CAZyme Information: MGYG000000919_00215

Basic Information

• Species: Niameybacter sp900551325
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Cellulosilyticaceae; Niameybacter; Niameybacter sp900551325
• CAZyme ID: MGYG000000919_00215
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
635	MGYG000000919_1|CGC2	73095.36	6.0325

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000919	4175004	MAG	China	Asia

• Gene Location: Start: 244623; End: 246530 Strand: -

Full Sequence      

MDNIIEAIKGSNIEAIRKIIATNQMAIEEKDEHNVLAPFVAAKTGSLEVLKFIVEYTRAS
MNYTDEINRNILHYAAMSDSLECFKYLVEQVGMDIYSGDKYGKTAIDIALETNNMAIVNY
LRNEKGIILEDMYRNPIITGAHPDPSIIRVGEDYYMVNSTFIYFPAIPVLHSKDLIHWKI
IGHGITNPNYLDFDRLETGRGIWAPDISYYEGKFYITATYRLNDDDPMIRKQIIISSNRA
EGPYSEPIFIEEDGIDPSLFVDDDGKRYMLLNRGARLIELDAKATKVVKEGELIYYGSNK
RAPEGPHLIKKDGYYYLFLAEGGTGLTHCITVARSKNIKGPYKPCPYNPILTQRNPLHKI
QRSGHGKPVQTQNGDWYMVYLCGRPIGDGYCILGRETAIDPLTWTPDGWPIINKNQGPSV
LQRRPNLPSCKWEEVVCDHFDKEDLDLNWLFVRTPDEGSYSIGKSYLRIVGSYKDLNEKE
AKNIIVKRQKHHHFEAELKLDFHSYGIGQEAGMTCYYDTLTYIKVGVMNKGEEWVIRVIE
RIGEREILSFEERVEKDKPIFIKVVTKYLERTFYYRQDETKWNKLGTLENVYYLSDEGEK
GKRFTGSMIGMYVVNGMTEPRCYGDFDYFSYKGLE

Enzyme Prediction     

No EC number prediction in MGYG000000919_00215.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	134	410	1.2e-98	0.99644128113879

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08989	GH43_XYL-like	2.25e-157	135	405	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	2.32e-132	135	412	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.
cd09000	GH43_SXA-like	1.71e-119	135	410	1	290	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.
COG3507	XynB2	4.29e-119	128	634	16	549	Beta-xylosidase [Carbohydrate transport and metabolism].
pfam04616	Glyco_hydro_43	7.63e-103	133	410	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABX41261.1	2.62e-206	126	635	124	635
AUO18981.1	2.35e-194	126	632	126	635
BCJ96881.1	3.68e-194	130	630	130	638
CBL11992.1	7.48e-194	126	635	125	629
CBL09363.1	7.48e-194	126	635	125	629

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MS2_A	1.62e-186	130	631	27	535	Crystalstructure of the GH43 BlXynB protein from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
6MS3_A	9.20e-186	130	631	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	5.14e-109	134	635	6	527	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	2.26e-99	133	633	13	510	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]
2EXH_A	1.64e-97	134	634	5	535	Structureof the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_B Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_C Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_D Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A7LXT8	1.64e-98	133	633	23	520	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
A9ZND1	3.78e-95	134	631	6	532	Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
P77713	1.55e-89	135	632	5	534	Putative beta-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yagH PE=3 SV=1
A7LXU0	1.80e-89	128	635	22	529	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
P94489	3.22e-87	135	632	5	531	Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 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
1.000073	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000919_00215.