CAZyme Information: MGYG000000218_01361

Basic Information

• Species: Acidaminococcus provencensis
• Lineage: Bacteria; Firmicutes_C; Negativicutes; Acidaminococcales; Acidaminococcaceae; Acidaminococcus; Acidaminococcus provencensis
• CAZyme ID: MGYG000000218_01361
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
265		29483.97	6.2423

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000218	2599623	Isolate	China	Asia

• Gene Location: Start: 69280; End: 70077 Strand: +

Full Sequence      

MRKLLYLLILLSAALCYYLTRPVVHTGAGPAPVPAYAAAAAAQEDPLTRLLPGIDVPRPL
RLVYRAWHLKEITRSRIPAEDWVPLKRMSPWLPKALVSVEDKRFYSHHGIDPDGIFRAIL
MNIQADEVVEGGSTITQQVVKNNLLTSEQSLERKILEAGLALVVEIHYSKDEILEMYLNT
TFLGAGATGVQQASETYYGLEPSQLSLSEAAALAGLPYAPSALNPFDNPEGCRERRNLVL
ERMNEQGMITEGEMREAQRQGLHLR

Enzyme Prediction     

No EC number prediction in MGYG000000218_01361.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	79	244	1.3e-63	0.9322033898305084

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02074	PBP_1a_fam	7.30e-87	82	264	4	186	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]
pfam00912	Transgly	2.79e-84	81	244	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.
COG0744	MrcB	3.76e-83	74	262	70	259	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	4.83e-74	76	265	67	252	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
TIGR02071	PBP_1b	4.98e-54	83	262	150	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
ADB46989.1	2.27e-105	1	257	1	256
AEQ23280.1	9.60e-88	1	265	1	256
QTV77901.1	6.12e-70	48	264	51	268
BBG64464.1	1.59e-62	47	249	53	255
QNP76977.1	1.59e-62	47	249	53	255

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	8.29e-51	82	257	22	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]
3NB6_A	3.31e-50	82	257	22	197	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
4OON_A	4.53e-38	95	251	54	210	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	6.56e-38	41	253	3	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]
3UDF_A	6.44e-37	83	264	42	223	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O66874	8.60e-46	82	257	65	240	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
Q07259	5.63e-44	81	265	48	231	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
P39793	4.86e-43	70	259	85	275	Penicillin-binding protein 1A/1B OS=Bacillus subtilis (strain 168) OX=224308 GN=ponA PE=1 SV=1
P02918	6.31e-41	74	251	64	237	Penicillin-binding protein 1A OS=Escherichia coli (strain K12) OX=83333 GN=mrcA PE=1 SV=1
O87626	7.69e-41	92	263	80	251	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
0.915411	0.063359	0.020787	0.000146	0.000085	0.000232

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000218_01361.