CAZyme Information: MGYG000001548_00143

Basic Information

• Species: Paenibacillus_A tuaregi
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A tuaregi
• CAZyme ID: MGYG000001548_00143
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
418	MGYG000001548_4|CGC1	44653.23	9.8977

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001548	5663842	Isolate	not provided	not provided

• Gene Location: Start: 75722; End: 76978 Strand: -

Full Sequence      

MNTFKKTKAVLCLALALTSFGAIGSGAAHAAGKVSILLDGYPLPFPAQPTVVKGTTLVPF
RAISEALGVAVIWDSKTKTITATRNSSGASKKVILTLGSKNATVNGQKVAVALAPQTING
TTMIPLSFFSQQFGAGVKWDGSTSTVSIVSPREKLYTLAFYAQGAFSEASLIPDFNAVGF
GWSRIDDQSNFTTTGKDFWWPKPAGDTTPEKLVTDAAAAGTSPYLLVYSGDAKGELTKLV
EDKTTRKQALTQMVDTAIQKQFKGILLDLEGLGLTGNPQTVQASYNNLVKEAADAAHAAG
LKLSLALPPLNGSYHGYDYKRLGELADELIIMAYAYTNEKLPQPADRVDKAVQLALKEAP
KDKLVLGVNLYSENENTVNTKVGLAKRYGLKGVAFWRLGLGKQAVWDKLNQTITLKNN

Enzyme Prediction     

No EC number prediction in MGYG000001548_00143.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	179	372	3.4e-19	0.5743243243243243

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam07833	Cu_amine_oxidN1	2.04e-33	52	148	1	93	Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
cd02874	GH18_CFLE_spore_hydrolase	8.52e-29	206	409	44	313	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	1.05e-20	207	410	147	419	Spore germination protein YaaH [Cell cycle control, cell division, chromosome partitioning].
cd00598	GH18_chitinase-like	4.95e-11	230	399	73	208	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.
pfam07833	Cu_amine_oxidN1	5.91e-09	32	81	43	92	Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIQ17369.1	6.91e-175	7	415	5	414
QWU17984.1	6.74e-173	8	415	6	413
AIQ68170.1	9.24e-173	8	415	6	414
QSF46743.1	9.24e-173	7	415	5	414
CQR54861.1	2.64e-172	8	413	6	412

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4S3J_A	3.39e-08	207	416	153	430	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]
4S3K_A	7.64e-07	239	371	190	327	ChainA, Spore germination protein YaaH [Priestia megaterium QM B1551]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P37531	2.02e-13	239	371	186	323	Cortical fragment-lytic enzyme OS=Bacillus subtilis (strain 168) OX=224308 GN=sleL PE=1 SV=2
P0DPJ9	5.94e-08	207	416	152	429	Cortical fragment-lytic enzyme OS=Bacillus anthracis OX=1392 GN=sleL PE=2 SV=1
O32258	6.05e-08	210	411	83	341	Uncharacterized glycosylase YvbX OS=Bacillus subtilis (strain 168) OX=224308 GN=yvbX PE=3 SV=1
Q9K3E4	4.32e-07	207	416	152	429	Cortical fragment-lytic enzyme OS=Bacillus cereus OX=1396 GN=sleL PE=1 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
0.000299	0.998934	0.000197	0.000211	0.000181	0.000151

TMHMM  Annotations     

start	end
9	31