CAZyme Information: MGYG000001542_04931

Basic Information

• Species: Paenibacillus_A sp900069005
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A sp900069005
• CAZyme ID: MGYG000001542_04931
• CAZy Family: GH87
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2135		232345	4.5049

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001542	5846629	Isolate	not provided	not provided

• Gene Location: Start: 727810; End: 734217 Strand: -

Full Sequence      

MRQFKPILAALMSLLLIVSAFPTFADQAKAAAEGSGAAEIPSGKVLIKNKWKSNYLYEAS
DGTVRYGMTNPADESAQWVVDTDQGQSRIKNVKTGHYITVARTTQRYQALTTNETANSHA
ETWIIDRSNRAGYMVIRSATVPEGNLVIHEEDQLGFAEASSDINITFESPQWAFIAVEGS
PVRIESYMHPGSVIYEEDGLVKHGARPADDLMSHWYIESSSGNQITIRNRATGHFMTQNE
TTWAGIFAIDEDPAQPELSRWKQEDAVNQPGYIVFENAGLPGNWMNPQFPDDNNVRSNDW
AGGPDGFNALWKVVPASDLPAVRIAAYTDAPAPADFLYEDGGEVRYGAIDPASGSDSRYL
WIIEDYDLSKRIRNAASNHYLNIAGDQLSSGEASVTNATYEWSFTASDSYDDYNTIRNVG
RPELYISTGSGGSATVTTDADGLGSQWERVDPALVLDGSDQYIRIQNVWQPFYIYENADG
TIKYGNMRTDDQRDQWLVVKHDGRKLLKNRETGHYMNIADMPDGHIQATPLSDLSNIDET
YIWSGKNIGGGTYLLSNVTDKVPGEPFTKFISIQNLSKYAEYSVINPNWGSPQWKFLPVG
EKHQQLYRFRIPGTEGQYLQDERTADSVTEVTYGPADDEYSIWFLDEKNGADGPVMMKNM
GSGRYLSIQNLADAQVESEDEPALTVEARSEVYDTWGSIKWKIEQRDQDEVNIRSAWTGH
YLYATLNEQGKPVFKVSRAEGAADRAESIFMAEPAQIAEKPLPDGPVRIKSALNHAYLYE
NRSGVVLYGDPAADNGYSHWVIEPSADGRQRVQNRATGHYLMLNEDYNFVESKELSGGDS
TASMWAINRVAGGDQVLIRSQYGDYNDEFIHVQNNTGYAERGLYPDSSASVQWELESAPS
QFSTPNMDEERNLNTATPVQDDTNVIAIAPQGAGGKMLAEQSGTIQLVSGDEAHAASRWI
LQDFNGRHLIKNTATGHYLSLDKSLKLSVSTSMKPLGAQWILNEPLGYRTLSNTVDASGL
LQYNMDGIFYGTAAATSESALWSFTPVAADIAYAAGDAFRTDKVIRFAVHAQEQGEYKGL
IRYKNDSGTEQLLSVKVNGLEEQSAAFKPSVGLSTVEVKLNLRAGMNTVSLSGANGDLSA
VQIDSLTVKNSVNKAYRGATVPYVNYEAEDMKTNGVLLGPSRKYRNIASEASGRQAIQLK
QTGDYVEFALAEAANSLVVRYSIPDSTDGAGDEQTLSLYVNEQFKQSLKLTSKYAWEYGS
YPWSNDPRQGSGHRFFDEIHALIGDVPQGTVIRLQKDAGDQADFYAIDLVDMEQVAPAYE
MPEGFVSVIDFGAVPNDGQDDTMALKEALSAARDRGTGVWFPAGSFDFGDQLLDLDAAVI
RGAGMWYTTLNGAKFYGHGGTVEVYDLLIDGGMNERDDEAFTNAFHGAFGPGSILQQVWI
EHTKAGLWLTQPIGEKARTNELYMMGLRIRNLMADGINFAVGTTNSMMEQSDIRYPGDDG
IAMWSFTDSKLTDMNGSERTPSVNNTARFNTVALPWLADNIVVFGGRDNKIQDNIVKDTV
ANGAGIAVSTRFNAEPFAGTTVVERNTLIRTGSYDTGYGVSLGALWLFAGESDMKGKIVV
QDNVVKDSTYAGLIAHGDFTVEDVLLRNIVIDGTGTNGVDVTSGLKGSATVDNMIIRGDR
MKMVSNPSSAFSFKEINEGFASGKKPSVDPEEPGNPGPGGGEHPGTGSTGGLSGGTGTGQ
SAGSLSDSILQEALRQGKTAIELKTDAEGRVNLTAAVLAAAAAEHPEAVIEARGEGGSVY
RFPLSLTDQVIEQAGVVDQKQAVVSIQISSQKQAGFNDKAKQQGMELVGNAMEFRVQVSE
GAKTVQIERYDGANYVLRQWIVDRELDPSTTVVLLYDPATGKLSYVPAWLENNADGTTTV
MVKSAANGIFVAAQHPATFADIEGHWAQMAIEKLAARQILNGVGGDLFAPRQPVSRAEFA
AMLVRALDLQGSSSGDASYNDVKSDAWYGDAIAAAVHYGLVQGYADHSFRPNAQITREEM
SVMGARALRLLQNGVKQGTGTEAFLAAGEGTDLVSGYADGPQLHPWSQAEAELMLQAGIM
QGQSQDKFAPASRTTRAEAAAILSRLLAAVKLLNP

Enzyme Prediction     

No EC number prediction in MGYG000001542_04931.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH87	1131	1687	1.6e-174	0.8509212730318257

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14490	CBM6-CBM35-CBM36_like_1	3.89e-70	1158	1311	1	155	uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily. Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules.
NF033190	inl_like_NEAT_1	4.68e-14	1939	2123	582	748	NEAT domain-containing leucine-rich repeat protein. Members of this family have an N-terminal NEAT (near transporter) domain often associated with iron transport, followed by a leucine-rich repeat region with significant sequence similarity to the internalins of Listeria monocytogenes. However, since Bacillus cereus (from which this protein was described, in PMID:16978259) is not considered an intracellular pathogen, and the function may be iron transport rather than internalization, applying the name "internalin" to this family probably would be misleading.
cd04083	CBM35_Lmo2446-like	2.78e-12	1038	1148	6	125	Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases.
pfam00395	SLH	3.84e-11	1999	2040	1	42	S-layer homology domain.
pfam12708	Pectate_lyase_3	3.66e-09	1325	1397	1	75	Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWV32140.1	0.0	1	2134	14	2300
ASS68999.2	0.0	1	2128	1	2224
QJD83813.1	0.0	15	2133	15	2210
QJC51422.1	0.0	3	2133	5	2213
QGG55568.1	0.0	3	2133	5	2230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7C7D_A	1.29e-78	1158	1703	54	577	Crystalstructure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3 [Streptomyces thermodiastaticus],7C7D_B Crystal structure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3 [Streptomyces thermodiastaticus]
5ZRU_A	6.34e-71	1150	1659	5	528	ChainA, Alpha-1,3-glucanase [Niallia circulans],5ZRU_C Chain C, Alpha-1,3-glucanase [Niallia circulans]
6K0M_A	2.26e-43	1157	1633	13	492	Catalyticdomain of GH87 alpha-1,3-glucanase from Paenibacillus glycanilyticus FH11 [Paenibacillus glycanilyticus],6K0N_A Catalytic domain of GH87 alpha-1,3-glucanase in complex with nigerose [Paenibacillus glycanilyticus]
6K0P_A	2.40e-42	1157	1633	13	492	Catalyticdomain of GH87 alpha-1,3-glucanase D1045A in complex with nigerose [Paenibacillus glycanilyticus]
6K0S_A	2.40e-42	1157	1633	13	492	Catalyticdomain of GH87 alpha-1,3-glucanase D1069A in complex with nigerose [Paenibacillus glycanilyticus],6K0V_A Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_B Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_C Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_D Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38536	8.01e-27	1882	2127	1628	1855	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
C6CRV0	1.38e-25	1885	2126	1231	1458	Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P38535	1.48e-21	1901	2127	867	1081	Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
P38537	6.88e-18	1914	2127	12	206	Surface-layer 125 kDa protein OS=Lysinibacillus sphaericus OX=1421 PE=3 SV=1
P36917	1.16e-15	1873	2041	981	1156	Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA 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
0.000250	0.998983	0.000234	0.000200	0.000169	0.000144

TMHMM  Annotations     

start	end
7	24