dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003137_02743

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Basic Information help

Species

Bradyrhizobium sp000015165

Lineage

Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Xanthobacteraceae; Bradyrhizobium; Bradyrhizobium sp000015165

CAZyme ID

MGYG000003137_02743

CAZy Family

GH108

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
558		59519.85	7.365

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003137	8388709	MAG	United States	North America

Gene Location

Start: 61658; End: 63334 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003137_02743.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH108	211	294	5.6e-26	0.9534883720930233

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3926	ZliS	2.43e-40	201	394	1	195	Lysozyme family protein [General function prediction only].
cd14845	L-Ala-D-Glu_peptidase_like	1.17e-33	10	125	4	125	L-Ala-D-Glu peptidase, also known as L-alanyl-D-glutamate endopeptidase. This L-Ala-D-Glu peptidase family includes L-alanyl-D-glutamate peptidase (bacteriophage T5) (also known as L-alanoyl-D-glutamate endopeptidase), and Ply118 and Ply500 L-Ala-D-Glu peptidase. Bacteriophage endolysin degrades the peptidoglycan of the bacterial host from within, leading to cell lysis and release of progeny virions. The bacteriophage endolysin Ply118 cleaves between L-Ala and D-Glu residues of Listeria cell wall peptidoglycan. This family belongs to the MEROPS peptidase M15 subfamily C.
cd13926	N-acetylmuramidase_GH108	2.06e-31	204	294	2	91	N-acetylmuramidase domain of the glycosyl hydrolase 108 family. This domain acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It contains a conserved EGGY motif near the N-terminus, the glutamic acid within this motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion. It is frequently found at the N-terminus of proteins containing a peptidoglycan binding domain.
pfam05838	Glyco_hydro_108	9.77e-31	210	294	2	86	Glycosyl hydrolase 108. This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It contains a conserved EGGY motif near the N-terminus, the glutamic acid within this motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion. It is frequently found at the N-terminus of proteins containing a C-terminal pfam09374 domain.
cd14814	Peptidase_M15	3.09e-07	32	91	17	80	Metalloproteases including zinc D-Ala-D-Ala carboxypeptidase, L-Ala-D-Glu peptidase, L,D-carboxypeptidase, bacteriophage endolysins, and related proteins. This family summarizes zinc-binding metallopeptidases which are mostly carboxypeptidases and dipeptidases, and includes zinc-dependent D-Ala-D-Ala carboxypeptidases, VanX, L-Ala-D-Glu peptidase, L,D-carboxypeptidase and bacteriophage endolysins, amongst other family members. These peptidases belong to MEROPS family M15 which are involved in bacterial cell wall biosynthesis and metabolism.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABQ35943.1	0.0	1	558	18	575
AVO38661.1	8.36e-125	1	544	25	592
APX14134.1	2.32e-112	1	544	1	551
AEB10705.1	2.62e-55	11	186	9	185
AGW13013.1	1.36e-46	10	176	13	179

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7DNP_A	1.05e-27	201	377	2	172	ChainA, Secretion activator protein, hypothetical [Brucella abortus bv. 1 str. 9-941]
2IS5_A	9.80e-18	216	364	17	155	Crystalstructure of 3 residues truncated version of protein NMB1012 from Neisseria meningitides [Neisseria meningitidis serogroup B],2IS5_B Crystal structure of 3 residues truncated version of protein NMB1012 from Neisseria meningitides [Neisseria meningitidis serogroup B],2IS5_C Crystal structure of 3 residues truncated version of protein NMB1012 from Neisseria meningitides [Neisseria meningitidis serogroup B],2IS5_D Crystal structure of 3 residues truncated version of protein NMB1012 from Neisseria meningitides [Neisseria meningitidis serogroup B]
2IKB_A	1.00e-17	216	364	16	154	CrystalStructure of a Protein of Unknown Function NMB1012 from Neisseria meningitidis [Neisseria meningitidis MC58],2IKB_B Crystal Structure of a Protein of Unknown Function NMB1012 from Neisseria meningitidis [Neisseria meningitidis MC58],2IKB_C Crystal Structure of a Protein of Unknown Function NMB1012 from Neisseria meningitidis [Neisseria meningitidis MC58],2IKB_D Crystal Structure of a Protein of Unknown Function NMB1012 from Neisseria meningitidis [Neisseria meningitidis MC58]
2NR7_A	3.03e-16	199	369	1	194	StructuralGenomics, the crystal structure of putative secretion activator protein from Porphyromonas gingivalis W83 [Porphyromonas gingivalis W83]
6AKV_A	3.75e-09	7	149	34	174	ChainA, LysB4 [Bacillus phage B4]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34360	7.74e-13	14	125	43	164	Peptidoglycan L-alanyl-D-glutamate endopeptidase CwlK OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlK PE=1 SV=1
Q37979	1.25e-07	7	132	14	143	L-alanyl-D-glutamate peptidase OS=Listeria phage A500 OX=40522 GN=ply 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
1.000039	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003137_02743.