CAZyme Information: MGYG000000348_01817

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485
• CAZyme ID: MGYG000000348_01817
• CAZy Family: GH51
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1526	MGYG000000348_42|CGC1	168097.04	4.6845

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000348	2655711	MAG	Sweden	Europe

• Gene Location: Start: 16706; End: 21286 Strand: +

Full Sequence      

MRQSIGMFLCGLLLAGASSATAAVEFGIDASHRGPEIGKLHYGIFFEEINHAGDGGIYAE
LVRNRSFEDNTGNPDGWNKTSGVTWKLVTDNLLNSAQGQALDVTFGAAGDAVTNEGFWGM
NCEAGKSYRFSFWARSDKGYDGNLTAEMVSHDGKPLGNATVTVKAGKDWTKYTATIQPTG
SDTNASLKISAGKAGNLTFDMVSLFPPTFKDRENGCRPDLAQMLADMHPAFMRFPGGCYI
EGTHQNGVTNRFEWKKTIGPVETRPGHRNVNWNYRVSDGLGFHEMLQLSEDLGAEPLFVV
NIGLGHGWSVPYNSIDEYIQEALDALEYCNGDVTTRWGAVRAANGHPEPFNLRLIEVGNE
NYQADANQQSDHYAERYIQFYNAIKAAYPEAIVIGNVESWGTDTPSWRNEHPVDAVDEHY
YRNPSWFAANYNKYDSYSRQGPKVYAGEYAVTSDFGTNGTLRAALGEAIYMLGMENNSDV
CIMNSYAPIFVNENDQCWRPDMIRFNSSESYGTPSYYVQKLFANNVGSRNLKWTETGNTQ
NAGNKVGFSTWKSTAEFDNVRVSDTDGNPVWSEDFTTAPAGWTMPSGWSVTNGVLRMTDG
SAEGLIAASAKDAPDNFIFEFDAKKTGGDEGFLVAFNYGGPRDYIWWNLGGWGNTRHAIE
IARDGSKSSYGSTNGTIETNHQYHGRIVLSGTSLRCYLDNVLIHDIEIPSDRKIYMSANL
SEDEKTLYVKTVNMNADDVPVTLNLTNGKFVSGEATVMANTDSEAENSVDNQNNVVPVQG
NVTVTAGKADFTAPANSMCILKFTVSDVVSMKGKPMSEAALAEINASLGGLRQRLANLRA
GAQLPTQLDNAATIEWSLSADADPNATLSTSAWTTTLDVTAVENRDAKRAAGTLTANVTA
ADGSTGTLSFPVTVAPLDDAYGYLYCYMNSGKEITNYALGSREDKGRVFNQLNNGKEIFD
TEALCGIEHGSRDAYMQKGQRDHEWFMTVTDMCNAKSKVWNNYGIDLLRSNDLIHWESTV
FDFRQGKKIFSDPDAVTDLYKTDAEYAKIRRVWAPQFIWDPAAFNGQGGYLVYYSVLSDN
AGDNHDRIVYSYADKDFKTLTQPRIFHDPGYSVIDGDIVYNDYDGKYHLWIKHEGASGTE
RGIWHLTSDRLVGDDWTYVDHNGNEGSENVEGSSAIRRINEDDMNIYYMRYSGGSHYKVC
TADHLGTNVKPSSDLGGTGAFQHGSVLYVNEAEYTLLTDWDELLKQMEWAQATESPIFKD
ALVQADAALKVQGFDALSEAIAKALDAMMKARETYMKDIVDNARDGDITSLIVNPDFNGN
NGRGWSGTGFTATNKGVAEFYNTTFDAYQELPYMPAGEYTLTCSGFYRNGGKEAYSLHTA
GTEALLAEVYMNETGTPFMSLFSADKYTNSPYTFPDDVTTANNAFNTDGSYAGNTVKLTL
DKTSTLRLGVRKSVHCDRDWTCFDNFRLTYTPDRSGMTGIVPDSNAPVNVYSLEGMLLRK
SVRRPDATAGLAPGLYIVGRTKVAVR

Enzyme Prediction     

No EC number prediction in MGYG000000348_01817.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH51	175	803	3.4e-104	0.8571428571428571
GH43	969	1226	2.2e-43	0.9914163090128756

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08983	GH43_Bt3655-like	2.29e-54	952	1240	2	262	Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655. This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
COG3534	AbfA	2.90e-42	200	797	34	492	Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].
smart00813	Alpha-L-AF_C	6.00e-21	447	543	1	97	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.
pfam06964	Alpha-L-AF_C	1.13e-20	447	539	1	96	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.
pfam02018	CBM_4_9	3.19e-07	59	195	1	134	Carbohydrate binding domain. This family includes diverse carbohydrate binding domains.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGB28798.1	0.0	12	1517	11	1417
QNT66893.1	2.04e-232	9	802	8	811
BCS85815.1	1.59e-228	17	802	3	793
ADE81175.1	1.91e-226	11	813	25	836
AGB28822.1	3.40e-223	8	802	6	803

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ZPS_AAA	2.15e-88	42	534	18	527	ChainAAA, MgGH51 [Meripilus giganteus],6ZPV_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPW_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPX_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPY_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPZ_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ0_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ1_AAA Chain AAA, MgGH51 [Meripilus giganteus]
4ATW_A	9.09e-19	213	421	46	237	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]
3S2C_A	9.22e-19	213	421	46	237	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]
3UG3_A	1.04e-18	213	421	66	257	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	1.15e-15	213	360	89	215	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P82593	2.85e-140	11	802	20	821	Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1
Q9SG80	9.56e-113	23	562	40	576	Alpha-L-arabinofuranosidase 1 OS=Arabidopsis thaliana OX=3702 GN=ASD1 PE=1 SV=1
Q8VZR2	2.33e-108	22	550	38	567	Alpha-L-arabinofuranosidase 2 OS=Arabidopsis thaliana OX=3702 GN=ASD2 PE=2 SV=1
Q8NK90	1.23e-85	3	527	11	528	Alpha-L-arabinofuranosidase A OS=Aspergillus kawachii (strain NBRC 4308) OX=1033177 GN=abfA PE=1 SV=2
Q96X54	2.27e-85	3	527	11	528	Probable alpha-L-arabinofuranosidase A OS=Aspergillus awamori OX=105351 GN=abfA 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
0.000482	0.998697	0.000219	0.000213	0.000188	0.000182

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000348_01817.