CAZyme Information: MGYG000000742_00867

Basic Information

• Species: Dialister sp900541605
• Lineage: Bacteria; Firmicutes_C; Negativicutes; Veillonellales; Dialisteraceae; Dialister; Dialister sp900541605
• CAZyme ID: MGYG000000742_00867
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
303	MGYG000000742_20|CGC1	32972.39	6.9209

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000742	2345274	MAG	Kazakhstan	Asia

• Gene Location: Start: 3613; End: 4524 Strand: -

Full Sequence      

MKKFLFLLLILGAAVYWGISQGDELSRNAVKSHTSSAVVAQKDSRPAEDTGVLATIKGTV
SSLASGISSSGTKESNSGNPGKEPPASPKSAKAEAQTLQEKWNDVAHFKPALESWVHREK
FVPYDKIPDLLKKGIIATEDRRYYDHGAIDLIGVGRAAFTNYMAGETVEGGSTIAQQTVK
NIFLSNERTMTRKVEELALAVQLEHNYSKDQILELYLNTIYFGHGAYGVGEASRTYFGRE
PKDLDLSQCAMLAGLPQAPSAYDPIAHPQEGAKRMTTVLALMAQEGYITPEQAATAALHL
WLK

Enzyme Prediction     

No EC number prediction in MGYG000000742_00867.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	117	282	1e-66	0.9322033898305084

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	2.04e-88	114	283	9	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	1.32e-85	117	301	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	8.28e-83	117	296	75	254	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	1.23e-74	118	296	66	244	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	5.99e-55	122	292	69	239	penicillin-binding protein 1a; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBK25656.1	7.26e-116	3	303	2	304
AOH38594.1	2.75e-85	96	303	63	270
AXL21687.1	1.73e-64	98	296	54	253
AXB81629.1	1.84e-61	98	296	50	249
ARF99932.1	2.34e-61	111	293	73	255

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	2.09e-55	116	292	17	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	8.35e-55	116	292	17	193	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
5U2G_A	1.67e-38	127	292	48	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]
5FGZ_A	2.24e-37	121	291	158	332	E.coli PBP1b in complex with FPI-1465 [Escherichia coli K-12],5HL9_A E. coli PBP1b in complex with acyl-ampicillin and moenomycin [Escherichia coli K-12],5HLA_A E. coli PBP1b in complex with acyl-cephalexin and moenomycin [Escherichia coli K-12],5HLB_A E. coli PBP1b in complex with acyl-aztreonam and moenomycin [Escherichia coli K-12],5HLD_A E. coli PBP1b in complex with acyl-CENTA and moenomycin [Escherichia coli K-12],6YN0_A Structure of E. coli PBP1b with a FtsN peptide activating transglycosylase activity [Escherichia coli K-12],7LQ6_A Chain A, Penicillin-binding protein 1B [Escherichia coli K-12]
3VMA_A	2.37e-37	121	291	179	353	CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38050	2.52e-52	122	296	70	244	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
O66874	5.05e-50	116	292	60	236	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
P39793	1.84e-48	109	292	85	269	Penicillin-binding protein 1A/1B OS=Bacillus subtilis (strain 168) OX=224308 GN=ponA PE=1 SV=1
O87626	2.91e-48	103	292	39	241	Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA PE=3 SV=1
Q07259	6.37e-47	111	289	39	216	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.376250	0.587882	0.034692	0.000368	0.000302	0.000490

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000742_00867.