CAZyme Information: MGYG000000027_00682

Basic Information

• Species: Mitsuokella jalaludinii
• Lineage: Bacteria; Firmicutes_C; Negativicutes; Selenomonadales; Selenomonadaceae; Mitsuokella; Mitsuokella jalaludinii
• CAZyme ID: MGYG000000027_00682
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
278		31556.22	8.0657

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000027	2393573	Isolate	United Kingdom	Europe

• Gene Location: Start: 203459; End: 204295 Strand: -

Full Sequence      

MATRRRRSPKRLIRFLFFLLILFLAAFFVSGGLAVFSAKTWQSAGGFLPRPTQSVPANEM
TDEVHHPGFSDRLSRVIFLRRAVESRVNVRDPHYVKLQDTPDSLQQAIVAVEDRRFYSHH
GFDFEGIARATLVNLQSGEIEEGASTITQQLVKNLFLSHEQSFGRKAEEFVLALDMEWNY
SKDEILEMYLNTIYYGSNYYGIGAASEGYFGKRPRDLALPESAMLAGLPNAPSLYSPYVD
FMMAKKRQFIVLDAMVSCGFIDKTMAEDAKIKPLYLAH

Enzyme Prediction     

No EC number prediction in MGYG000000027_00682.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	90	256	5.8e-67	0.9378531073446328

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	1.87e-90	94	256	15	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	2.10e-87	94	274	4	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	1.07e-82	93	276	77	261	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	2.10e-75	94	274	69	249	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
TIGR02071	PBP_1b	1.86e-53	94	274	149	333	penicillin-binding protein 1B. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAL83720.1	2.42e-121	29	278	30	277
AEB99985.1	7.27e-99	7	278	2	249
AOH48229.1	6.29e-95	3	274	24	289
QNH53709.1	4.63e-94	2	274	18	287
AKT54947.1	3.51e-93	18	276	37	292

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3NB6_A	7.03e-47	67	269	2	197	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
2OQO_A	9.92e-47	67	269	2	197	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]
4OON_A	6.65e-43	95	274	42	221	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	4.84e-42	95	278	43	226	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]
3DWK_A	2.26e-37	83	270	18	205	ChainA, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_B Chain B, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_C Chain C, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_D Chain D, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O87626	1.95e-45	94	275	70	251	Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA PE=3 SV=1
P70997	6.81e-45	93	274	75	256	Penicillin-binding protein 2D OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpG PE=2 SV=3
Q07259	1.06e-44	92	276	47	230	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	1.11e-44	90	276	67	251	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
Q5FAC7	1.29e-44	94	275	70	251	Penicillin-binding protein 1A OS=Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) OX=242231 GN=mrcA PE=3 SV=3

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
0.951017	0.045825	0.000402	0.000314	0.000158	0.002300

TMHMM  Annotations     

start	end
13	35