222	44	208	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	6.40e-37	58	226	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]
5U2G_A	1.05e-34	60	226	47	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38050	8.00e-42	60	229	74	243	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
O66874	5.22e-40	55	226	65	236	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
P39793	5.60e-40	44	226	85	269	Penicillin-binding protein 1A/1B OS=Bacillus subtilis (strain 168) OX=224308 GN=ponA PE=1 SV=1
O87579	5.82e-39	55	226	70	241	Penicillin-binding protein 1A OS=Neisseria lactamica OX=486 GN=mrcA PE=3 SV=1
O86088	1.09e-38	55	226	70	241	Penicillin-binding protein 1A OS=Neisseria cinerea OX=483 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
0.999153	0.000140	0.000143	0.000001	0.000001	0.000598

TMHMM  Annotations     

start	end
12	34