CAZyme Information: MGYG000004526_01034

Basic Information

• Species: CAG-103 sp000432375
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-103; CAG-103 sp000432375
• CAZyme ID: MGYG000004526_01034
• CAZy Family: CBM50
• CAZyme Description: Gamma-D-glutamyl-L-diamino acid endopeptidase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
426	MGYG000004526_17|CGC1	45640.98	5.696

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004526	1961384	MAG	Israel	Asia

• Gene Location: Start: 13166; End: 14446 Strand: +

Full Sequence      

MTQTLKQGDRGALVSLLQLGLQRAGQTPGALDGIFGAQTAAAVRAFQAANALTPDGIAGA
RTHRALLPYYTGFVTRTIRAGDTFSALARQYGTSVDAIALANPYLDPERLPLGRALTIPL
PFSVTPADIPYSSALIGYVVRGLAARYPMLAVGEFGRSVLGRPLWYLTLGSGPKLVFYNA
AHHANEWITTPLLLTFCEQLCARLGDGGDMEGQNIRDLLSRVTLVLAPAVDPDGIDLVTG
ALDAETTAAAKALAENYPDIPFPSGWKANIRGIDLNLQYPAGWSTAREIKFAAGYTRPGP
RDYVGPAPLVAPESLAMYGFTRALDPLLTLSYHTQGRVIYWQYDGYDVPGSEAIARQFAA
VSGYDVAATPYAAGHAGYKDWFIQDYRRPGFTIEAGSGENPLPLSQFPDIWSDNLGILLV
GMTAVL

Enzyme Prediction     

No EC number prediction in MGYG000004526_01034.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06229	M14_Endopeptidase_I	3.03e-99	176	418	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	1.18e-37	141	407	12	273	Zn_pept domain.
cd00596	Peptidase_M14_like	2.12e-33	176	418	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	2.69e-32	141	415	6	285	Zinc carboxypeptidase.
cd03859	M14_CPT	5.70e-27	143	415	17	289	Peptidase M14 Carboxypeptidase T subfamily. Peptidase M14-like domain of carboxypeptidase (CP) T (CPT), CPT belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding 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. CPT has moderate similarity to CPA and CPB, and exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues like CPA and C-terminal positively charged residues like CPB. CPA and CPB are M14 family peptidases but do not belong to this CPT group. The substrate specificity difference between CPT and CPA and CPB is ascribed to a few amino acid substitutions at the substrate-binding pocket while the spatial organization of the binding site remains the same as in all Zn-CPs. CPT has increased thermal stability in presence of Ca2+ ions, and two disulfide bridges which give an additional stabilization factor.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWT55181.1	6.59e-166	5	423	4	424
VCV21589.1	5.46e-138	3	423	2	437
AGC68495.1	1.83e-129	3	421	2	420
ANW98855.1	1.83e-129	3	421	2	420
AGI39513.1	1.83e-129	3	421	2	420

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5K2L_A	4.06e-07	75	119	4	48	Crystalstructure of LysM domain from Volvox carteri chitinase [Volvox carteri f. nagariensis],5YZK_A Solution structure of LysM domain from a chitinase derived from Volvox carteri [Volvox carteri f. nagariensis]
5YZ6_A	1.42e-06	75	119	4	48	Solutionstructure of LysM domain from a chitinase derived from Volvox carteri [Volvox carteri f. nagariensis]
4B6Z_A	2.31e-06	142	234	145	240	Crystalstructure of metallo-carboxypeptidase from Burkholderia cenocepacia [Burkholderia cenocepacia],4B6Z_B Crystal structure of metallo-carboxypeptidase from Burkholderia cenocepacia [Burkholderia cenocepacia],4B6Z_C Crystal structure of metallo-carboxypeptidase from Burkholderia cenocepacia [Burkholderia cenocepacia],4B6Z_D Crystal structure of metallo-carboxypeptidase from Burkholderia cenocepacia [Burkholderia cenocepacia]
5NM7_A	4.35e-06	1	66	1	65	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	1.21e-78	131	422	110	394	Gamma-D-glutamyl-L-diamino acid endopeptidase 1 OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P54497	1.61e-57	131	418	84	368	Uncharacterized protein YqgT OS=Bacillus subtilis (strain 168) OX=224308 GN=yqgT 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
1.000019	0.000029	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004526_01034.