CAZyme Information: P170DRAFT_351866-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_351866-t37_1-p1
• CAZy Family: AA7
• CAZyme Description: extracellular invertase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
618		67327.90	4.9130

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000002:5536911-5538826(+)

Full Sequence      

MKPTSAALLLLAGQAVDAIDYNAAPPNLSTLANGSLFETWRPRAHVLPVSGKTGDPCMKY
TDPKTGLFHVGWLHNDSGITGATTDDMVTYRDLNGGGPSIVPGGINDPLAVFDGSVIPRG
INGTPTLIYTSVSFLPIHWSIPYTRGAESQSLAVSYDGGRNFTKVNQGPVIPEAPFGVNV
TAFRDPYVFQNPQLDTLSDSSVGTWYTVVSGGVHDVGPSQFLYRQTDPDFQYWEYLGEWW
REGVNTTWGDGTWAGGWGFNFETGNIFGLNDEGYDPEGEVFNTLGTEGSNAPIKRELSSI
HDLLWTAGKISNNGSIKFTPTMAGVLDWGASAYAAAGKVLTADSQASKKSGAPARFVTYP
WLTGDEYGQAKLFPTRQQNWTGTLLLPRELHTLSIHNVVDNELARETGVSWRVQGKSKSG
TLELKTLGIDIARETYNALTRGSSTDESDRKLSNQSTPVPFAKSPENKFFVLRANLTFPQ
SARKSGLKSGFQILSSEFESTNIYYQFSNESIIIDRSNTSAAAQSTSGITTYNEAGRLRL
FDVVEDGAEKIESLELTIVVDNGVLEVFANGRFALSTWARSWYAKSTGIKFLHNGVGQVQ
FSDVSVSEGLFEAWPERQ

Enzyme Prediction     

EC	3.2.1.26:10	2.4.1.100:6	2.4.1.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	45	392	1.4e-38	0.9590443686006825

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350133	GH32_XdINV-like	7.19e-128	54	394	4	337	glycoside hydrolase family 32 protein such as Xanthophyllomyces dendrorhous beta-fructofuranosidase (Inv;Xd-INV;XdINV). This subfamily of glycosyl hydrolase family GH32 includes fructan:fructan 1-fructosyltransferase (FT, EC 2.4.1.100) and beta-fructofuranosidase (invertase or Inv, EC 3.2.1.26), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Xanthophyllomyces dendrorhous beta-fructofuranosidase (XdINV) also catalyzes the synthesis of fructooligosaccharides (FOS, a beneficial prebiotic), producing neo-FOS, making it an interesting biotechnology target. Structural studies show plasticity of its active site, having a flexible loop that is essential in binding sucrose and beta(2-1)-linked oligosaccharide, making it a valuable biocatalyst to produce novel bioconjugates. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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.
214757	Glyco_32	5.33e-42	45	571	1	436	Glycosyl hydrolases family 32.
350110	GH32_FFase	5.65e-41	66	390	14	279	Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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.
400517	Glyco_hydro_32C	2.21e-23	441	608	6	162	Glycosyl hydrolases family 32 C terminal. This domain corresponds to the C terminal domain of glycosyl hydrolase family 32. It forms a beta sandwich module.
395193	Glyco_hydro_32N	4.35e-20	82	390	43	295	Glycosyl hydrolases family 32 N-terminal domain. This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHC54391.1|GH32|2.4.1.100	1.18e-316	19	618	28	627
AAQ31828.1|GH32|3.2.1.26	5.59e-316	19	618	7	603
ABB59678.1|GH32|3.2.1.26	5.67e-315	19	618	28	627
BCS13398.1|GH32	2.18e-312	19	618	28	627
GAA88101.1|GH32|2.4.1.100	2.18e-312	19	618	28	627

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5XH8_A	3.22e-314	19	618	5	604	Aspergillus kawachii beta-fructofuranosidase complexed with glycerol [Aspergillus luchuensis IFO 4308],5XH9_A Aspergillus kawachii beta-fructofuranosidase [Aspergillus luchuensis IFO 4308],5XHA_A Aspergillus kawachii beta-fructofuranosidase complexed with fructose [Aspergillus luchuensis IFO 4308]
3LF7_A	4.37e-269	19	617	4	634	Crystal structure of fructosyltransferase (wild-type) from A. japonicus [Aspergillus japonicus],3LFI_A Crystal structure of fructosyltransferase (wild-type) from A. japonicus in complex with glucose [Aspergillus japonicus],3LFI_B Crystal structure of fructosyltransferase (wild-type) from A. japonicus in complex with glucose [Aspergillus japonicus]
3LDK_A	7.16e-268	19	617	4	634	Crystal Structure of A. japonicus CB05 [Aspergillus japonicus],3LDR_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with 1-Kestose [Aspergillus japonicus],3LEM_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with Nystose [Aspergillus japonicus],3LIG_A Crystal structure of fructosyltransferase (D191A) from A. japonicus [Aspergillus japonicus],3LIH_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with raffinose [Aspergillus japonicus]
5ANN_A	1.02e-78	18	617	43	641	Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5ANN_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma]
6S82_A	1.02e-78	18	617	43	641	Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S82_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O33833|BFRA_THEMA	1.25e-08	40	464	2	350	Beta-fructosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=bfrA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000271	0.999671	CS pos: 18-19. Pr: 0.9698

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_351866-t37_1-p1.