CAZyme Information: MGYG000003572_00078

Basic Information

• Species: Prevotella sp900770025
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900770025
• CAZyme ID: MGYG000003572_00078
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
947		104101.46	5.1752

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003572	2050564	MAG	Fiji	Oceania

• Gene Location: Start: 409; End: 3252 Strand: +

Full Sequence      

MKKTKRMMLVGMLLAGMVAGYTAQAQTTVTSEEAAAMYKAVSKKRISVHDPSVVYDNATG
RYYIFGSHKAGAYTTDMRNWTSANPTWAAATGGTASNAEAFVTPQVTKVKKGGVEVDFPA
FNAMEWSKRTDEAYDINGNMWAPDVVWNPTMNKWCYYLSVNGDKWHSSIILLTADKITGP
YRYQGPVVICGFDGGDHSYKDTDLELVLGTQTALPARYDVGDKWGNRWPHTIDPAVFYDE
EGKLWMVYGSWSGGIWMLELDETTGLRDYDVTYPSTAGSTDGVTSDPYYGTKVGGGYYVS
GEGPYIEHIGNYYYMFVSYGFFNPDGGYEMRVFRSDKPNGPYKDSRGVSAIFNGYVMNYG
TNGDKRGEKLLGAYNHWGAMGVGECAQGHNSIIAAPDDRTYLVYHTKFNNGTFFHEVRTH
QVFVNKEGWLVASPFEYNGEQITNTDIATKALFTAEEMAGGYQLLVHSYNMDYANRQECT
PRNIVLHADGTVTGDKTGTWTIDTEAAYITLKLGSNTYTGVAVPATMDGYDIPLVTFTAC
CTATGENIWGYKMDARYELAWQINHQRVPVSDGMAINRHVPLMDIYFGMPNVSVEWTSEQ
PEVVSPIGRYNPTSLQADLPLSLGVKVSTPGYCWQKSWQVTALSADNATPKCNWSGGMVA
HYGFDDALLGNSLNPSEQATTGKNGAGTLPQMVEEGEFRQGNVAHLYFGANGNESYVSIP
NALKGRTLEQGATLSFWVYRADDNLWDALFAFVSGNSRFYMTGNAYLGYNDGSASGVNNW
IDLNHPAAVKTWLIGGNDWHLVTLTVATDALHLYIDGREAGFYACNGMLNNAAVSSADAF
DYGLILSVLQSADELCLGKGSFWGSPDCFVDDVVLYARALSAEDVQGLEQMENRVFNFSS
LATGITAVHHTQPQHRAVYDLCGRKVSSAMPTTKGIYIVNGKKVAVK

Enzyme Prediction     

No EC number prediction in MGYG000003572_00078.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	47	430	1.3e-95	0.9967741935483871

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18832	GH43_GsAbnA-like	1.02e-146	48	425	1	332	Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1,5-L-arabinanase AbnA. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. It includes Geobacillus stearothermophilus T-6 NCIMB 40222 AbnA, Bacillus subtilis subsp. subtilis str. 168 (Abn2;YxiA;J3A;BSU39330) (Arb43B), and Thermotoga petrophila RKU-1 (AbnA;TpABN;Tpet_0637). 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 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 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.
cd08988	GH43_ABN	1.45e-63	49	423	1	276	Glycosyl hydrolase family 43. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. 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 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. 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.
cd08998	GH43_Arb43a-like	4.12e-47	48	419	1	274	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.
COG3507	XynB2	3.31e-39	44	500	34	395	Beta-xylosidase [Carbohydrate transport and metabolism].
cd08978	GH_F	1.72e-37	49	406	1	250	Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. 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 of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 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
AGB28616.1	2.10e-280	25	947	21	947
ADB43998.1	2.12e-209	40	568	12	552
ADE81768.1	2.44e-196	40	552	19	543
QVJ79600.1	3.44e-196	40	552	19	543
AGH13983.1	1.52e-142	77	554	1	497

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KCA_A	2.64e-202	44	552	121	637	CrystalStructure of Endo-1,5-alpha-L-arabinanase from a Bovine Ruminal Metagenomic Library [Bos taurus],4KCA_B Crystal Structure of Endo-1,5-alpha-L-arabinanase from a Bovine Ruminal Metagenomic Library [Bos taurus]
5HO0_A	1.19e-85	46	819	51	792	Crystalstructure of AbnA (closed conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HO2_A Crystal structure of AbnA (open conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HOF_A Crystal structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus],5HP6_A Structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus (a new conformational state) [Geobacillus stearothermophilus]
5HO9_A	8.96e-82	46	643	51	637	Structureof truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus],5HO9_B Structure of truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus]
2X8F_A	2.11e-60	44	552	32	469	Nativestructure of Endo-1,5-alpha-L-arabinanases from Bacillus subtilis [Bacillus subtilis],2X8F_B Native structure of Endo-1,5-alpha-L-arabinanases from Bacillus subtilis [Bacillus subtilis]
2X8S_A	1.39e-59	44	553	32	470	CrystalStructure of the Abn2 D171A mutant in complex with arabinotriose [Bacillus subtilis],2X8S_B Crystal Structure of the Abn2 D171A mutant in complex with arabinotriose [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P42293	1.13e-59	44	552	32	469	Extracellular endo-alpha-(1->5)-L-arabinanase 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=abn2 PE=1 SV=2
A5IKD4	2.21e-56	48	554	30	470	Extracellular endo-alpha-(1->5)-L-arabinanase OS=Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1) OX=390874 GN=Tpet_0637 PE=1 SV=1
P95470	6.30e-15	126	429	81	330	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
Q93HT9	2.24e-08	125	429	69	310	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1
B3EYM8	3.04e-08	121	429	12	310	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
0.001156	0.976505	0.021306	0.000467	0.000302	0.000254

TMHMM  Annotations     

start	end
7	29