dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

HGM13634 sp900770385

Lineage

Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; HGM13634; HGM13634 sp900770385

CAZyme ID

MGYG000000482_00326

CAZy Family

CBM50

CAZyme Description

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

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
424		47669.64	9.0588

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000482	1135888	MAG	Fiji	Oceania

Gene Location

Start: 347461; End: 348735 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000000482_00326.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06229	M14_Endopeptidase_I	7.40e-97	174	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	9.64e-42	129	411	2	277	Zn_pept domain.
cd00596	Peptidase_M14_like	1.60e-30	174	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.
cd03859	M14_CPT	2.87e-27	129	414	5	288	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	2.71e-24	138	414	5	284	Zinc carboxypeptidase.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWT55181.1	3.85e-152	1	421	1	422
CDZ24839.1	1.02e-143	1	423	1	422
AUS95891.1	9.84e-142	1	423	1	422
AGC68495.1	4.40e-140	1	424	1	423
ANW98855.1	4.40e-140	1	424	1	423

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6TCI_A	8.35e-08	2	66	5	69	Thecrystal structure of SleB N-terminal domain [Bacillus cereus ATCC 14579]
3BKH_A	4.26e-07	2	122	10	122	ChainA, lytic transglycosylase [Pseudomonas phage phiKZ],3BKV_A Chain A, lytic transglycosylase [Pseudomonas phage phiKZ]
4LPQ_A	5.82e-07	7	65	14	72	Crystalstructure of the L,D-transpeptidase (residues 123-326) from Xylanimonas cellulosilytica DSM 15894 [Xylanimonas cellulosilytica DSM 15894]
4FET_A	1.25e-06	2	66	5	69	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]
5TV7_A	3.27e-06	2	65	107	169	ChainA, Putative peptidoglycan-binding/hydrolysing protein [Clostridioides difficile 630],5TV7_B Chain B, Putative peptidoglycan-binding/hydrolysing protein [Clostridioides difficile 630]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q03415	4.83e-87	128	424	109	396	Gamma-D-glutamyl-L-diamino acid endopeptidase 1 OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P54497	2.23e-61	129	418	84	368	Uncharacterized protein YqgT OS=Bacillus subtilis (strain 168) OX=224308 GN=yqgT PE=3 SV=1
O17754	3.43e-06	153	280	66	179	Carboxypeptidase E OS=Caenorhabditis elegans OX=6239 GN=egl-21 PE=1 SV=1
P0A3V0	7.03e-06	2	82	36	115	Spore cortex-lytic enzyme OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=sleB PE=1 SV=1
P0A3V1	7.03e-06	2	82	36	115	Spore cortex-lytic enzyme OS=Bacillus cereus OX=1396 GN=sleB 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
1.000084	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000482_00326.

You are here: Home > Sequence: MGYG000000482_00326