INUE_PICGM
ID INUE_PICGM Reviewed; 514 AA.
AC A8W7I5; A8W7I4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 3.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Extracellular exo-inulinase inuE;
DE EC=3.2.1.80;
DE Flags: Precursor;
OS Meyerozyma guilliermondii (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=4929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-223 AND PHE-432,
RP SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=1, and M-30;
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).
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|Ref.1}.
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|Ref.1};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; EU195800; ABW75766.2; -; Genomic_DNA.
DR EMBL; EU195799; ABW70125.2; -; Genomic_DNA.
DR AlphaFoldDB; A8W7I5; -.
DR SMR; A8W7I5; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR VEuPathDB; FungiDB:PGUG_02777; -.
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; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..514
FT /note="Extracellular exo-inulinase inuE"
FT /id="PRO_0000429669"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 214
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 33..34
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 162..163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 223
FT /note="A -> V (in strain: 1)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 432
FT /note="L -> F (in strain: 1)"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 514 AA; 57797 MW; 1DDFB74C32F90833 CRC64;
MRAFLALIFL TFVMNVESSR PLMAFTPSHG WMNDPNGQFY DSKNELWHLY YQYNPNDTVW
GTPLYWGHAT SKDLSTWKDY GATIGPDRDE DGIFSGNIVV DHNNTSGFFN DSIDPRQRVV
AIYTYNTEGS QTQHVAYSLD GGYTFEKYEH NPVLDVDNIN FRDPKVFWHE PTNQWIMVIA
LSQQFKIQIY GSIDLTNWSL HSNFTGGLFG FQYECPGLIE VPAEGTDESK WVMFIAINPG
SPLGGSSNQY FIGSFDGFEF VPDDSQARLM DYGKDFYAFQ TFDNAPKESG VVGLAWASNW
QYANLAPTKE WRSSMTLARQ MTLASRNMNP ETKVLSLLQK PIFGESVVAA NKISKRNITG
QDEQAVKIHK NSTGTFSFDI TFSVDSSKNQ TGQLQVISGQ NGESIRAGFD PTAGQFFVDR
GNTSGLKENP FLTDKTSAYV EPWKHQNDLP VYKMFGVIDG NLIEVFLNDG IATLTNTFFI
PGTEGLEYLE IESSSDAIHI VESEVKELKL RATS
