dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003425_01644

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Basic Information help

Species

CAG-127 sp900766925

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-127; CAG-127 sp900766925

CAZyme ID

MGYG000003425_01644

CAZy Family

GH73

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1101	MGYG000003425_216\|CGC1	122552.81	6.3026

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003425	5056923	MAG	Fiji	Oceania

Gene Location

Start: 55507; End: 58812 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003425_01644.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH73	965	1090	2.6e-18	0.9296875

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	3.36e-51	223	423	1	172	N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.
pfam01520	Amidase_3	2.06e-46	224	422	1	172	N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
COG0860	AmiC	2.35e-44	215	429	36	231	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
TIGR02883	spore_cwlD	7.71e-30	223	425	2	189	N-acetylmuramoyl-L-alanine amidase CwlD. Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]
PRK10319	PRK10319	2.69e-21	220	313	55	148	N-acetylmuramoyl-L-alanine amidase AmiA.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYX25930.1	3.69e-187	61	1096	104	1137
QWT54385.1	2.58e-137	410	1096	1	608
QNM00238.1	1.45e-74	2	1101	5	624
VCV20908.1	2.17e-71	59	1090	168	1458
CBL07763.1	9.05e-71	57	1090	160	1452

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BIN_A	9.91e-15	217	313	169	266	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
1JWQ_A	4.75e-14	223	429	3	179	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5EMI_A	1.22e-13	219	319	2	103	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
3NE8_A	3.55e-13	222	313	5	97	Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5J72_A	9.97e-12	216	415	446	626	ChainA, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630],5J72_B Chain B, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [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
O51481	1.88e-21	951	1064	58	171	Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1
Q02114	1.05e-16	224	402	322	472	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
O48471	3.28e-16	223	430	4	185	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
P54525	1.04e-15	217	425	29	203	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
Q9K0V3	2.52e-14	215	316	182	284	N-acetylmuramoyl-L-alanine amidase AmiC OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=amiC PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000898	0.847597	0.150564	0.000333	0.000303	0.000270

TMHMM Annotations download full data without filtering help

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