CAZyme Information: MGYG000000262_01726

Basic Information

• Species: Anaerobutyricum hallii
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerobutyricum; Anaerobutyricum hallii
• CAZyme ID: MGYG000000262_01726
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
316	MGYG000000262_9|CGC2	36271.76	10.1715

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000262	3404550	Isolate	China	Asia

• Gene Location: Start: 92931; End: 93881 Strand: -

Full Sequence      

MKKIVDVSSYNGTVSWAKVKKYGCSGAILKIIRKDLERDKGFNRNYQACNENHINWGVYN
YTYATTPKKARADMNLVCDILDKIDKSYFKYGVWFDLEDKVQAKLTKSQIADIVNAAQEI
VEKRGYVFGVYTGKAYFEEHIDRKKVLCQNWWIARYYRGDARMQIAVNPNEKYKPTTANI
AWQYTSKGRFPKIVSTGNSGNFDFNIMYREPFEKEGVKKEEKTEEKPKKVYTGSLPALKS
KAYFARPDGIKTSKKRKDIKKIQNFLNWAIDAGLTVDGKYGAKTETAVAVFQELCGIRID
GKFGSITLTKAKTFKK

Enzyme Prediction     

No EC number prediction in MGYG000000262_01726.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	5	191	6.3e-33	0.9830508474576272

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	8.55e-39	2	208	1	191	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599	GH25_muramidase	2.23e-21	3	207	1	186	Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
pfam01183	Glyco_hydro_25	1.70e-18	5	193	1	180	Glycosyl hydrolases family 25.
cd06522	GH25_AtlA-like	2.21e-14	2	208	1	192	AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
cd06525	GH25_Lyc-like	3.01e-14	3	205	1	182	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SOB72812.1	1.54e-125	3	316	2	313
ACR75068.1	5.64e-36	3	210	2	201
QDW73665.1	6.41e-24	5	209	1026	1223
QPS13527.1	1.13e-21	2	208	1465	1660
QMW73215.1	1.13e-21	2	208	1465	1660

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.04e-09	2	208	269	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	2.48e-09	2	208	269	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
5A6S_A	3.75e-08	1	207	21	201	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000262_01726.