INUE_PICGU
ID INUE_PICGU Reviewed; 514 AA.
AC A5DHM6;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Extracellular exo-inulinase {ECO:0000303|PubMed:17111131};
DE EC=3.2.1.80 {ECO:0000269|PubMed:17111131, ECO:0000269|PubMed:19107534, ECO:0000269|Ref.3};
DE Flags: Precursor;
GN ORFNames=PGUG_02777;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=17111131; DOI=10.1007/s10295-006-0184-2;
RA Gong F., Sheng J., Chi Z., Li J.;
RT "Inulinase production by a marine yeast Pichia guilliermondii and inulin
RT hydrolysis by the crude inulinase.";
RL J. Ind. Microbiol. Biotechnol. 34:179-185(2007).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX DOI=10.1016/j.bej.2008.10.018;
RA Yu X., Guo N., Chi Z., Gong F., Sheng J., Chi Z.;
RT "Inulinase overproduction by a mutant of the marine yeast Pichia
RT guilliermondii using surface response methodology and inulin hydrolysis.";
RL Biochem. Eng. J. 43:266-271(2009).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19107534; DOI=10.1007/s10295-008-0519-2;
RA Guo N., Gong F., Chi Z., Sheng J., Li J.;
RT "Enhanced inulinase production in solid state fermentation by a mutant of
RT the marine yeast Pichia guilliermondii using surface response methodology
RT and inulin hydrolysis.";
RL J. Ind. Microbiol. Biotechnol. 36:499-507(2009).
CC -!- FUNCTION: Exo-inulinase involved in utilization of the plant storage
CC polymer inulin, consisting of fructooligosaccharides with a degree of
CC polymerization (DP) value from 2 to 60. Splits off terminal fructose
CC units successively from the non-reducing end of the inulin molecule.
CC {ECO:0000269|PubMed:17111131, ECO:0000269|PubMed:19107534,
CC ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked
CC beta-D-fructofuranose residues in fructans.; EC=3.2.1.80;
CC Evidence={ECO:0000269|PubMed:17111131, ECO:0000269|PubMed:19107534,
CC ECO:0000269|Ref.3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:17111131};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:17111131};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:17111131,
CC ECO:0000305|PubMed:19107534, ECO:0000305|Ref.3}.
CC -!- INDUCTION: Expression is up-regulated by inulin and maltose, and
CC repressed by glucose. Ammonium sulfate, ammonium chloride and urea are
CC inhibitory for inulinase synthesis, presumably because of the release
CC of ammonium ions. {ECO:0000269|PubMed:17111131}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; CH408157; EDK38679.2; -; Genomic_DNA.
DR RefSeq; XP_001485048.1; XM_001484998.1.
DR AlphaFoldDB; A5DHM6; -.
DR SMR; A5DHM6; -.
DR STRING; 4929.XP_001485048.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR CLAE; INX32A_PICGU; -.
DR EnsemblFungi; EDK38679; EDK38679; PGUG_02777.
DR GeneID; 5127324; -.
DR KEGG; pgu:PGUG_02777; -.
DR VEuPathDB; FungiDB:PGUG_02777; -.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_3_3_1; -.
DR InParanoid; A5DHM6; -.
DR OMA; GTEWRHA; -.
DR OrthoDB; 405663at2759; -.
DR BRENDA; 3.2.1.7; 1115.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051669; F:fructan beta-fructosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..514
FT /note="Extracellular exo-inulinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432723"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT ACT_SITE 214
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 33..34
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96TU3"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96TU3"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96TU3"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96TU3"
FT BINDING 162..163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96TU3"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96TU3"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96TU3"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 514 AA; 57859 MW; 28E3437BE2CCBA63 CRC64;
MRAFLALIFL TFVMNVESSR PLMAFTPSHG WMNDPNGQFY DSKNELWHLY YQYNPNDTVW
GTPLYWGHAT SKDLSTWKDY GATIGPDRDE DGIFSGNIVV DHNNTSGFFN DSIDPRQRVV
AIYTYNTEGS QTQHVAYSLD GGYTFEKYEH NPVLDVDNIN FRDPKVFWHE PTNQWIMVIA
LSQQFKIQIY GSIDLTNWSL HSNFTGGLFG FQYECPGLIE VPVEGTDESK WVMFIAINPG
SPLGGSSNQY FIGSFDGFEF VPDDSQARLM DYGKDFYAFQ TFDNAPKESG VVGLAWASNW
QYANLAPTKE WRSSMTLARQ MTLASRNMNP ETKVLSLLQK PIFGESVVAA NKISKRNITG
QDEQAVKIHK NSTGTFSFDI TFSVDSSKNQ TGQLQVISGQ NGESIRAGFD PTAGQFFVDR
GNTSGLKENP FFTDKTSAYV EPWKHQNDLP VYKMFGVIDG NLIEVFLNDG IATLTNTFFI
PGTEGLEYLE IESSSDAIHI VESEVKELKL RATS
