CAZyme Information: MGYG000000221_00384

Basic Information

• Species: Parabacteroides bouchesdurhonensis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides bouchesdurhonensis
• CAZyme ID: MGYG000000221_00384
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
700		79095.57	4.6456

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000221	3481201	Isolate	China	Asia

• Gene Location: Start: 448781; End: 450883 Strand: -

Full Sequence      

MNIYKVIVLSVCALFISFSCIEKKVMQETTYYQNPIIENGADPWIIKKDDIYYYCASTKD
HTISVGKSALLHIPGDLKPVWKAPNAGWNSDCIWAPELHYLNGRWYIYYAAGESGPPFIH
QRAGVLESVTDDPQGEYIDKGMLYTGDSIGNWDSNRWAIDMTVFELNNKLYAVWSGWKNQ
ENTDHTSQMLYIAEMENPWTISSNRQLISMPDKPYEVGGDLDLNEGPEVLIHNGDVFIIY
SCCQSWLPTYKLASLRLTASDADPMNPDNWIKSEQPVFQGTDDVYGVGHASFTTSPDGTE
SYIVYHSKKDTIPGWNRDVRLQKFTWDTDGTPNFGVPHSLSESQPVPSGSKIKDKVTLTY
SNPLSVQFGDPYILLASDGRYYMYGTGAGAVDGFCVYSSDDLISWKSEGQVYHGNTPQSW
AVANFWAPEVYEKDGKFYMFFSADWRYNPTNEEENFRIGVAVADKPTGPFVELRDKPLFD
PGYPVIDGNILQDENGKCFLYYSRCCYKHPVESEIAEEAKRKGLFSEVEESWIYGVEISP
DFTQVIGEPVLLLRPPVSLTDKQSEWESRSVTSGEVNRRWTEGSFIFKHNGLYYMMYSAN
FFGGENYAVGYAVSESPLGPFKKADNNPVLEKNTAKGGIVTGTGHNSITWSKDRKQMYCV
YHGRTQKTGEERVVFIDKMHITPEGVLVVDGPTTDIQTIE

Enzyme Prediction     

No EC number prediction in MGYG000000221_00384.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	366	683	5.7e-142	0.9904761904761905
GH43	32	332	1.6e-99	0.9965986394557823

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18820	GH43_LbAraf43-like	1.10e-112	41	308	1	258	Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities, similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). 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.
cd08991	GH43_HoAraf43-like	7.57e-110	369	693	1	283	Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been 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.
cd08980	GH43_LbAraf43-like	2.09e-68	41	306	1	274	Glycosyl hydrolase family 43 proteins such as Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities. In addition to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) familiesGH43 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.
COG3940	COG3940	1.26e-67	32	337	5	313	Beta-xylosidase, GH43 family [Carbohydrate transport and metabolism].
cd18817	GH43f_LbAraf43-like	4.11e-64	41	308	1	262	Glycosyl hydrolase family 43 such as Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with alpha-L-arabinofuranosidase (EC 3.2.1.55) activity. 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. Characterized enzymes belonging to this subgroup include Lactobacillus brevis (LbAraf43) and Weissella sp (WAraf43) which show activity with similar catalytic efficiency on 1,5-alpha-L-arabinooligosaccharides with a degree of polymerization (DP) of 2-3; size is limited by an extended loop at the entrance to the active site. 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
QUT53433.1	3.45e-221	358	700	31	373
QUT22424.1	3.45e-221	358	700	31	373
QUT96106.1	3.45e-221	358	700	31	373
ABR43499.1	4.00e-221	358	700	35	377
AST52848.1	4.00e-221	358	700	35	377

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4QQS_A	9.73e-60	359	697	4	309	Crystalstructure of a thermostable family-43 glycoside hydrolase [Halothermothrix orenii H 168],4QQS_B Crystal structure of a thermostable family-43 glycoside hydrolase [Halothermothrix orenii H 168]
3K1U_A	5.34e-54	34	346	11	328	Beta-xylosidase,family 43 glycosyl hydrolase from Clostridium acetobutylicum [Clostridium acetobutylicum]
5M8B_A	5.42e-51	26	337	21	340	ChainA, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis],5M8B_B Chain B, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis]
3AKF_A	7.22e-51	32	337	11	315	Crystalstructure of exo-1,5-alpha-L-arabinofuranosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKG_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-1,5-L-arabinofuranobiose [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKH_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-1,5-L-arabinofuranotriose [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKI_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-L-arabinofuranosyl azido [Streptomyces avermitilis MA-4680 = NBRC 14893]
5M8E_A	6.84e-50	29	341	22	342	Crystalstructure of a GH43 arabonofuranosidase from Weissella sp. strain 142 [Weissella cibaria],5M8E_B Crystal structure of a GH43 arabonofuranosidase from Weissella sp. strain 142 [Weissella cibaria]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q82P90	5.18e-50	32	337	37	341	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=Araf43A PE=1 SV=1
G4MMH2	7.73e-43	32	337	41	347	Alpha-L-arabinofuranosidase B OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=abfB PE=1 SV=1
P82594	9.69e-35	32	309	50	320	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1
P49943	1.95e-18	396	621	54	259	Xylosidase/arabinosidase OS=Bacteroides ovatus OX=28116 GN=xsa PE=2 SV=1
P48791	1.44e-12	420	658	78	286	Beta-xylosidase OS=Prevotella ruminicola OX=839 GN=xynB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000003	0.000954	0.999094	0.000000	0.000001	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000221_00384.