CAZyme Information: MGYG000001607_01254

Basic Information

• Species: Dorea_B phocaeensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Dorea_B; Dorea_B phocaeensis
• CAZyme ID: MGYG000001607_01254
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1173		130478.25	4.685

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001607	2347571	MAG	China	Asia

• Gene Location: Start: 1351; End: 4872 Strand: -

Full Sequence      

MQKFKRKAVSIALSLAMLFSILPASGAFAADENQVQESAPQTEAASGEQLEVQSETEGGE
VQTQEMSVPQLQYLYIDTPYLMTPDTQKIMVSFQDEIELESVSMVYENVETAEQYEVLAG
EIQDATAVFSIDYLENSTAGSYHLLKVRTVSGGITNEIDLGEAGIDSRFGVNQECDTQPD
AIVEEESTSSSARTVNEPGNPVNFLTYDEEGELVESESVEEAVEEAKTDVPAMASRAAET
SEKAGNLIVVIDPGHGGYDPGAVGVNGAKEKDLTLKIAKYCKEELEKYSGVTVYMTRTTD
TGLSPSNNLSDDLKKRVEYAKGKKADVLVSMHLNSTGLGTAHGAEVYYPNANYNPGVGSE
GKNLASKIQKELVGLGLTDRGIKIRNSGTNTLYPDGSLQDYYALIWQSKRAGFPAIIVEH
AFIDNTSDYNKYLSSDEKLKALGIADAKGIAEAYGFAKGQWIQNDKGWWYQYADGSYAKN
TWAAINGAWYHFDSDGYMQTGWFTEGTAKYYLDPVSGAMKTGWQLINNKWYYFNGSGIMV
TGWQWIGNTCYYFDGTGVMATDTWIGNDYVNSNGAWVPGMVKPGWVQDGRGWWYRHSDGS
YTKSNWEKIEGQWYYFDAAGYMTTGWQNVGGSWYYMDGSGKMLTGWQTIGGSKYYLNGSG
VMLTGWQWINSKCYYFTASGAMASNTWIGNDYVDASGAWVPGKVKEEAKWILDEHGWWYR
HSDGSYTKSNWEVIGGQWYYFNAAGYMLTGWQWIGGKCYYFASSGAMASNTWIGNDYVDA
SGAWVPGKVKEEAKWILDGRGWWYRHSDGSYTKSNWEVIGGQWYYFDAAGYMVTGWQWIG
GKCYYFASSGAMASNTWIGNDYVDASGAWVPGKVKEEAKWILDGRGWWYRHKDGSYTRSN
WEVIGGQWYYFDADGYMVTGWIALGGTHYYLNTSGAMHKGWLKDNGTWYYLNPTANNFGA
EGAMTRGYRQIDGVWYYFNKEISPEGAMTYEGVTPIMGATALGNKTTAVNKMVKMYMNSK
RTYPSGALSKGGASNITQFCEILYEEAIVENVKPEVVFGQAMKETGYLQFGGDVKVEQFN
FAGLGATGGVPGESFKDVRTGIRAQVQHLKAYASKDSPKNEIVDTRFAYVTRNCAPYVEW
LGIKENPDGKGWATARKYGMSLMESYIKPIYGM

Enzyme Prediction     

No EC number prediction in MGYG000001607_01254.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	1041	1164	8.1e-16	0.921875

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	1.19e-59	248	451	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	5.60e-53	249	450	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.
NF033930	pneumo_PspA	6.11e-50	458	700	442	660	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
NF033930	pneumo_PspA	2.54e-46	518	785	440	660	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
COG0860	AmiC	1.52e-44	234	455	30	229	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM00238.1	2.95e-85	70	458	42	416
QEI32622.1	1.01e-80	7	1163	2	1303
QHB25110.1	1.01e-80	7	1163	2	1303
QRT31212.1	1.36e-80	7	1163	2	1303
CBL07763.1	1.66e-78	70	459	163	540

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J72_A	3.10e-19	239	452	444	635	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]
1JWQ_A	1.49e-16	248	452	3	174	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A	2.14e-15	249	434	6	163	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5EMI_A	2.42e-15	244	450	2	174	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
3NE8_A	3.82e-13	249	347	7	97	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
P54525	3.34e-18	238	454	21	204	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
Q06320	3.85e-18	249	458	4	179	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
O51481	1.47e-17	1045	1168	77	194	Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1
Q9RMZ0	4.40e-17	249	454	335	520	Uncharacterized cell wall amidase pXO2-42/BXB0045/GBAA_pXO2_0045 OS=Bacillus anthracis OX=1392 GN=pXO2-42 PE=3 SV=2
O48471	1.18e-15	248	458	4	185	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1

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
0.000343	0.998811	0.000250	0.000212	0.000194	0.000164

TMHMM  Annotations     

start	end
7	29