CAZyme Information: MGYG000002473_01578

Basic Information

• Species: Victivallis vadensis
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis vadensis
• CAZyme ID: MGYG000002473_01578
• CAZy Family: GH51
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
675		74237.94	7.3452

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002473	4576885	Isolate	not provided	not provided

• Gene Location: Start: 21036; End: 23063 Strand: +

Full Sequence      

MFHKLLPCTVIGAAISLGAATVVTVDPSRSEGAVNPYIFGHNIEGGNGKGYQGRTDTPAG
NYASGAWRPELNAPNSELVGILREAGAKLIRYPGGCLSHNFDWETAVGPQEKRPHQKFGI
PELVRFCREIGAEPLITLGDLTTPESAAELAEYLNSPADDAHPWAKQRAADGFPQPCNVK
FIEIANESDHGNHQGEPRLVRTPQQYADWVDRVIRAIRKVDPTIRLGGHFSTGTGWQDPW
NTALLRKNGRQLDFIALHPYATVVEQAARANAYPELILESALAAPDQTGALVREYHANTR
RLTGRDIPIALTEYNMLWIDTRSPQGMLSYGPALYCADLIRVMLQKENNIAFANQWQFVN
GYFGFVHGGRWKEGRPLNPWHKLPGYWLYRLWGSHFGTEQVGVAVTGEPKVEFGGISRTR
QAGDAPAVPVEFRPDAADKENYRIIPTGPDSFTLKLKDFSGEAYHNFPPFAIRPGVSYRA
DYEFRVKSGDDSGAAVGLGFTDARGWSKTMSASGMESELWEREWIRRSVSLAVLPDAEQL
SLVVRMIRGVKPVNAEIEFRNIRLTQGPQFPAYSAVTSAASLSPDRRTLYVIIFNKLQKE
SAPITVKVADGSARSARLWQVTGPSLAANNWKTQEVAETVSGAEIPAVSPQGFGLTLPPL
SMTAVEITRELPAGK

Enzyme Prediction     

No EC number prediction in MGYG000002473_01578.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH51	21	360	5.5e-52	0.49206349206349204

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3534	AbfA	7.87e-31	23	360	6	352	Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].
pfam01229	Glyco_hydro_39	1.33e-06	181	358	151	310	Glycosyl hydrolases family 39.
cd21510	agarase_cat	4.43e-05	144	260	76	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHF91758.1	7.09e-113	20	667	37	722
AVM45703.1	5.90e-111	13	669	14	686
AVM45928.1	2.82e-109	4	666	6	687
AHF89202.1	1.38e-108	7	669	14	700
SDT94913.1	3.92e-108	25	669	38	695

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3S2C_A	2.59e-25	23	408	5	369	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	3.40e-25	23	408	5	369	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	4.10e-25	23	408	25	389	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]
2Y2W_A	1.71e-19	13	325	45	352	Elucidationof the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_B Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_C Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_D Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_E Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_F Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum]
5O7Z_A	3.53e-16	23	412	5	421	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P53627	6.05e-22	24	323	7	303	Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces lividans OX=1916 GN=abfA PE=1 SV=1
Q841V6	9.09e-19	13	325	45	352	Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Bifidobacterium longum OX=216816 GN=abfB PE=1 SV=1
E7CY70	3.03e-17	23	360	18	373	Exo-alpha-(1->6)-L-arabinofuranosidase OS=Bifidobacterium longum OX=216816 GN=afuB PE=1 SV=1
A3DIH0	3.58e-16	23	412	6	422	Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=Cthe_2548 PE=1 SV=1
Q59219	1.93e-14	1	272	1	273	Intracellular exo-alpha-L-arabinofuranosidase OS=Bacteroides ovatus OX=28116 GN=asdII PE=3 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
0.225392	0.771751	0.001914	0.000332	0.000285	0.000307

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002473_01578.