CAZyme Information: FPRO_16010-t41_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRO_16010-t41_1-p1
• CAZy Family: GT64
• CAZyme Description: probable beta-xylosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
483		55251.19	6.4031

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FproliferatumET1	16509	1227346	366	16143

• Gene Location: location=FJOF01000019:138813-140425(-)

Full Sequence      

MPSVRNPILPGFNPDPSILRVGKDYYIATSTFEWYPGVQIYHSTDLANWTLVTRPLSRES
QLDLRGEPDSCGVWAPCLTYDGDEFWLVYTDVKRKAGSFKDTHNYIIHASSIGGPWSDPI
YTNSSGFDPSLFHDDDGRKWFVNMLTDHRSRPEPFAGICLQEFDYEKSRLIGPRKNVYKG
TDVRITEAPHMYKRNGWYYILIAEGGTGYSHACTLARSRDIWGPYKTHPDKHILTSKDTP
FAALQKAGHGDIVEALDGKVYLVHLTERKYTFEKGLPQDFQWLRTPKPDRLFSFRDDKLV
LHGRESIGSWYEHSLVARRQEHFSYEAETVIDFSPEDERQLAGLTAYYNRYCFFYLAVTT
DSDGQRELLIMTSEQSYPRSYLKEPFVDPVQIPNEGKVKLALAIHGGQQLQFFYALKGQD
LVKVGPIFDASIMSDECGGQDSLTGAFAGVACSDLNGLGKKAIFDYFIYRPIEHKYDRYE
IKS

Enzyme Prediction     

EC	3.2.1.37:21	3.2.1.55:3	3.2.1.-:1	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	4	271	2.2e-132	0.9143835616438356
CBM91	269	472	1.1e-42	0.97

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350114	GH43_SXA-like	0.0	6	268	1	263	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.
226038	XynB2	2.94e-158	5	471	22	548	Beta-xylosidase [Carbohydrate transport and metabolism].
350129	GH43_XynB-like	1.58e-112	6	270	1	260	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.
350103	GH43_XYL-like	1.02e-111	6	268	1	251	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.
398349	Glyco_hydro_43	8.60e-95	5	269	2	257	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
AEO58399.1|GH43_11	4.49e-266	1	481	1	537
AEO58399.1|CBM91|GH43_11	4.49e-266	1	481	1	537
UPL01618.1|CBM91|GH43_11	5.75e-262	1	481	1	537
CEI70293.1|GH43_11	9.47e-261	1	481	1	537
CEI70293.1|CBM91|GH43_11	9.47e-261	1	481	1	537

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1YRZ_A	7.27e-151	4	473	5	527	Chain A, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125],1YRZ_B Chain B, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125]
2EXH_A	6.82e-137	1	472	1	535	Structure of 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]
2EXK_A	7.73e-136	1	472	1	535	Chain A, beta-D-xylosidase [Geobacillus stearothermophilus],2EXK_B Chain B, beta-D-xylosidase [Geobacillus stearothermophilus],2EXK_C Chain C, beta-D-xylosidase [Geobacillus stearothermophilus],2EXK_D Chain D, beta-D-xylosidase [Geobacillus stearothermophilus]
2EXI_A	7.73e-136	1	472	1	535	Chain A, beta-D-xylosidase [Geobacillus stearothermophilus],2EXI_B Chain B, beta-D-xylosidase [Geobacillus stearothermophilus],2EXI_C Chain C, beta-D-xylosidase [Geobacillus stearothermophilus],2EXI_D Chain D, beta-D-xylosidase [Geobacillus stearothermophilus]
2EXJ_A	7.73e-136	1	472	1	535	Chain A, beta-D-xylosidase [Geobacillus stearothermophilus],2EXJ_B Chain B, beta-D-xylosidase [Geobacillus stearothermophilus],2EXJ_C Chain C, beta-D-xylosidase [Geobacillus stearothermophilus],2EXJ_D Chain D, beta-D-xylosidase [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P07129|XYNB_BACPU	8.34e-129	4	469	3	530	Beta-xylosidase OS=Bacillus pumilus OX=1408 GN=xynB PE=1 SV=2
sp|P94489|XYNB_BACSU	4.43e-128	4	470	3	531	Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2
sp|P77713|YAGH_ECOLI	7.05e-122	4	472	3	536	Putative beta-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yagH PE=3 SV=1
sp|A9ZND1|XLOA_VIBSX	1.94e-115	3	474	4	535	Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
sp|A7LXT8|GH43A_BACO1	1.54e-64	6	475	25	526	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 OTHER

Other	SP_Sec_SPI	CS Position
1.000041	0.000008

TMHMM  Annotations     

There is no transmembrane helices in FPRO_16010-t41_1-p1.