CAZyme Information: FPRN_12187-t42_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRN_12187-t42_1-p1
• CAZy Family: GH5
• CAZyme Description: related to acetylxylan esterase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1269		139561.15	5.1974

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FproliferatumNRRL62905	15602	N/A	348	15254

• Gene Location: location=FCQG01000010:162948-167239(-)

Full Sequence      

MQIKYRGLCWPLAAVSLLLMSHTKAYESSDGIEPHGHGNAPDVVSWGPSWNESYPASEGD
EPSLGADRGLSSRADDFYLRVMPLGASITQGYLSTDNNGYRKWLRSQLRYKGWKVNMVGS
KQNGDMTDRDNEGWPGYVIDQVHNEFRKSMWMKPNLVLINAGTNDCNQKIDINGAGGRMK
ALVDDIYSNIPGVTIVLSTIVRSTNVTNDACASKVSKQIRQLVKTYRGQRIGLADINPVL
PTSMLQKDGIHPTDAVYKLFASVWWDAIRKIQADIQPPAKVSGIDDAVSEKSSECKKTAG
NSRAPQQSQRGSGHDDGIYRHYSHAHGVLKSLRLENGGDSASLIKDYPWHVFFANIVLNS
ANSPRSNALDDMIRIHHEKDGTNTYWYRQNQGGGKFAASKRFDVDMDCSDGPRYAFADFN
NDGLDDFFCLKSGSAVWVSINQGGNPPKFKSIGQVVGKHDGYEPTDVRITDIDGDGRADY
CLVEDNGAVICSRNGGTGDKYAWQGFKTAKGLRDTVFDKNPKSASSKSGVVFADLNGDFR
DEYMWIGDTGSVHTWNNMRGWGKGIVPEWRDAGLTHKGQAAKGIQNRIKFGRIYGSGRRD
YIYLRSDKTGIDMVVWENKGFGGTKRKADGNFYCDMRGTGSDDYVWIYFDGHAAELNANI
HNPPLWGNDLKIELKVPGPRVGIHLADWTGDGKCDVLVQNEATGALTLYENTYETGSKSV
TFTNKGVVTPATCSQGWGVSPFDRGMRLADIDGDGRADVLCLDTNGRITGWLNLKSGMEN
VGQVKFPEGQERADIRFADVENSGRADIIYLDKYTGAATVFKNLGRKSGTGSSFNWSNRG
VLYAPIDRGETMHFTNQGGLGRADLVHVLPFTNKAYTYFNECGASGGDDGPITDPGLPKY
STGGQDGGTDDGSEDGDGSGDDCSKPSFDGDSKVILSENFPDPSFVFDFESCTWYSFGSQ
DKGKLVQIARYNKSKDTWELLSDDPLKDAGSWGQNLDIVAPDVQWNGKQWVMYYSAFTQD
DHDGKRCVGVAFSDSIRGPYTPRDEPLVCQLDKGGVIDPSAFYDPGSDTRWVMYKIDGNR
ICGKTSIMLQQVENDGFTLKNDPVEILSETDDEKLLETPSLVYEDGSYLLFYSSGCYTSD
KYSIKYATSGSISGPYDRGDDKVLGSIAGSIQSPGSASSNGNGHLLFAAWCDKDLTTRCL
YSLSYKFEDGQVTLRYNEDAPPISLSRSSCEFFKSTTNMLFGIIAELVIYLCSVVDGHAF
ILSFGDLEF

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	939	1202	5.4e-80	0.9924528301886792
CE3	79	268	3e-57	0.9948453608247423

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350113	GH43_ABN-like	3.83e-93	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	9.72e-38	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	1.54e-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.
350105	GH43_HoAraf43-like	8.28e-20	941	1175	1	235	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.
398349	Glyco_hydro_43	1.53e-19	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCT73237.1|CE3|GH43_30	0.0	1	1214	1	1214
AEO70515.1|CE3	1.78e-290	38	892	42	938
UDD56943.1|CE0	5.85e-186	69	905	45	869
EAA58486.1|CE0	9.63e-134	76	899	58	918
UPK91538.1|CE0	1.27e-133	37	904	27	911

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3KST_A	4.32e-06	990	1214	75	295	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     

FPRN_12187-t42_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000259	0.999706	CS pos: 25-26. Pr: 0.9765

TMHMM  Annotations     

There is no transmembrane helices in FPRN_12187-t42_1-p1.