CAZyme Information: MGYG000003372_03495

Basic Information

• Species: Citrobacter werkmanii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter werkmanii
• CAZyme ID: MGYG000003372_03495
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
107	MGYG000003372_68|CGC5	12445.47	6.3211

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003372	4983851	MAG	United States	North America

• Gene Location: Start: 119974; End: 120297 Strand: -

Full Sequence      

MPLRSTHFTPACVAFIKHWQGLSLEKYRDKHGIWVIGYGHEIAADETFDTPITLMQAEAL
LLADLHLCEALLYEKKPQIKDRFQQETLIAWIFSVGITRFNMTEIWP

Enzyme Prediction     

No EC number prediction in MGYG000003372_03495.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	11	101	9.2e-17	0.6715328467153284

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	4.11e-20	12	100	1	89	endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
COG3772	RrrD	3.38e-15	10	100	9	100	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900	endolysin_R21-like	6.24e-07	13	100	9	95	endolysin R21-like proteins. Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
cd00735	T4-like_lys	0.001	20	65	10	57	bacteriophage T4-like lysozymes. Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYL68120.1	3.86e-76	1	107	1	107
QET68457.1	3.86e-76	1	107	1	107
BBV28722.1	9.12e-75	1	107	1	107
BBV33736.1	9.12e-75	1	107	1	107
AWS94741.1	9.12e-75	1	107	1	107

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4EVX_A	7.23e-32	5	100	4	98	Crystalstructure of putative phage endolysin from S. enterica [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],4EVX_B Crystal structure of putative phage endolysin from S. enterica [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
6H9D_A	2.17e-06	4	105	1	101	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000045	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003372_03495.