CAZyme Information: MGYG000004006_02017

Basic Information

• Species: Alistipes sp000434235
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp000434235
• CAZyme ID: MGYG000004006_02017
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
654	MGYG000004006_9|CGC1	73856.53	5.6833

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004006	2755781	MAG	United Kingdom	Europe

• Gene Location: Start: 103736; End: 105700 Strand: -

Full Sequence      

MKRLYRSGVALFVLLAAQTAVTAQETRQTSGAETTYAASDERSGNPLFEGWYADPEGVVF
GDEYWIFPTWSAPYDEQTFLDAFSSKDLVRWTKHPRIVSTEEVRWIRRAMWAPAAIHANG
KYYLFFSGNDIQNNDETGGIGVAVADRPEGPYRDALGRPLIDRIVHGAQPIDQFVFRDDD
GEYYMYYGGWGHCNMVRLAPDLLSVIPFEDGETFKEITPENYVEGPFMLKRQGKYYFMWS
EGGWGGPDYSVAYAIADSPFGPFERVGKILQQDPEVATGAGHHSVIRIPGKDEWYIVYHR
RPLGETAANSRATCIDRLRFDAEGRILPVRMTHEGVGPRPADPQGAYRNPVVNYSLPDPT
VVRGDDGLFYLYATENIPNVPIHRSRDLVNWKFIGTAFDEATRPDFEPGGRVWAPDINRI
GDRYVMYYSMSRWGGEWTCGIGIAVADRPEGPFDDLGMLFRSNEIGVQNSIDPFYIEDDG
HKYLFWGSFRGIHAVELTDDGLAVAQGAQPQRIAGTAYEGTYIHKHGGYYYLFASTGSCC
EGMKSSYTTVVGRSKHLMGPYTDRAGRPMADNHHEVVIHGNYDFVGTGHNAELVTDDKGQ
TWILYHAVSRANPDGRVLMLDRVTWRKGWPEVRGAEPSHLAERPVWRHRERKQD

Enzyme Prediction     

No EC number prediction in MGYG000004006_02017.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	347	630	7.8e-112	0.9966555183946488
GH43	45	324	4.6e-108	0.9928571428571429

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18827	GH43_XlnD-like	0.0	53	329	1	277	Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); includes mostly xylanases. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have mostly been annotated as xylanases (endo-alpha-L-arabinanase, EC 3.2.1.8). It belongs to the GH43_bXyl-like 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_bXyl-like subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidases (EC 3.2.1.37) and xylanases, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). 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.
cd18616	GH43_ABN-like	7.35e-151	349	625	1	291	Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activity. 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 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. 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.
cd09004	GH43_bXyl-like	2.59e-109	53	329	1	266	Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675) and (BT3662;BT_3662); includes mostly xylanases. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. 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.
cd18828	GH43_BT3675-like	1.36e-80	53	329	1	283	Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675). This glycosyl hydrolase family 43 (GH43) subgroup includes the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the GH43_bXyl 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_bXyl subgroup also includes enzymes annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. 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.
cd08998	GH43_Arb43a-like	3.83e-74	358	625	3	277	Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. 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. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT41415.1	0.0	43	644	30	634
AAO78622.1	0.0	43	647	30	637
ALJ44297.1	0.0	43	647	30	637
QQA08353.1	0.0	43	647	30	637
QMW85896.1	0.0	43	647	30	637

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QZ4_A	5.67e-48	40	329	3	307	Crystalstructure of an Endo-1,4-beta-xylanase D (BT_3675) from Bacteroides thetaiotaomicron VPI-5482 at 1.74 A resolution [Bacteroides thetaiotaomicron],3QZ4_B Crystal structure of an Endo-1,4-beta-xylanase D (BT_3675) from Bacteroides thetaiotaomicron VPI-5482 at 1.74 A resolution [Bacteroides thetaiotaomicron]
5A8C_A	1.92e-39	46	336	30	324	ChainA, CARBOHYDRATE BINDING FAMILY 6 [Acetivibrio thermocellus],5A8D_A Chain A, CARBOHYDRATE BINDING FAMILY 6 [Acetivibrio thermocellus]
1GYD_B	2.56e-38	358	643	6	313	Structureof Cellvibrio cellulosa alpha-L-arabinanase [Cellvibrio japonicus]
1GYH_A	3.42e-37	358	643	9	316	Structureof D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus],1GYH_B Structure of D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus],1GYH_C Structure of D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus],1GYH_D Structure of D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus],1GYH_E Structure of D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus],1GYH_F Structure of D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus]
1GYE_B	5.99e-37	358	643	7	314	Structureof Cellvibrio cellulosa alpha-L-arabinanase complexed with Arabinohexaose [Cellvibrio japonicus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P95470	2.91e-37	358	643	38	345	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
P49943	6.70e-30	53	329	15	320	Xylosidase/arabinosidase OS=Bacteroides ovatus OX=28116 GN=xsa PE=2 SV=1
P48791	2.03e-29	53	330	13	319	Beta-xylosidase OS=Prevotella ruminicola OX=839 GN=xynB PE=3 SV=1
P94522	3.99e-27	353	630	39	321	Extracellular endo-alpha-(1->5)-L-arabinanase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abnA PE=1 SV=3
B3EYM8	8.53e-27	358	630	27	311	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000561	0.998410	0.000277	0.000265	0.000238	0.000216

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004006_02017.