CAZyme Information: MGYG000004405_00391

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-269
• CAZyme ID: MGYG000004405_00391
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
238	MGYG000004405_2|CGC1	27258.97	4.8331

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004405	1459374	MAG	Israel	Asia

• Gene Location: Start: 147346; End: 148062 Strand: -

Full Sequence      

MGDVMKILKNILFKIIVFIFILLIICTSILLFLGYNYYSNALKENSLSSRVNTIRNDNDF
VNFDDLNEDYINAVIATEDHRFYEHGAIDPIAIARAIYINIKHMELQEGGSTITQQVAKN
VCFDQNKNAIRKIAEFFAAYDLEKNYNKKEIFELYVNTAYFGNGYYGIKQASEGYYNKEP
KELNLSEASMLAGVPNAPSVYAPTKNPDLAEQRQAQVLKRMLEYGYISQEDFDSVINN

Enzyme Prediction     

No EC number prediction in MGYG000004405_00391.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	55	221	4.3e-63	0.9378531073446328

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	9.59e-81	59	222	14	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	1.73e-78	60	237	4	181	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	4.56e-73	43	233	61	252	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	4.87e-67	60	237	69	246	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	3.73e-47	71	234	79	242	penicillin-binding protein 1a; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUO38940.1	2.69e-75	5	238	1	234
ADL05597.1	6.24e-73	34	235	10	211
QNM09777.1	1.13e-71	34	236	39	241
QRV21928.1	2.79e-71	38	235	2	199
SET89048.1	5.34e-71	34	235	29	230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3NB6_A	1.11e-49	60	237	22	199	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
2OQO_A	1.57e-49	60	237	22	199	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	3.18e-38	61	236	42	217	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	3.68e-38	61	236	42	217	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	5.30e-38	65	236	47	218	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
O66874	1.21e-44	60	237	65	242	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
Q07259	3.39e-41	59	236	48	224	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
P38050	1.59e-40	73	231	82	240	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
O87579	1.90e-39	59	237	69	247	Penicillin-binding protein 1A OS=Neisseria lactamica OX=486 GN=mrcA PE=3 SV=1
O87626	4.85e-39	59	236	69	246	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
0.998541	0.000396	0.000020	0.000003	0.000002	0.001070

TMHMM  Annotations     

start	end
15	37