CAZyme Information: MGYG000001237_00515

Basic Information

• Species: UMGS1600 sp900553295
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; UMGS1600; UMGS1600 sp900553295
• CAZyme ID: MGYG000001237_00515
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
617	MGYG000001237_14|CGC1	69196.4	6.4553

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001237	2708995	MAG	Austria	Europe

• Gene Location: Start: 8400; End: 10253 Strand: +

Full Sequence      

MDTAQLMRIIREDNVAEVRRALALWPGLVETATPAGEPLSHWAAREGSLAMLRLLVEYGT
KVNLNAVDESGRDMLHYAAESGNVGKCRYLVERGGMDPLRGDLELITPYDLAHQGGWKQL
EAYFAAVVGAPWEAMYRNPIRSGMYPDPSICRVGEDYYMVNSTFVYFPCIPVSHSRDLVH
WEVIGHAITRPEWANLEGLEGGRGYWAPDISYAEGRFYICATLRLNDGGEVCRRQMVVTA
QRPEGPYSEPVFFEEDGIDPSLFHDTDGRHYMLLNRGARIFEVDAQATRRLSETTLLYYG
SCKRAPEGPHLLKKDGWYYLFLAEGGTGMGHRETVARSRNLHGPYEPSPYGPVLRQWDER
ALIQRCGHAKPVSTPDGRWYLVYLCGRALEGQWTLLGRETALDPIQWTADGWPLLNHGRG
PSVLQRKLLPDAPVHGSVDWLTPRPPQPGTVHWCGERLTLRAGDSDLTEVSCRSLQVRRQ
TAFRCSFAATVTVPRRGEAGIVCYYDEHSFLALGVRHRENGMRLWQREQIGLECREQDLG
PCPVQAGQGLRLGVRCDGLTRRLYAGEGDTPVSLVERATYLSDEGVSLGKRFTGAMIGMY
AVRQAEAQFADITYTEG

Enzyme Prediction     

No EC number prediction in MGYG000001237_00515.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	137	413	1.1e-93	0.99644128113879

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08989	GH43_XYL-like	6.82e-152	138	408	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.
cd18617	GH43_XynB-like	6.66e-126	138	413	1	284	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.
cd09000	GH43_SXA-like	9.25e-112	138	415	1	292	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.
pfam04616	Glyco_hydro_43	7.18e-97	136	413	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.
COG3507	XynB2	2.45e-96	135	602	20	530	Beta-xylosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL11992.1	2.31e-211	6	611	3	619
CBL09363.1	2.31e-211	6	611	3	619
VCV21971.1	1.32e-210	6	611	3	619
ABX41261.1	2.78e-206	5	614	2	631
QOV20144.1	1.33e-197	44	602	532	1105

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MS2_A	6.42e-128	133	614	27	535	Crystalstructure of the GH43 BlXynB protein from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
6MS3_A	3.60e-127	133	614	27	535	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]
1YRZ_A	1.54e-89	137	599	6	504	ChainA, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125],1YRZ_B Chain B, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125]
5JOW_A	4.89e-82	136	523	13	415	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]
5JOZ_A	1.63e-77	136	524	5	411	Bacteroidesovatus Xyloglucan PUL GH43B [Bacteroides ovatus],5JOZ_B Bacteroides ovatus Xyloglucan PUL GH43B [Bacteroides ovatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A7LXT8	3.47e-81	136	523	23	425	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
A7LXU0	1.27e-76	136	524	27	433	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	1.30e-71	137	435	6	327	Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
P94489	3.84e-66	138	599	5	511	Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2
P77713	2.18e-64	138	614	5	530	Putative beta-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yagH 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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001237_00515.