CAZyme Information: MGYG000001374_01580

Basic Information

• Species: Mediterraneibacter torques
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter torques
• CAZyme ID: MGYG000001374_01580
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
508		55234.27	8.6989

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001374	3092406	Isolate	not provided	not provided

• Gene Location: Start: 697510; End: 699036 Strand: -

Full Sequence      

MAAPKIEKLLTPYNFTNKDNAGRIKYIVIHYVGALGGAEANCKYYASKYLGASAHYFVGF
NGEVWQSVEDEDIAWHCGASSYKHAECRNSNSIGIEMCVRNKGSQSAESKDWYFEEATVN
AAIELTKYLMQKYGVPASNVIRHHDVTGKICPNPYVYNSTKHTWDAFKKAISGGTEQKDS
MTKITGKSEATAEQMTAYIKAKNGSVAQSVLDMIPLYLSEGEAENIRGDIAFAQSCLETG
NFTFSGSAVELSQNNFCGMGVTQNGETGNSFKTPQLGIRAQIQHLKAYANTTKLKQECVD
PRFDLVSRGCAPYVEYLGIQENPKSKGWAAGAGYGEKILKILDAIKETGSSQAGDGSPKP
DETKKDDDFKEYLITTTCDVLNIRSGAGTDNKVVGAIREVAGKKNKYTIVEEKNGWGRLK
SGAGWISLSYTKKVAASTGTTFTPYLITTTCDVLNIRSGAGTGYSVVGAIREVAGKKNKY
TIVEEKNGWGRLKSGAGWISLSYTKKAS

Enzyme Prediction     

No EC number prediction in MGYG000001374_01580.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	213	345	1.5e-17	0.9765625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01510	Amidase_2	1.08e-35	23	154	1	121	N-acetylmuramoyl-L-alanine amidase. This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.
cd06583	PGRP	2.43e-27	23	155	1	126	Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.
smart00644	Ami_2	2.15e-26	22	152	1	126	Ami_2 domain.
COG3023	AmpD	9.87e-24	10	155	32	167	N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis].
COG5632	CwlA	7.66e-18	17	180	17	174	N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW80001.1	1.95e-109	5	506	2	500
QIB57222.1	1.95e-109	5	506	2	500
AFC63685.1	1.81e-106	6	508	4	499
ADL53623.1	4.47e-101	47	506	47	487
QHJ84983.1	5.19e-91	5	182	2	179

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BH7_A	4.86e-13	23	146	28	154	Crystalstructure of a SeMet derivative of AmiD at 2.2 angstroms [Escherichia coli K-12]
2WKX_A	4.86e-13	23	146	28	154	Crystalstructure of the native E. coli zinc amidase AmiD [Escherichia coli K-12],3D2Y_A Complex of the N-acetylmuramyl-L-alanine amidase AmiD from E.coli with the substrate anhydro-N-acetylmuramic acid-L-Ala-D-gamma-Glu-L-Lys [Escherichia coli str. K-12 substr. MG1655],3D2Z_A Complex of the N-acetylmuramyl-L-alanine amidase AmiD from E.coli with the product L-Ala-D-gamma-Glu-L-Lys [Escherichia coli str. K-12 substr. MG1655]
1YB0_A	9.18e-09	7	174	5	157	Structureof PlyL [Bacillus anthracis],1YB0_B Structure of PlyL [Bacillus anthracis],1YB0_C Structure of PlyL [Bacillus anthracis]
2L47_A	1.40e-08	7	182	5	165	Solutionstructure of the PlyG catalytic domain [Bacillus phage Gamma]
2AR3_A	5.88e-08	7	174	5	157	ChainA, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis],2AR3_B Chain B, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis],2AR3_C Chain C, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O51481	1.42e-20	217	347	75	197	Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1
P36550	6.18e-16	24	225	24	230	N-acetylmuramoyl-L-alanine amidase CwlL OS=Bacillus licheniformis OX=1402 GN=cwlL PE=3 SV=1
Q99125	3.67e-13	24	205	24	202	Probable N-acetylmuramoyl-L-alanine amidase OS=Bacillus licheniformis OX=1402 PE=3 SV=1
P75820	3.23e-12	23	146	43	169	N-acetylmuramoyl-L-alanine amidase AmiD OS=Escherichia coli (strain K12) OX=83333 GN=amiD PE=1 SV=1
O31982	9.73e-12	24	202	24	208	N-acetylmuramoyl-L-alanine amidase BlyA OS=Bacillus subtilis (strain 168) OX=224308 GN=blyA PE=3 SV=1

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
1.000094	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001374_01580.