CAZyme Information: QRD87510.1

Basic Information

• Species: Aspergillus flavus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus flavus
• CAZyme ID: QRD87510.1
• CAZy Family: GH2
• CAZyme Description: putative glycosyl hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
548	CP044619|CGC39	62733.19	6.1991

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AflavusNRRL3357_2020	13958	N/A	249	13709

• Gene Location: location=CP044619:1321941-1323704(-)

Full Sequence      

MYNNPIIPGFNPDPSIIRVKNDFFLVTSSFEYFPGAPIYHSTDLIRWTLIGHALTRRSQI
HIQTPEPGGGVWATTLRYHDGVYYIIAASFERYRPQDDDRVWPRGFYVKTENIWDSGSWS
DPVFFDQVGFDQDLFWDDDGTVYLSSTYRKLNRTPNANLKDFAIHIATIDLASGASTSEP
KLIRESTSGVSEGSHIFKRGKYYYLFTAEGGTESGHCEWVSRSETGPFGPWEVGPNNPLW
RNGINDEVQNTGHADLVEDAQGRWWAVLLGVRPVRKDGYWEESVFGNFAHSLLGLCCRTN
SIATVTIGRETFLIPVEWKDDWPIFNRGKKISLQSDTPHLYEYQHPVAWRDDFSSPELQL
GWYRKNTPMRTDYSLTERPNHLRLHGGPYNLSVPSCPTLFLRKQIHHYCTWETKLSFSPQ
SQHTEAGTVVWWNYFTYSSIGIRLSPTKEGARIVRFRPAEGEVIDRELRSAVSDVVFFIE
CGDQYRFGFKEVNGTSSETQWIGEVQNSTMTQSPPVGAPFTGMMLGLYAFGERQRCLLPA
EFGYAEFR

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	2	287	5.5e-146	0.9506578947368421
CBM91	349	547	9.6e-38	0.96

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350129	GH43_XynB-like	1.73e-143	4	325	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.
350154	GH43_PcXyl-like	3.22e-96	4	324	1	292	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.
350103	GH43_XYL-like	1.57e-83	4	319	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.
350114	GH43_SXA-like	2.56e-81	4	323	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.
226038	XynB2	1.19e-77	1	548	20	547	Beta-xylosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD87510.1|GH43_13	0.0	1	548	1	548
QRD87510.1|CBM91|GH43_13	0.0	1	548	1	548
QMW26389.1|GH43_13	0.0	1	548	1	526
QMW26389.1|CBM91|GH43_13	0.0	1	548	1	526
QMW38468.1|GH43_13	0.0	1	548	1	526

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z5D_A	1.23e-99	2	547	3	507	Crystal structure 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	7.94e-84	2	548	5	504	Bacteroides ovatus Xyloglucan PUL GH43B [Bacteroides ovatus],5JOZ_B Bacteroides ovatus Xyloglucan PUL GH43B [Bacteroides ovatus]
5JOW_A	1.08e-79	2	548	13	509	Bacteroides ovatus 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	2.48e-73	4	469	6	448	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]
1YRZ_A	1.12e-72	4	548	7	524	Chain A, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125],1YRZ_B Chain B, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A7LXU0|GH43B_BACO1	5.89e-83	2	548	27	526	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
sp|A7LXT8|GH43A_BACO1	7.19e-79	2	548	23	519	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
sp|A9ZND1|XLOA_VIBSX	2.74e-70	4	547	7	532	Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
sp|P94489|XYNB_BACSU	1.63e-65	4	442	5	422	Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2
sp|P77713|YAGH_ECOLI	2.73e-60	4	438	5	420	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	CS Position
1.000048	0.000001

TMHMM  Annotations     

There is no transmembrane helices in QRD87510.1.