dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Paenibacillus_B sp900539405

Lineage

Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B sp900539405

CAZyme ID

MGYG000002817_01286

CAZy Family

CBM50

CAZyme Description

Gamma-D-glutamyl-L-diamino acid endopeptidase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
404		45652.73	6.6337

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002817	6425839	MAG	United States	North America

Gene Location

Start: 205452; End: 206666 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000002817_01286.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06229	M14_Endopeptidase_I	3.94e-105	158	394	1	238	Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I. Peptidase M14-like domain of Gamma-D-glutamyl-L-diamino acid endopeptidase 1 (also known as Gamma-D-glutamyl-meso-diaminopimelate peptidase I, and Endopeptidase I (ENP1); EC 3.4.19.11). ENP1 is a member of the M14 family of metallocarboxypeptidases (MCPs), and is classified as belonging to subfamily C. However it has an exceptional type of activity of hydrolyzing the gamma-D-Glu-(L)meso-diaminopimelic acid (gamma-D-Glu-Dap) bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala peptides. ENP1 has a different substrate specificity and cellular role than MpaA (MpaA does not belong to this group). ENP1 hydrolyzes the gamma-D-Glu-Dap bond of MurNAc-tripeptide and MurNAc-tetrapeptide, as well as the amide bond of free tripeptide and tetrapeptide. ENP1 is active on spore cortex peptidoglycan, and is produced at stage IV of sporulation in forespore and spore integuments.
smart00631	Zn_pept	1.13e-43	117	372	6	259	Zn_pept domain.
cd00596	Peptidase_M14_like	7.43e-36	162	384	5	206	M14 family of metallocarboxypeptidases and related proteins. The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.
pfam00246	Peptidase_M14	1.04e-31	118	372	1	263	Zinc carboxypeptidase.
cd06227	M14-CPA-like	1.44e-20	163	322	9	146	Peptidase M14 carboxypeptidase A-like domain; uncharacterized subfamily. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SYX85282.1	2.65e-203	1	398	1	398
QKS44867.1	7.83e-153	3	402	2	402
QYR23328.1	1.34e-144	3	398	2	397
BBH19109.1	1.44e-143	3	394	2	393
QHT64030.1	1.59e-143	3	398	1	396

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7EQX_C	9.60e-12	117	348	11	223	ChainC, Carboxypeptidase B [Aedes aegypti],7EQX_D Chain D, Carboxypeptidase B [Aedes aegypti],7EQZ_A Chain A, Carboxypeptidase B [Aedes aegypti]
3D66_A	4.25e-09	84	371	89	387	Crystalstructure of Thrombin-Activatable Fibrinolysis Inhibitor (TAFI) [Homo sapiens],3D66_B Crystal structure of Thrombin-Activatable Fibrinolysis Inhibitor (TAFI) [Homo sapiens],3D66_C Crystal structure of Thrombin-Activatable Fibrinolysis Inhibitor (TAFI) [Homo sapiens],3D67_A Crystal structure of Thrombin-Activatable Fibrinolysis Inhibitor (TAFI) in complex with 2-guanidino-ethyl-mercaptosuccinic acid (GEMSA) [Homo sapiens],3D67_B Crystal structure of Thrombin-Activatable Fibrinolysis Inhibitor (TAFI) in complex with 2-guanidino-ethyl-mercaptosuccinic acid (GEMSA) [Homo sapiens],3D67_C Crystal structure of Thrombin-Activatable Fibrinolysis Inhibitor (TAFI) in complex with 2-guanidino-ethyl-mercaptosuccinic acid (GEMSA) [Homo sapiens]
3LMS_A	8.70e-09	120	371	7	272	Structureof human activated thrombin-activatable fibrinolysis inhibitor, TAFIa, in complex with tick-derived funnelin inhibitor, TCI. [Homo sapiens]
7NEE_A	9.41e-09	84	371	65	363	ChainA, Carboxypeptidase B2 [Homo sapiens]
7NEU_A	9.41e-09	84	371	65	363	ChainA, Carboxypeptidase B2 [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q03415	1.28e-90	58	398	5	394	Gamma-D-glutamyl-L-diamino acid endopeptidase 1 OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P54497	3.57e-61	61	398	12	372	Uncharacterized protein YqgT OS=Bacillus subtilis (strain 168) OX=224308 GN=yqgT PE=3 SV=1
O05495	1.01e-11	5	101	4	95	Putative sporulation-specific glycosylase YdhD OS=Bacillus subtilis (strain 168) OX=224308 GN=ydhD PE=1 SV=2
Q9EQV9	9.85e-09	103	371	106	385	Carboxypeptidase B2 OS=Rattus norvegicus OX=10116 GN=Cpb2 PE=2 SV=1
Q96IY4	2.32e-08	84	371	88	386	Carboxypeptidase B2 OS=Homo sapiens OX=9606 GN=CPB2 PE=1 SV=2

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
1.000029	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000002817_01286.

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