CAZyme Information: MGYG000002836_03980

Basic Information

• Species: Anaerocolumna aminovalerica
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerocolumna; Anaerocolumna aminovalerica
• CAZyme ID: MGYG000002836_03980
• CAZy Family: CBM50
• CAZyme Description: Spore germination protein YaaH

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
296		32992.78	4.4589

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002836	4582914	MAG	United States	North America

• Gene Location: Start: 15148; End: 16038 Strand: -

Full Sequence      

MTIHVVQPGETITTIANQYDVTPERLITDNELPNPENLLVGQSIVVQHAEVIHTVVAGDT
LYGIAETYGVTPNQILQNNPRIGELGYLVPGETIVIKFAEVDERNKLGNIVIGGYAYPFI
DRAVLRKTLPFLTYLYLFAYGFTPTGELIPIDDEELIATARDYGVGPILVLAPMTPEGNF
SNELAHTMFTNPEVQNRLIDNLVATMKAKNYVGMDVDFEFVLPGDKDLFIQFIRNLKNRL
EPEGLLLTVALAPKVSAEQPGLLYEAHDYPAIGAIADKVLLMTYEWGYTYSHTRHR

Enzyme Prediction     

No EC number prediction in MGYG000002836_03980.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02874	GH18_CFLE_spore_hydrolase	1.70e-66	110	291	2	184	Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.
COG3858	YaaH	9.02e-62	1	289	1	286	Spore germination protein YaaH [Cell cycle control, cell division, chromosome partitioning].
cd00598	GH18_chitinase-like	3.31e-14	178	284	72	176	The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
cd02872	GH18_chitolectin_chitotriosidase	3.38e-13	130	292	25	200	This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
cd00118	LysM	8.20e-10	51	96	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHQ61716.1	2.83e-120	1	290	1	287
BCJ94528.1	1.22e-116	1	290	1	287
BCJ99370.1	7.16e-116	1	291	1	288
CUH92236.1	1.39e-112	1	290	1	285
BBF41719.1	1.26e-108	1	290	1	287

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4S3K_A	3.25e-38	3	289	6	291	ChainA, Spore germination protein YaaH [Priestia megaterium QM B1551]
4S3J_A	7.19e-29	3	288	5	288	Crystalstructure of the Bacillus cereus spore cortex-lytic enzyme SleL [Bacillus cereus ATCC 10876],4S3J_B Crystal structure of the Bacillus cereus spore cortex-lytic enzyme SleL [Bacillus cereus ATCC 10876],4S3J_C Crystal structure of the Bacillus cereus spore cortex-lytic enzyme SleL [Bacillus cereus ATCC 10876]
3CZ8_A	1.34e-27	107	286	3	185	ChainA, Putative sporulation-specific glycosylase ydhD [Bacillus subtilis subsp. subtilis str. 168],3CZ8_B Chain B, Putative sporulation-specific glycosylase ydhD [Bacillus subtilis subsp. subtilis str. 168]
4Q6T_A	4.23e-12	140	285	38	187	Thecrystal structure of a class V chitininase from Pseudomonas fluorescens Pf-5 [Pseudomonas protegens Pf-5]
5JH8_A	2.51e-09	178	285	74	179	Crystalstructure of chitinase from Chromobacterium violaceum ATCC 12472 [Chromobacterium violaceum ATCC 12472]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P37531	2.31e-33	1	289	1	287	Cortical fragment-lytic enzyme OS=Bacillus subtilis (strain 168) OX=224308 GN=sleL PE=1 SV=2
O05495	6.45e-28	1	286	1	277	Putative sporulation-specific glycosylase YdhD OS=Bacillus subtilis (strain 168) OX=224308 GN=ydhD PE=1 SV=2
P0DPJ9	1.38e-27	3	288	4	287	Cortical fragment-lytic enzyme OS=Bacillus anthracis OX=1392 GN=sleL PE=2 SV=1
Q9K3E4	1.90e-27	3	288	4	287	Cortical fragment-lytic enzyme OS=Bacillus cereus OX=1396 GN=sleL PE=1 SV=1
O32258	8.01e-10	95	287	15	212	Uncharacterized glycosylase YvbX OS=Bacillus subtilis (strain 168) OX=224308 GN=yvbX 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
1.000049	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002836_03980.