CAZyme Information: MGYG000000626_00793

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_J
• CAZyme ID: MGYG000000626_00793
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
845		92611.36	6.3157

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000626	2453643	MAG	Madagascar	Africa

• Gene Location: Start: 755; End: 3292 Strand: -

Full Sequence      

MKLHTKNHIPGQHHILRRTFAGLLAAATLVCTLPGGSTPVYAAQTQKQSLKTLGVIDTPG
EEDTANDLPDLADIPTAQAQLQTADNGDLIIAIDAGHGGSDAGATYDGMKEKDVNLKIAQ
YIKAYFADYAGVQIYLTRDSDTAVELSTRVEQAAAAGADVFISIHNNASSNEKTSGSMVF
YPNNNYRPALGAEGAELSQSILDQLTALGLPDLGIRTRNSENNTKYKDGSLADYYSVIRN
AKLQNITGIIVEHAFVSCASDRKNYLGTDAQLQKLAQADVKGIADYYGLEYVGLTKPAVT
LSAPGYKQLAVEWDEQEDARGYLVYRSEKKASGYKKIATVTGSYNTSYVDTGLALNKDYY
YKVKAYRKIDGVAYYSDESRILKGNVIGGTQFTEIKQTGDNFKLSWKAMSDADGYVISRS
EDGGSYVRIAEIDDPSRTTYTDRDVFSEITYRYRIRPLHYLYNNEGYGKMSTVVTLSYLD
PPEIKNTMARTDGKVKVTWSKVSGASQYVLQRSDSENGTYKTVATLKGEATTSYIDTKVE
IAKEYYYRVKAYNEHGIVKGSSYYSDALDAFNFRTPEFTNVAISNKTPGVSLTWSKTPFA
EGYRIYRSETEDGGYTRIGTVKGSSTVTYLDTSGTDIGTTYYYKVRAYVTKSKKTVLSYV
SDPRAITPGYAIMGESSTTAAKMANWYTARGGVYPEEIYSEYGAPTLKDFCKLVYNEAKA
EGVKAEVLFAQICKETGFLKFGGDVQPDQCNFGGIGATGGGAAGASFPDVQTGIRAQVQH
LKAYASDQPLNKECVDPRFTYVDRCAAIYVEWLGVHENPTGAGWATGKNYGYSLRDDYIS
SLLGY

Enzyme Prediction     

No EC number prediction in MGYG000000626_00793.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	712	835	1.9e-17	0.9140625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	8.32e-50	90	284	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	9.18e-43	91	283	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	2.59e-40	74	289	28	230	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
PRK10319	PRK10319	2.37e-18	85	287	53	276	N-acetylmuramoyl-L-alanine amidase AmiA.
PRK10431	PRK10431	4.67e-16	75	287	180	416	N-acetylmuramoyl-l-alanine amidase II; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL07763.1	3.15e-119	60	834	297	1450
CBL13779.1	8.00e-118	60	834	298	1451
VCV20908.1	3.07e-117	60	834	303	1456
QYX25930.1	4.46e-71	56	845	228	1140
QNM00238.1	2.61e-60	55	839	176	616

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EMI_A	3.08e-13	86	286	2	177	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
4BIN_A	8.87e-13	74	287	156	393	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
1JWQ_A	1.03e-12	90	286	3	175	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5J72_A	1.08e-10	91	261	454	612	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]
3NE8_A	6.90e-09	86	208	2	124	Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O51481	4.02e-18	694	835	55	189	Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1
O48471	9.59e-17	90	290	4	184	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
Q02114	1.19e-15	91	287	322	495	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
Q06320	7.37e-14	91	290	4	178	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
P54525	1.85e-13	91	287	32	204	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.002850	0.980194	0.012675	0.003645	0.000401	0.000215

TMHMM  Annotations     

start	end
20	42