CAZyme Information: FPRO_12749-t41_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRO_12749-t41_1-p1
• CAZy Family: GH47
• CAZyme Description: related to acetylxylan esterase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1215		133608.28	5.3352

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FproliferatumET1	16509	1227346	366	16143

• Gene Location: location=FJOF01000013:353578-357544(-)

Full Sequence      

MQIKYRDLCWPLAAISLLLMSHTKAYESSDGIEPHGHGNAPDVVSWGPSWNESYPASEGD
EPNLGADRGLSSRADDFYLRVMPLGASITQGYLSTDNNGYRKWLRSQLRYKGWKVNMVGS
KQNGDMTDRDNEGWPGYVIDQVHNEFRKSMWMKPNLVLINAGTNDCNQKIDINGAGGRMK
ALVDDIYSNIPGVTIVLSTIVRSTNVTNDACASKVSKQIRQLVKTYRSQRIGLADINPVL
PTSMLQKDGIHPTDAGYKLFASVWWDAIRKIQADIQPPAKVSGIDDAVSEKSSECKKTAG
NSRAPTQSQRGSGHDDGIYRHYSHAQGVLKSLRLENGGDSASLIKDYPWHVFFANIVLNS
ANSPRSHALDDMIRIHHEEDGTNTYWYRQNQGGGKFAASKRFDVDMDCNDGPRYAFADFN
NDGLDDFFCLKSGSAVWVSINQGGNPPKFKSIGQVVGKHDGYEPTDVRITDIDGDGRADY
CLVEDNGAVICSRNGGTGDKYAWQGFKTAKGLRDTVFDKNPKSASSKSGVVFADLNGDFR
DEYMWVSDTGSVHTWNNMRGWGKGIVPEWRDAGLTHKGQAAKGIQNRIKFGRIYGSGRRD
YIYLRSDKTGIDMVVWENKGFGGTKRKADGNFYCDMRGTGSDDYVWIYFDGHAAELNANI
HNPPLWGNDLKIELKVPGPRVGIHLADWTGDGKCDVLVQNEATGALTLYENTYKTGSKSV
TFTNKGVVTPATCSQGWGVSPFDRGMKLADIDGDGRADVICLEPNGRITGWLNLKSGMEN
VGQVKFPEGRERADIRFADVENSGRADIIYLDKYTGAATVFKNLGRKSGTGSSFNWSNRG
VLYAPIDRGETMHFTNQGGLGRADLVHVLPFTNKAYTYFNECGASGGDDGPITDPGLPKY
STGGQDGGTDDGSEDGDGSGDDCSKPSFDGDSKVILSENFPDPSFVFDFESCTWYSFGSQ
DKGKLVQIAQYNKSKDTWELLNDDPLKDAGAWGQNLDIVAPDVQWNGKQWVMYYSAFTQD
DHDGKRCIGVAFSDSIRGPYTPRDEPLVCQLDKGGVIDPSSFYDPGSDTRWVVYKIDGNR
ICGKTSIMLQQVENDGFTLKNDPVEILSETDDEKLLETPSLVYEDGSYLLFYSSGCYTSD
KYSIKYATSGSISGPYDRGNDKVLGSIAGSIQSPGSASSNGNGHLLFAAWCDKDLTTRCL
YSLSYKFEDGQVTLS

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	939	1202	1.5e-80	0.9924528301886792
CE3	79	268	3.9e-59	0.9948453608247423

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350113	GH43_ABN-like	6.98e-94	935	1213	3	284	Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase. 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.
238871	XynB_like	2.76e-39	79	268	1	157	SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
350102	GH43_ABN	7.65e-25	941	1204	1	274	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.
398349	Glyco_hydro_43	5.26e-20	934	1178	4	239	Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
350128	GH43_ABN-like	1.39e-19	935	1184	3	250	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCT73237.1|CE3|GH43_30	0.0	1	1215	1	1215
AEO70515.1|CE3	5.51e-298	38	892	42	938
UDD56943.1|CE0	5.56e-193	69	905	45	869
EAA58486.1|CE0	5.48e-141	76	899	58	918
CCT65127.1|CE3	2.43e-135	70	900	40	907

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3KST_A	5.57e-07	990	1215	75	296	Crystal structure of Endo-1,4-beta-xylanase (NP_811807.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.70 A resolution [Bacteroides thetaiotaomicron VPI-5482],3KST_B Crystal structure of Endo-1,4-beta-xylanase (NP_811807.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.70 A resolution [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits     

FPRO_12749-t41_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000279	0.999705	CS pos: 25-26. Pr: 0.9773

TMHMM  Annotations     

There is no transmembrane helices in FPRO_12749-t41_1-p1.