CAZyme Information: MGYG000001525_04857

Basic Information

• Species: Paenibacillus_A rubinfantis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A rubinfantis
• CAZyme ID: MGYG000001525_04857
• CAZy Family: CBM12
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
250	MGYG000001525_20|CGC31	26594.73	8.004

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001525	5369528	Isolate	not provided	not provided

• Gene Location: Start: 1456377; End: 1457129 Strand: -

Full Sequence      

MTSRKVSMKATSLLVVLAVILSTFLAVIPASAAARGAWAPNTAYAVNDTVTYNGSTYTCI
QAHTSLVGWEPPIVPALWSSSGGGGTNPNPNPNPNPNPSPVTKPGEVPSHIWTYVMNADN
AYGKGGDFALLLSAVIKKESSFGAGLPGSPSAGDGLMQVEPNTRNAYLSQFSAKFGHAYN
HGSEQDQVYMGALILNEKINRFGSIYNGLLHYNGGDYWYPGATDSYGRPILADQYANQVY
AQYKSYGGRS

Enzyme Prediction     

EC	3.2.1.14

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd12214	ChiA1_BD	7.11e-17	40	79	4	43	chitin-binding domain of Chi A1-like proteins. This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)).
cd13400	LT_IagB-like	1.02e-07	130	245	6	109	Escherichia coli invasion protein IagB and similar proteins. Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.
pfam01464	SLT	5.17e-04	131	215	14	95	Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.
cd00254	LT-like	6.12e-04	131	228	3	90	lytic transglycosylase(LT)-like domain. Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
smart00495	ChtBD3	0.002	40	78	6	41	Chitin-binding domain type 3.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAH10650.1	7.43e-144	1	249	1	251
AUO08603.1	1.04e-138	1	250	1	250
AJE53774.1	4.24e-138	1	250	1	250
QOH62288.1	4.24e-138	1	250	1	250
QNR69760.1	4.24e-138	1	250	1	250

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W6B_A	6.16e-98	101	249	32	180	Crystalstructure of catalytic domain of chitinase from Ralstonia sp. A-471 [Ralstonia sp. A-471],3W6B_B Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 [Ralstonia sp. A-471],3W6B_C Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 [Ralstonia sp. A-471],3W6B_D Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 [Ralstonia sp. A-471],3W6C_A Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 in complex with disaccharide [Ralstonia sp. A-471],3W6C_B Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 in complex with disaccharide [Ralstonia sp. A-471],3W6C_C Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 in complex with disaccharide [Ralstonia sp. A-471],3W6C_D Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 in complex with disaccharide [Ralstonia sp. A-471]
3W6D_A	1.76e-97	101	249	32	180	Crystalstructure of catalytic domain of chitinase from Ralstonia sp. A-471 (E141Q) in complex with tetrasaccharide [Ralstonia sp. A-471],3W6D_B Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E141Q) in complex with tetrasaccharide [Ralstonia sp. A-471],3W6D_C Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E141Q) in complex with tetrasaccharide [Ralstonia sp. A-471],3W6D_D Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E141Q) in complex with tetrasaccharide [Ralstonia sp. A-471]
3W6E_A	1.76e-97	101	249	32	180	Crystalstructure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) [Ralstonia sp. A-471],3W6E_B Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) [Ralstonia sp. A-471],3W6E_C Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) [Ralstonia sp. A-471],3W6E_D Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) [Ralstonia sp. A-471],3W6F_A Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) in complex with disaccharide [Ralstonia sp. A-471],3W6F_B Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) in complex with disaccharide [Ralstonia sp. A-471],3W6F_C Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) in complex with disaccharide [Ralstonia sp. A-471],3W6F_D Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) in complex with disaccharide [Ralstonia sp. A-471]
1ED7_A	1.17e-13	37	78	1	42	ChainA, CHITINASE A1 [Niallia circulans]
4ILV_A	1.40e-12	36	78	203	245	Structureof the dioxygenase domain of SACTE_2871, a novel dioxygenase carbohydrate-binding protein fusion from the cellulolytic bacterium Streptomyces sp. SirexAA-E [Streptomyces sp. SirexAA-E],4ILV_B Structure of the dioxygenase domain of SACTE_2871, a novel dioxygenase carbohydrate-binding protein fusion from the cellulolytic bacterium Streptomyces sp. SirexAA-E [Streptomyces sp. SirexAA-E]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	1.13e-10	37	78	655	696	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
P52320	1.03e-09	36	78	412	454	Streptogrisin-C OS=Streptomyces griseus OX=1911 GN=sprC PE=3 SV=1
P27050	1.25e-07	30	82	28	78	Chitinase D OS=Niallia circulans OX=1397 GN=chiD PE=1 SV=4

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
0.000235	0.999149	0.000149	0.000178	0.000145	0.000133

TMHMM  Annotations     

start	end
12	34