CAZyme Information: MGYG000001371_05135

Basic Information

• Species: Paenibacillus lautus_A
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus lautus_A
• CAZyme ID: MGYG000001371_05135
• CAZy Family: GH51
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
671	MGYG000001371_153|CGC1	75668.19	5.2444

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001371	6950059	Isolate	not provided	not provided

• Gene Location: Start: 6556; End: 8571 Strand: -

Full Sequence      

MNTNATITIDCSRKSEHEINPYLFGHFVEDIRDHMEAMLAFPLKDMDFESDAETKTPVSG
SWRAYTNGRNTQYAMEAPAPRHSGRTQRIRILSDDEAYAGITQKAALKGPMNYTVRLVAR
ASVELQYVTVEAVDRRTEETLGRLRMELGSHNWQHCEAQLSISRACSDAEIRVYVPAEHP
RWIDHVSTGMLWIDHVSFLPVDSIAMVKREVVEMTKDLNAGMMRLAGNYISAYHWEHGVG
PVLERPVMYNEAWGGWTSKYFGTDEFIRFCRELQVEPLICVNDGSGTPEEAAQWIEYCNG
GADTPMGALRARNGFPEPYNVKYWEIGNEVWGQWQVGTCTAEQFAERTISFAKAMKEADP
SIVLLACGHYEQNWNKAVLDLAGESIDYLTLHLYHGYGPFGMNRDTPAEDRYKAIASYPE
WTRHHVRQTTELIRSRPEHSHVKLAITEYNTMYYPNTVRKGLPNEHTLGAAVANAANLNE
MMRCSDMVHIGSFSDLVNGWLGGCIRVGDYYADQYCGKQPGWSGHPLTIYGTPTYEVLKL
YANRDVRRVLPVQAECGTFSVASRKETPLALDALPDLDIVAGTNDDGSIVTVLIVNRSLE
AVRAVLDLKAFEASGETTLYEITGDSYDDINSVFQPEHIMCKESRVPAEAWRQGYDLRPS
SVYALEFRAQV

Enzyme Prediction     

No EC number prediction in MGYG000001371_05135.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH51	207	668	3.6e-90	0.6492063492063492

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3534	AbfA	1.48e-71	207	670	50	501	Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].
pfam06964	Alpha-L-AF_C	4.35e-11	528	639	66	169	Alpha-L-arabinofuranosidase C-terminal domain. This family represents the C-terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase (EC:3.2.1.55). This catalyzes the hydrolysis of nonreducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.
smart00813	Alpha-L-AF_C	6.94e-11	529	651	64	178	Alpha-L-arabinofuranosidase C-terminus. This entry represents the C terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase. This catalyses the hydrolysis of non-reducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.
cd21510	agarase_cat	2.23e-04	281	394	73	187	alpha-beta barrel catalytic domain of agarase, such as GH86-like endo-acting agarases identified in non-marine organisms. Typically, agarases (E.C. 3.2.1.81) are found in ocean-dwelling bacteria since agarose is a principle component of red algae cell wall polysaccharides. Agarose is a linear polymer of alternating D-galactose and 3,6-anhydro-L-galactopyranose. Endo-acting agarases, such as glycoside hydrolase 16 (GH16) and GH86 hydrolyze internal beta-1,4 linkages. GH86-like endo-acting agarase of this protein family has been identified in the human intestinal bacterium Bacteroides uniformis. This acquired metabolic pathway, as demonstrated by the prevalence of agar-specific genetic cluster called polysaccharide utilization loci (PULs), varies considerably between human populations, being much more prevalent in a Japanese sample than in North America, European, or Chinese samples. Agarase activity was also identified in the non-marine bacterium Cellvibrio sp.
pfam03662	Glyco_hydro_79n	0.003	319	394	163	244	Glycosyl hydrolase family 79, N-terminal domain. Family of endo-beta-N-glucuronidase, or heparanase. Heparan sulfate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulfate (HS) affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena involving cell migration and response to changes in the extracellular micro-environment. Heparanase degrades HS at specific intra-chain sites. The enzyme is synthesized as a latent approximately 65 kDa protein that is processed at the N-terminus into a highly active approximately 50 kDa form. Experimental evidence suggests that heparanase may facilitate both tumor cell invasion and neovascularization, both critical steps in cancer progression. The enzyme is also involved in cell migration associated with inflammation and autoimmunity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYB46505.1	0.0	1	671	1	671
ACX63063.1	0.0	1	671	1	671
QOT08713.1	0.0	1	671	1	671
AWP29691.1	0.0	1	670	1	670
ANA80826.1	0.0	1	670	1	670

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3S2C_A	9.44e-63	208	636	50	451	Structureof the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_B Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_C Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_D Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_E Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_F Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_G Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_H Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_I Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_J Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_K Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_L Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1]
4ATW_A	1.74e-62	208	636	50	451	Thecrystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_B The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_C The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_D The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_E The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_F The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8]
3UG3_A	2.89e-62	208	636	70	471	Crystalstructure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG4_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG5_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima]
5O7Z_A	1.53e-39	208	498	50	354	ChainA, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_B Chain B, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_C Chain C, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_D Chain D, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_E Chain E, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_F Chain F, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_A Chain A, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_B Chain B, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_C Chain C, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_D Chain D, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_E Chain E, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_F Chain F, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila]
2C7F_A	1.83e-39	208	498	61	365	ChainA, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C7F_B Chain B, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C7F_C Chain C, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C7F_D Chain D, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C7F_E Chain E, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C7F_F Chain F, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C8N_A Chain A, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus],2C8N_B Chain B, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus],2C8N_C Chain C, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus],2C8N_D Chain D, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus],2C8N_E Chain E, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus],2C8N_F Chain F, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q4WTB3	5.71e-50	208	631	60	470	Probable alpha-L-arabinofuranosidase C OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abfC PE=3 SV=2
B0XQB2	5.71e-50	208	631	60	470	Probable alpha-L-arabinofuranosidase C OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=abfC PE=3 SV=2
A1CQC3	2.05e-49	208	631	60	470	Probable alpha-L-arabinofuranosidase C OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=abfC PE=3 SV=2
Q5BDV3	3.81e-49	208	626	60	465	Alpha-L-arabinofuranosidase C OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=abfC PE=2 SV=1
Q0D1I6	5.24e-49	208	631	60	470	Probable alpha-L-arabinofuranosidase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=abfC 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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001371_05135.