CAZyme Information: MGYG000004667_01142

Basic Information

• Species: Clostridium beijerinckii
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium beijerinckii
• CAZyme ID: MGYG000004667_01142
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
348	MGYG000004667_39|CGC1	39876.25	4.3688

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004667	6180974	Isolate	United States	North America

• Gene Location: Start: 28256; End: 29302 Strand: +

Full Sequence      

MANYILGIDVSNNNGSIDFSGMGPNDGVKIVYLKATEGQSFKDSTMSPFYLECKANGLKV
GAYHFLVGTSSPEAQAQNFYSMIKDYEWDCLPMLDVETNFDGLANYVTRFINTFKQLSPL
KLGIYSYTSFLPYLRTICSEIKDIPFWEANYNNDPWNLSDTFFANRIGHQYTEKGIITGI
TSEGCDLDSFTDGVYLNSDTIPGEWKLESNGKWWYKHEDGSYTKNGWEHINGEWYLFDSE
GYMCYSWKKDGNNWYFLGGSNDGTMKYGWVLTDNKWYYFGDKNDGAMKTGWQQIDGKWYY
FNTDGAMQTGWIADNSKLYCCYSSGEMICNCDLYGYHFNENGEAAKLS

Enzyme Prediction     

No EC number prediction in MGYG000004667_01142.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	8	180	2.8e-38	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	3.65e-71	7	190	2	184	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.
cd00599	GH25_muramidase	1.83e-38	7	190	2	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.
NF033840	PspC_relate_1	7.96e-36	205	343	512	645	PspC-related protein choline-binding protein 1. Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.
NF033838	PspC_subgroup_1	2.90e-31	205	345	488	625	pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
NF033930	pneumo_PspA	7.23e-31	205	345	445	582	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AQS14730.1	6.47e-138	4	348	3	344
AQR90843.1	6.47e-138	4	348	3	344
AQS10409.1	6.47e-138	4	348	3	344
AGX43545.1	6.47e-138	4	348	3	344
AQS00747.1	6.47e-138	4	348	3	344

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	8.09e-30	5	198	20	215	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.01e-28	5	198	20	215	X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
2WAG_A	3.66e-10	5	97	16	107	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
6ZM8_A	3.53e-09	5	151	2	162	ChainA, muramidase [Sodiomyces alcalophilus]
4IWT_A	1.76e-07	205	249	6	50	Crystalstructure of the C-teminal choline-binding domain of the Streptococcus pneumoniae prophage LytA [Streptococcus pneumoniae GA60080],4IWT_B Crystal structure of the C-teminal choline-binding domain of the Streptococcus pneumoniae prophage LytA [Streptococcus pneumoniae GA60080]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	1.27e-29	7	204	3	196	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
P26836	1.14e-25	2	194	6	200	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P76421	1.22e-07	5	194	67	268	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.64e-07	5	194	67	268	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	2.95e-07	5	194	67	268	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2

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
1.000029	0.000008	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004667_01142.