CAZyme Information: MGYG000000559_02148

Basic Information

• Species: Paraprevotella sp900546665
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella sp900546665
• CAZyme ID: MGYG000000559_02148
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
961		108205.64	4.8603

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000559	3371833	MAG	China	Asia

• Gene Location: Start: 39719; End: 42604 Strand: +

Full Sequence      

MKKEMTTRFLHCFLGLSFIGGIVQAQNTSIQISDSEIEKMYTTETMNRTSVHDPSVVYDE
TSKQYYIFGSHIAVARTRDLQNWTWVNVPWGSINADGETVSGTPSVDAFHTNQTKEITVN
GQSIKFGNFDAAGWSCALGNGNDSDGSLTDWSVEGNMWAPDVIYNPVMKKWCQYLSLNGP
SWNSCIILLTADHIEGPYIYQGPVVYTGFRNNTDERISFHKTDLELVIGPQTSLPDRYNK
GNSWGSFWPHAIDPCVFYDEAGKLWIAYGSWSGGIFMLQLDEQTGLRDYNVTYDSDYDSL
HERLTSDAYFGKKIAGGYYVSGEGPYIEHIGRYYYLFMSYGEYAPDGGYEMRIFRSENPD
GPYKDINNIDARYSQYALNYGMNADNRGEKLMGYYNKWGFMNVGECSQGHNSAIVAPDGN
TYLVYHTKFNDGTVGHQVRVHQLFVNSKDWLVAAPFEYQGEKISNEQISGEELFSKAEIA
GNYKVLIHPYGMNHRQFQESVPSSITLLEDGSIQGAYTGKWSLTEGTSYLTLTLNNQKYE
GVVIEQHMEPTTIKALCFTACSQSGVNVWGYKMEEPYAIAYAVNSLHLPFNNNQVVSKHL
PLYETEVPEGIHMQWTSSEPEVISNTGMYNPQGLTEELPVELSLKLSCGQYYWTKTYQVT
AKRETAPTGDYLTGLKAYYSFDQQPVINAYNTSQKAIFRKEGNNQIPALLEDSSRVGNVL
HQYFGASGNCSYTQMSNSLKDVTEEGATIAMWIKRTDNVPWDAVWSFYNPAANTRLYFTG
NAYFGFNDGQNWLDINHPSSVTSDLIPVGKWTHVAVTVSKESGVTIYIDGIRMRSMTYAG
VSHGSEITSQVGFDYALLVDFIRNCPQFYLGYGSFWGSVDVKVDDVMLYNRALPASDIRA
LNTMCNRLTDFTVGEGGTSIEQVETEPETDTSDRIYDLSGKRTDRPQKGIYIMDGKKKII
R

Enzyme Prediction     

No EC number prediction in MGYG000000559_02148.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	50	451	3.5e-99	0.9967741935483871

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18832	GH43_GsAbnA-like	2.64e-143	51	446	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	1.65e-62	52	444	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	3.21e-45	51	444	1	276	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	1.65e-38	48	521	35	395	Beta-xylosidase [Carbohydrate transport and metabolism].
cd08978	GH_F	6.80e-31	52	427	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	7.20e-301	31	961	24	947
ADB43998.1	9.73e-191	46	584	15	548
ADE81768.1	1.82e-181	45	584	21	555
QVJ79600.1	4.05e-180	45	584	21	555
QNT66897.1	5.15e-160	32	705	23	721

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KCA_A	1.11e-192	46	579	120	644	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	2.30e-87	50	852	52	813	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	2.30e-84	50	660	52	635	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]
3LV4_A	1.45e-66	47	575	9	445	Crystalstructure of the glycoside hydrolase, family 43 YxiA protein from Bacillus licheniformis. Northeast Structural Genomics Consortium Target BiR14. [Bacillus licheniformis DSM 13 = ATCC 14580],3LV4_B Crystal structure of the glycoside hydrolase, family 43 YxiA protein from Bacillus licheniformis. Northeast Structural Genomics Consortium Target BiR14. [Bacillus licheniformis DSM 13 = ATCC 14580]
4KC7_A	2.92e-65	51	575	33	474	CrystalStructure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC7_B Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC7_C Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC8_A Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1],4KC8_B Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1],4KC8_C Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A5IKD4	1.49e-64	51	575	30	471	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
P42293	5.86e-62	50	572	35	469	Extracellular endo-alpha-(1->5)-L-arabinanase 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=abn2 PE=1 SV=2
P95470	6.97e-11	152	450	88	330	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
Q93HT9	2.28e-08	150	369	16	249	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1
B3EYM8	2.32e-08	150	369	16	249	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
0.010045	0.981148	0.007851	0.000405	0.000265	0.000254

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000559_02148.