CAZyme Information: MGYG000000948_01378

Basic Information

• Species: UMGS1994 sp900553945
• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; UMGS1994; UMGS1994 sp900553945
• CAZyme ID: MGYG000000948_01378
• CAZy Family: CBM50
• CAZyme Description: Gamma-D-glutamyl-L-diamino acid endopeptidase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
375		42512.38	8.7621

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000948	1605952	MAG	China	Asia

• Gene Location: Start: 26810; End: 27937 Strand: +

Full Sequence      

METLKLGSTGTIVQYLQSTLKTLGFYNGKIDGIFGNQTKNAVIIFQREFGISQDGIVGQN
TWNKLSSFFYIVPTDISYGSNILEINSKGFTSKFPFLEQGNIGYSVLGKELKYFKFGNGS
KQVFYSGSIHGNEWINTTLLMKFLENLCTAYLNRENIWGYPAVSLFNQYTLYIVPLANPD
GVDLVVSNLQKYDLKSYNSARQLSLNYPSIPFPNGWKANIEGIDLNLQFPAEWEMARSNK
FSQGYTKPGPRDYVGPSPLYAPEARALYNFTLSKRFSLILAYHSQGETIYWKFLNYLPPR
SYEIGRHFSQVSGYLLETTPYASGFAGYKDWFIQNYNLPGYTIETGLGENPLPISQFQDI
YNKNIGILILGMLLV

Enzyme Prediction     

No EC number prediction in MGYG000000948_01378.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06229	M14_Endopeptidase_I	1.96e-90	123	368	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	1.74e-37	102	361	27	277	Zn_pept domain.
cd00596	Peptidase_M14_like	1.16e-33	123	368	1	216	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	5.25e-29	102	364	21	284	Zinc carboxypeptidase.
cd06904	M14_MpaA-like	6.39e-22	102	369	4	210	Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins. Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A (MpaA) and related proteins. MpaA is a member of the M14 family of metallocarboxypeptidases (MCPs), however it has an exceptional type of activity, it hydrolyzes the gamma-D-glutamyl-meso-diaminopimelic acid (gamma-D-Glu-Dap) bond in murein peptides. MpaA is specific for cleavage of the gamma-D-Glu-Dap bond of free murein tripeptide; it may also cleave murein tetrapeptide. MpaA has a different substrate specificity and cellular role than endopeptidase I, ENP1 (ENP1 does not belong to this group). MpaA works on free murein peptide in the recycling pathway.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWT55181.1	2.72e-129	1	372	1	423
AUS95891.1	9.95e-116	1	371	1	420
AGC68495.1	2.51e-113	1	371	1	420
ANW98855.1	2.51e-113	1	371	1	420
AGI39513.1	2.51e-113	1	371	1	420

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5TV7_A	1.38e-09	7	65	112	169	ChainA, Putative peptidoglycan-binding/hydrolysing protein [Clostridioides difficile 630],5TV7_B Chain B, Putative peptidoglycan-binding/hydrolysing protein [Clostridioides difficile 630]
3BKH_A	1.74e-09	4	67	12	75	ChainA, lytic transglycosylase [Pseudomonas phage phiKZ],3BKV_A Chain A, lytic transglycosylase [Pseudomonas phage phiKZ]
6TCI_A	1.12e-08	7	65	10	68	Thecrystal structure of SleB N-terminal domain [Bacillus cereus ATCC 14579]
4FET_A	1.74e-07	7	65	10	68	Catalyticdomain of germination-specific lytic tansglycosylase SleB from Bacillus anthracis [Bacillus anthracis],4FET_B Catalytic domain of germination-specific lytic tansglycosylase SleB from Bacillus anthracis [Bacillus anthracis]
5NM7_A	2.56e-07	2	67	3	67	Crystalstructure of Burkholderia AP3 phage endolysin [Burkholderia],5NM7_G Crystal structure of Burkholderia AP3 phage endolysin [Burkholderia]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q03415	8.64e-77	77	374	109	396	Gamma-D-glutamyl-L-diamino acid endopeptidase 1 OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P54497	1.11e-61	78	368	84	368	Uncharacterized protein YqgT OS=Bacillus subtilis (strain 168) OX=224308 GN=yqgT PE=3 SV=1
P59105	4.21e-09	7	65	41	99	Spore cortex-lytic enzyme OS=Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831) OX=221109 GN=sleB PE=3 SV=1
L7N653	6.00e-09	10	80	105	171	N-acetylmuramoyl-L-alanine amidase CwlM OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=cwlM PE=1 SV=1
O17754	2.16e-08	102	230	66	179	Carboxypeptidase E OS=Caenorhabditis elegans OX=6239 GN=egl-21 PE=1 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
0.999887	0.000128	0.000013	0.000000	0.000000	0.000007

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000948_01378.