CAZyme Information: MGYG000002365_00561

Basic Information

• Species: Bifidobacterium globosum
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium globosum
• CAZyme ID: MGYG000002365_00561
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
560		61063.67	4.4576

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002365	2036949	Isolate	Kenya	Africa

• Gene Location: Start: 642066; End: 643748 Strand: +

Full Sequence      

MTATTATMDITNPVLRGMYPDPSWMWDEPGERVALVNSSFELVPGLPIHVSDDIANWELA
GNAVDEAMAQRLLIPFVLDSGGLYAPTLRMIRGKYVIACTVARIDLDAAAAAGVDPESIE
GARASQGNFIIEADALEGPWRGPYWIEGAEGIDPDIFEDLDGSVYWTQTRPAVRPRWEGQ
TEVWTQRIDPETWRLCASHDADGDYGKTVLWTGYGVEAVWAEGPHLYRIGDWVYLMTAEG
GTSFDHSEMTMRAWAPDGLGPAVEALQFQAHEDGTEPRAPRADERSVVGRYARLFHPCKK
NPFLTHRHLGLEERVQCVGHADLLHHPRLGWWVTCLGSRETPTADHGALSFLGRETFVAP
VDWQHDPAQWSLESNGPAQRRTDDPGWPILAGGVGRLAQTLRIDAADGTLLDMCIGPCES
QAVVDARVPFAVGDGEGAAVRADGTVYRRMPEDRCVVLCPPRGTVRIRQDGRHTLSVATD
GASVQWALGEGTERREGMVPIPEGEPGSVMLVFDKGMVRVVVAQSAEQAWTAPAVEVIDV
APLSTEWSGGFVGCLVGCDA

Enzyme Prediction     

EC	3.2.1.55

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	11	366	3.6e-95	0.9857651245551602

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18617	GH43_XynB-like	3.81e-117	12	366	1	281	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.
cd08989	GH43_XYL-like	4.61e-47	12	364	1	272	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.
cd09000	GH43_SXA-like	8.22e-47	12	366	1	287	Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA. This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. 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. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. 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.
cd18833	GH43_PcXyl-like	6.08e-45	12	363	1	285	Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). This glycosyl hydrolase family 43 (GH43) subgroup includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a characterized bifunctional enzyme with beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) activities. This subgroup belongs to the GH43_XybB subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_XybB subgroup includes enzymes having beta-1,4-xylosidase and alpha-L-arabinofuranosidase 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. The GH43_XybB subgroup includes 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. 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	2.85e-44	10	366	1	278	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIZ15987.1	0.0	1	560	1	560
ASW24482.1	0.0	1	560	1	560
ATO40315.1	0.0	1	560	1	560
AYN23377.1	0.0	1	560	1	560
AFI62741.1	0.0	1	560	1	560

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z5D_A	9.75e-42	8	405	1	298	Crystalstructure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 [Geobacillus thermoleovorans],5Z5F_A Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 in complex with L-arabinose [Geobacillus thermoleovorans],5Z5H_A Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 in complex with D-xylose [Geobacillus thermoleovorans],5Z5I_A Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 in complex with L-arabinose and D-xylose [Geobacillus thermoleovorans]
5JOZ_A	2.87e-40	12	366	7	280	Bacteroidesovatus Xyloglucan PUL GH43B [Bacteroides ovatus],5JOZ_B Bacteroides ovatus Xyloglucan PUL GH43B [Bacteroides ovatus]
7K1R_A	5.11e-35	8	393	1	308	ChainA, Beta xylosidase GH43 [Enterobacter sp. enrichment culture clone nf1B6],7K1R_B Chain B, Beta xylosidase GH43 [Enterobacter sp. enrichment culture clone nf1B6],7K1R_C Chain C, Beta xylosidase GH43 [Enterobacter sp. enrichment culture clone nf1B6],7K1R_D Chain D, Beta xylosidase GH43 [Enterobacter sp. enrichment culture clone nf1B6]
5JOW_A	2.57e-34	11	388	14	306	Bacteroidesovatus Xyloglucan PUL GH43A [Bacteroides ovatus ATCC 8483],5JOW_B Bacteroides ovatus Xyloglucan PUL GH43A [Bacteroides ovatus ATCC 8483],5JOX_A Bacteroides ovatus Xyloglucan PUL GH43A in complex with AraDNJ [Bacteroides ovatus],5JOX_B Bacteroides ovatus Xyloglucan PUL GH43A in complex with AraDNJ [Bacteroides ovatus],5JOY_A Bacteroides ovatus Xyloglucan PUL GH43A in complex with AraLOG [Bacteroides ovatus],5JOY_B Bacteroides ovatus Xyloglucan PUL GH43A in complex with AraLOG [Bacteroides ovatus]
3C2U_A	5.70e-29	8	407	1	320	Structureof the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium],3C2U_B Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium],3C2U_C Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium],3C2U_D Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45982	6.04e-50	12	557	6	493	Xylosidase/arabinosidase OS=Butyrivibrio fibrisolvens OX=831 GN=xylB PE=3 SV=1
A7LXU0	1.92e-39	12	366	29	302	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
P77713	1.30e-33	8	393	1	308	Putative beta-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yagH PE=3 SV=1
A7LXT8	1.58e-33	11	388	24	316	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
P07129	1.13e-25	8	393	1	306	Beta-xylosidase OS=Bacillus pumilus OX=1408 GN=xynB PE=1 SV=2

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
1.000057	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002365_00561.