CAZyme Information: MGYG000002717_02475

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides
• CAZyme ID: MGYG000002717_02475
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1205		136469.77	4.5436

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002717	5602088	MAG	Canada	North America

• Gene Location: Start: 2876; End: 6493 Strand: +

Full Sequence      

MKNITNVFYELLIALCCLMSSSTLWAWEDMPMPRLHVEGRYLVDPHGNKVNLHGFAQTYS
PWFNEMGQKWDNYDVAKCLKYNQGLIDDIMDAGWKMNFLRLHMDPYWSNSPGIHVEGEND
ISAFDFNRFKTYLDRVFIPMAEYAISKGLYVVMRPPGVCPEKIAVGDEYNQYLIKVWTHV
AQHPKLKNHPNIMFELGNEPINILGPDGTYGAGSQGHFDKLKEYFQSVVDAMRAQGCDNI
LWIPGLGYQGLYKGFAVNPIEGENIGYAVHLYPGWMGSDGENGDGGSSTGGYEPFQQGWD
DSVAPVAAFAPIMITEMDWAPSKYNASWGKAHTGTFGGPGFGANMKHIVDNSGNVSWLIF
TGADLLAKFKDTPPAEGEAYTFLTDPEACPWPTYHWYQEYAKENYPRPDFTYQSHSDNGD
GTYTNPVIFGDFPDPDVIRVGDVYYMVSTTMFIFPGATILKSYDLVNWKYCCNPLERIEA
SDGYNLENGQNRYSRGQWATALQYHDGKFYLLFTTLDEGGYLLTTTDIEGEWEKKKLNDG
FYDCGLLFDNDKIYVVYGINQLRIAELDADFNKIPGSDKDVVKWSFREGLEGSRLYKIGE
YYYIYSTYGGWPAFQTVFRSKDIYGPYEEKKLIDDDNIHQGALVETQTGEWWTMLFYDKG
AYGRFPNLQPVKWVDGWPEIGENGKGVTTYRKPDVGREYPIKSLPTNDNFRHYKLELQWG
WNHNADRSKWSLTEHAGYLRLYTANVTDNLHKAKNTLTQRILGYPQDLEHSYGTVRMEIG
KMQEGDVAGLAVFQDPYAFIGIKVIDGQKRLVYTTAPVVSSAAKSEQIGEVVTELVIYLR
AIANYSTSKSSFYYSLDNKTYTKLGDDLNMKYDLTVFTGNKFAIFNYATVQTGGYVDVDW
FSTEPEFDEEFYFDDSFEGYSEESLTLTELAINGDEELTLLTGSSSTITVKGIYADGHTE
DITMAADYENQNPDVVRVTNGRIMALQDGESDIVISYKGPLGDRQSLTIHVTSSTFPLTA
ELFNPNIYATGSFDENTHTLVTGQYGFGGWWYDNGIDLSEYKYVVAKMGNDNSDNGASFR
LFDENNYWSGAAEYEIKSSKQVVVDLNNMYKGNPKVKLDPSHIYIVGFWALGGKPIVIEK
VYLTNSDDYEDPTGIEDVTVDKDPLVDVYTITGIKLRTQVRRSEVIRELPAGIYIVGREK
IAILK

Enzyme Prediction     

EC	3.2.1.8

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	49	324	4.8e-121	0.9922779922779923
GH43	424	678	3e-95	0.996309963099631

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09001	GH43_FsAxh1-like	2.06e-125	422	681	1	270	Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase. This glycosyl hydrolase family 43 (GH43) includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase; xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These 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. This subfamily includes the characterized Clostridium stercorarium F-9 beta-xylosidase Xyl43B. It also includes Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase (EC 3.2.1.55) that hydrolyzes O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. It possesses an additional C-terminal beta-sandwich domain such that the interface between the domains comprises a xylan binding cleft that houses the active site pocket. The HiAXHd3 active site is tuned to hydrolyze arabinofuranosyl or xylosyl linkages, and the topology of the distal regions of the substrate binding surface confers specificity. It also includes Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase (Axh1;Fisuc_1769;FSU_2269), Paenibacillus sp. E18 alpha-L-arabinofuranosidase (Abf43A), Bifidobacterium adolescentis ATCC 15703 double substituted xylan alpha-1,3-L-specific arabinofuranosidase d3 (AXHd3;AXH-d3;BaAXH-d3;BAD_0301;E-AFAM2), and Chrysosporium lucknowense C1 arabinoxylan hydrolase / double substituted xylan alpha-1,3-L-arabinofuranosidase (Abn7;AXHd). 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.
COG3507	XynB2	8.38e-70	416	901	14	544	Beta-xylosidase [Carbohydrate transport and metabolism].
cd08989	GH43_XYL-like	8.14e-57	425	673	1	271	Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). 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.
pfam04616	Glyco_hydro_43	4.67e-46	423	678	1	281	Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd18617	GH43_XynB-like	8.81e-44	425	680	1	285	Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These 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. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDO68289.1	0.0	1	1205	1	1205
EDV06040.1	0.0	1	1205	1	1205
ALJ60064.1	0.0	1	1205	1	1205
QUT88923.1	0.0	1	1205	1	1205
BCS84804.1	0.0	30	1203	1	1152

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MLY_A	3.26e-103	424	920	22	532	ChainA, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_B Chain B, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_C Chain C, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_D Chain D, Bifunctional GH43-CE protein [Bacteroides eggerthii]
3ZXK_A	1.73e-66	422	898	7	526	Engineeringthe active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens],3ZXK_B Engineering the active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens]
3ZXL_A	4.35e-66	422	898	7	526	Engineeringthe active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens],3ZXL_B Engineering the active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens]
3ZXJ_A	2.75e-65	422	898	7	526	Engineeringthe active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens],3ZXJ_B Engineering the active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens]
6MS3_A	1.88e-43	418	901	25	533	Crystalstructure of the GH43 protein BlXynB mutant (K247S) from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580],6MS3_B Crystal structure of the GH43 protein BlXynB mutant (K247S) from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
T2KN85	6.24e-68	414	902	42	581	Beta-xylosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22160 PE=1 SV=1
Q9WXE8	4.64e-51	407	767	22	387	Putative beta-xylosidase OS=Prevotella ruminicola OX=839 PE=3 SV=2
A7LXU0	9.55e-42	422	741	26	367	Non-reducing end alpha-L-arabinofuranosidase BoGH43B OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02656 PE=1 SV=2
A9ZND1	1.37e-37	422	901	4	530	Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
A7LXT8	7.86e-35	423	795	23	408	Non-reducing end alpha-L-arabinofuranosidase BoGH43A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02654 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
0.000383	0.998861	0.000263	0.000168	0.000146	0.000141

TMHMM  Annotations     

start	end
7	26