CAZyme Information: MGYG000002609_01050

Basic Information

• Species: CAG-882 sp003486385
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-882; CAG-882 sp003486385
• CAZyme ID: MGYG000002609_01050
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
555	MGYG000002609_8|CGC2	62352.97	4.457

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002609	3323522	MAG	China	Asia

• Gene Location: Start: 69508; End: 71175 Strand: +

Full Sequence      

MEYQLLCYTRKPDETMYYGPRLAYSMHIALREGDGKYIPLNHNSGVLFARATENADGSLN
PKSLKKPYIVRLADGSFEIHALRIEGDGQAEVNETELCFKSSDLVVYEEMSECDCTCTAQ
KPDEAGEAFDEALISGIVGCVPGNVISITEKEAQYLKNKLMTPEIVRLEVQDSVQVSGAE
DIGKIQATAYYSDGTSLNRSVDWNVGEIDFTKKGVAQKITGTVKQKRFAFPLLINRADPC
ITSWNGKYYFIATNDADNNHTIYIREADSIEGLESAEDVLLLDSSTYEDIGNLLWAPEFH
EINGRLYIFHAATPGEFFSEESHIMMLKDGGNPCNKDDWSRPKKIVKMDGSALCEAGKTI
SLDMTCFHWMGEYYVVWSQRQFLPKDLGAWLYIAKLNQERPWELASEPVLLSKPDYGWDN
NHTFVDEGPFALVSGDKLFVTFSGAAVDESYVVSYLELINNDSLLDRNSWRKNNYPILSA
RSVDGEYGTGHNAYVIDEDGIVWNTYHARPGADGPRSTGIRRVHFDVDGCPMLDVTEDRD
MTDELRKVETTIILV

Enzyme Prediction     

EC	3.2.1.55	3.2.1.37

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	236	531	7.7e-100	0.9966555183946488

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18818	GH43_GbtXyl43B-like	1.70e-153	237	509	1	273	Glycosyl hydrolase family 43 such as Geobacillus thermoleovorans IT-08 beta-xylosidase/exo-xylanase (GbtXyl43B). This glycosyl hydrolase family 43 (GH43) subgroup includes the characterized enzymes Geobacillus thermoleovorans IT-08 beta-xylosidase (EC 3.2.1.37) / exo-xylanase (GbtXyl43B), and Paenibacillus sp. strain E18 alpha-L-arabinofuranosidase (EC 3.2.1.55) Abf43B. 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.
cd08980	GH43_LbAraf43-like	5.56e-89	237	509	1	276	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.
cd18819	GH43_LbAraf43-like	7.87e-74	237	509	1	277	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.
COG3940	COG3940	1.59e-55	231	547	8	324	Beta-xylosidase, GH43 family [Carbohydrate transport and metabolism].
cd18817	GH43f_LbAraf43-like	1.21e-53	237	509	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
BCZ45323.1	6.26e-224	5	554	13	604
QUL57140.1	1.22e-223	4	554	11	603
AIQ29060.1	9.87e-223	4	548	11	597
AIQ40836.1	2.28e-221	4	554	11	603
VCV24055.1	1.18e-220	3	554	2	596

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3K1U_A	2.19e-47	231	537	12	318	Beta-xylosidase,family 43 glycosyl hydrolase from Clostridium acetobutylicum [Clostridium acetobutylicum]
5M8E_A	2.05e-41	227	532	24	334	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]
5M8B_A	9.95e-39	214	531	13	335	ChainA, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis],5M8B_B Chain B, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis]
3AKF_A	1.09e-35	228	531	11	310	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q82P90	7.17e-35	228	531	37	336	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
P82594	8.06e-35	231	509	53	319	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1
G4MMH2	4.32e-33	232	531	45	342	Alpha-L-arabinofuranosidase B OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=abfB PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000057	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002609_01050.