CAZyme Information: MGYG000001507_04030

Basic Information

• Species: Paenibacillus ihuae
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus ihuae
• CAZyme ID: MGYG000001507_04030
• CAZy Family: CBM54
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1515	MGYG000001507_1|CGC58	162122.52	4.6484

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001507	6631509	Isolate	not provided	not provided

• Gene Location: Start: 4176517; End: 4181064 Strand: -

Full Sequence      

MYRRGISKLLVTVMLLSGLQLPGNIGLAKAAGPEGLPGSAVSASNINAAGTAMFADMKQH
WAAEAADRLAAAGILQGDGQGQFGPSRAVSRAEMAVILNRVFRYTDSGSAVFSDVSASSW
YGKDIGGVNAAGIIKGYADGRFQPEAAVTRQEVITMLVRAFLLEAASQTALALQADGSSV
SEYAREAVSAMLDAGYIRGDSAGKLNPQAPMTRAELAVLLGRMIGWISPDKGSYSIGEVS
GSVIVNRADVRIEGGSVNGNLYVTAGIGEGEVSLSGLKVKGTTRISGGGGHSVVFHKSSL
GQTIVDKPKVPVRLVLEDESSAARIELIQPAKVEIGTGSRVEALIVGAGAAGSEIVNRGH
IGLLDPKAGSVLLNGTALKTGETLRGLSGSASSPQTSATVTAAGGGNGGGVTPSPTPAAT
ASAVPTATAAASATPAATATATPSTHNDPWELVWNDEFDGSSIDGNKWNVQDTGTVYNNE
LEYYHPDNVALETESGQGVLALEARKEAYGGKEYTSGKLTSKMKGDWTYGKFTVRAKLPI
QQGMWPAIWMMPTDEEKQYGPWPGSGEMDIMELTGPVAGDTEKADLYPRTVHGSLHYDIP
HTSQSKTYVLPEGKTFADDYHDFTLEWLPGLIRYYVDGKMYFETSDWGTKAEGQPDYYTY
PAPFDRPFYMILNLAVGGDWPGNPAADFQSDKMYVDYVRVYKYKKLDEWPDVTGKRPTKP
ETSDPQRPVLADGNQIYNGDFKGATAADGLPQYWELIKNAGGAGTASVIEDKDKGKAVKV
AIQQAGTQNYSVQLTQMPLILEKGKAYKVTFDAKADAVRPVMSKLTEFGGGWTAYSKERN
FQLTPDWQSFEYTFNMAQATDNNVRFEFNLGLNDITAYFANVRVVETQPLPVVRTPLADG
NLIYNGGFELGEDRLGYWRFAVKPESGAAADAKVTNILELPLMKRIFSAQVDTTGKSAED
VMLTQTGLPVSAGGVYQLYFDARSEQSQPMGIKLEAGGGDTLYPDGSTLTLTPEWKSYTA
EISMSSTAGTEGTLSFLLGQAAGHTEIDNVRLVRMAEPPALNGYLHLRGDQYSGASGITL
MPSGEGGKDITDMNKGDYAEYKVVLPQAASIVPVARVSSVQAESELELSVLDAGKRSVAT
AAVYSAAIGDTGGLQSYRTVIGVPLELPAGSYYFRLEGSGYNLAWLDLSRELVVNGSFRE
ATTEGWTLFKKDWVDNDPVKNTVMTAEHGALQVDLGGSGDEEWNVQVKQGGIPMEQGKKY
LLRFDAEASIARQIRILLQHDGSIDKDWTAYMNEKVDLSEAGGHFEYLFTAPASDPAALL
QFSLGKVSEPLEAHRIKLSNISLLQVSPVMAGEAYGENLIPNGDFSAPLQGWSSYSSDSG
ELSIDNVNGALRMQVGSTGSNSWDRQVYYEGVAYNEGNHYTLTFKAKAEAARKMNISIGW
LDAANNYTWHGYASKVVDLGTDYNTYTLEFDVTGDSTSIGRISFELGNITDGGTGHLAVD
VDDVVLMNNGAIPAP

Enzyme Prediction     

No EC number prediction in MGYG000001507_04030.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	454	701	6.8e-73	0.9956521739130435
CBM4	734	871	5.9e-35	0.9920634920634921
CBM4	1358	1487	5.2e-31	0.9920634920634921
CBM4	1191	1325	2e-27	0.9920634920634921
CBM54	219	331	2.3e-27	0.9824561403508771

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	2.30e-83	454	701	1	235	Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
cd08024	GH16_CCF	1.03e-41	452	702	1	330	Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
cd00413	Glyco_hydrolase_16	1.80e-40	456	701	1	210	glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.
cd02182	GH16_Strep_laminarinase_like	5.37e-39	450	701	2	258	Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel.
COG2273	BglS	1.94e-36	446	709	37	271	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSF43977.1	0.0	1	1515	1	1515
QUL53694.1	0.0	1	1515	1	1514
AIQ60350.1	0.0	1	1514	1	1505
ASA23665.1	0.0	54	1512	40	1500
QZN74350.1	0.0	3	1510	2	1482

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ILN_A	8.13e-50	450	703	5	249	ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
2HYK_A	2.06e-46	452	702	9	243	Thecrystal structure of an endo-beta-1,3-glucanase from alkaliphilic Nocardiopsis sp.strain F96 [Nocardiopsis sp. F96]
3AZX_A	3.32e-46	450	702	10	255	Crystalstructure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZX_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZZ_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3B00_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B01_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8]
4DFS_A	5.33e-46	450	704	18	265	Structureof the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4DFS_B Structure of the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1]
2VY0_A	2.28e-45	450	703	13	261	TheX-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus],2VY0_B The X-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45798	2.67e-49	450	703	40	284	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
P23903	1.40e-42	452	702	425	680	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
Q27082	9.52e-34	445	702	20	253	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
C1IE32	2.01e-32	450	703	20	269	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q9ZG90	2.45e-29	450	702	56	288	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 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
0.000287	0.998976	0.000195	0.000202	0.000161	0.000136

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001507_04030.