dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000698_01013

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Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; DTU072; CAG-1782;

CAZyme ID

MGYG000000698_01013

CAZy Family

GT51

CAZyme Description

Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
720		80208.62	6.0827

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000698	1742225	MAG	Kazakhstan	Asia

Gene Location

Start: 10992; End: 13154 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000698_01013.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT51	38	202	1.5e-68	0.9265536723163842

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02074	PBP_1a_fam	3.43e-166	41	557	4	517	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	5.30e-158	5	557	33	585	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	2.49e-103	41	589	69	740	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
pfam00912	Transgly	4.56e-87	40	203	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.
TIGR02071	PBP_1b	5.36e-86	34	571	142	692	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDF78290.1	2.80e-115	11	564	34	589
AWV39925.1	2.80e-115	11	564	34	589
ARC71535.1	2.80e-115	11	564	34	589
ASV14639.1	2.80e-115	11	564	34	589
QAT52435.1	2.80e-115	11	564	34	589

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZG8_B	7.91e-71	123	555	3	447	CrystalStructure of Penicillin Binding Protein 4 from Listeria monocytogenes in the Ampicillin bound form [Listeria monocytogenes],3ZG9_B Crystal Structure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the Cefuroxime bound form [Listeria monocytogenes],3ZGA_B Crystal Structure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the Carbenicillin bound form [Listeria monocytogenes]
3DWK_A	1.97e-67	31	582	19	602	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]
3ZG7_B	2.92e-66	123	555	3	447	CrystalStructure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the apo form [Listeria monocytogenes]
2OLU_A	5.58e-64	31	582	28	611	StructuralInsight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Apoenzyme [Staphylococcus aureus],2OLV_A Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex [Staphylococcus aureus],2OLV_B Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex [Staphylococcus aureus]
3UDF_A	5.51e-56	23	539	21	687	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 download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38050	1.52e-100	42	586	70	614	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
A0A0H2ZMF9	2.02e-81	41	581	113	665	Penicillin-binding protein 2a OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=pbp2a PE=1 SV=1
Q8DNB6	2.02e-81	41	581	113	665	Penicillin-binding protein 2a OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pbp2a PE=1 SV=1
P70997	2.39e-80	41	588	76	628	Penicillin-binding protein 2D OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpG PE=2 SV=3
P39793	1.58e-76	41	589	97	663	Penicillin-binding protein 1A/1B OS=Bacillus subtilis (strain 168) OX=224308 GN=ponA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000698_01013.