CAZyme Information: MGYG000001542_02698

Basic Information

• Species: Paenibacillus_A sp900069005
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A sp900069005
• CAZyme ID: MGYG000001542_02698
• CAZy Family: CBM50
• CAZyme Description: Gamma-D-glutamyl-L-diamino acid endopeptidase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
306		34533.98	4.4826

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001542	5846629	Isolate	not provided	not provided

• Gene Location: Start: 63838; End: 64758 Strand: +

Full Sequence      

MDLWSFADRIEPAIVEVCGGYRYADFQAQSMELMRKYPQLCRRSIGRSVLGRSIDCFIIG
NGSEHLHMNGAVHANEWITTPLLLRFMEELLEHAGSQRSEAIACLLERATLWIVPMVNPD
GVDLAQDGAAMADDSWRSCLLAWNEGSDDFTAWKANIRGVDLNDQFPACWEIERERRQVC
GPASQDYSGPCPLSEPEAQALAELTETVEFSRVLSLHTQGREIYWNYRNQEPPEAEVLAE
KLAAVSGYRAVKLSGSDAGYKDWFIMQFRRPGYTVEAGEGKNPLPPEQFDSIYKDLAPLL
FEFIRG

Enzyme Prediction     

No EC number prediction in MGYG000001542_02698.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06229	M14_Endopeptidase_I	4.03e-105	66	300	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	8.26e-54	21	293	2	277	Zn_pept domain.
cd00596	Peptidase_M14_like	5.96e-41	66	300	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.
cd03859	M14_CPT	8.46e-41	19	295	2	287	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.
pfam00246	Peptidase_M14	2.03e-37	32	295	7	283	Zinc carboxypeptidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHT64030.1	1.14e-104	14	300	104	392
BBH19109.1	8.33e-104	14	305	105	398
APQ58836.1	5.21e-103	11	300	102	400
APB71683.1	7.38e-103	11	300	102	400
QYK66652.1	7.38e-103	11	300	102	400

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2PCU_A	1.33e-10	37	257	25	234	Humancarboxypeptidase A4 in complex with a cleaved hexapeptide. [Homo sapiens]
2BO9_A	1.35e-10	37	257	27	236	Humancarboxypeptidase A4 in complex with human latexin. [Homo sapiens],2BO9_C Human carboxypeptidase A4 in complex with human latexin. [Homo sapiens]
4A94_A	1.37e-10	37	257	29	238	Structureof the carboxypeptidase inhibitor from Nerita versicolor in complex with human CPA4 [Homo sapiens],4A94_B Structure of the carboxypeptidase inhibitor from Nerita versicolor in complex with human CPA4 [Homo sapiens],4BD9_A Structure of the complex between SmCI and human carboxypeptidase A4 [Homo sapiens]
2BOA_A	1.95e-10	37	257	123	332	Humanprocarboxypeptidase A4. [Homo sapiens],2BOA_B Human procarboxypeptidase A4. [Homo sapiens]
2NSM_A	6.98e-08	21	227	7	205	Crystalstructure of the human carboxypeptidase N (Kininase I) catalytic domain [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q03415	2.64e-88	9	295	98	385	Gamma-D-glutamyl-L-diamino acid endopeptidase 1 OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P54497	1.19e-63	37	301	100	369	Uncharacterized protein YqgT OS=Bacillus subtilis (strain 168) OX=224308 GN=yqgT PE=3 SV=1
B8NBP9	2.33e-11	19	240	191	418	Inactive metallocarboxypeptidase ecm14 OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=ecm14 PE=3 SV=1
Q2TZK2	2.33e-11	19	240	191	418	Inactive metallocarboxypeptidase ecm14 OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=ecm14 PE=3 SV=1
P18143	4.68e-11	21	288	133	416	Zinc carboxypeptidase OS=Streptomyces griseus OX=1911 GN=scpD PE=1 SV=2

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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001542_02698.