INUB_ASPNG
ID INUB_ASPNG Reviewed; 516 AA.
AC O74642;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Extracellular endo-inulinase inuB;
DE EC=3.2.1.7;
DE Flags: Precursor;
GN Name=inuB;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=12;
RX PubMed=9805373; DOI=10.1271/bbb.62.1731;
RA Ohta K., Akimoto H., Matsuda S., Toshimitsu D., Nakamura T.;
RT "Molecular cloning and sequence analysis of two endoinulinase genes from
RT Aspergillus niger.";
RL Biosci. Biotechnol. Biochem. 62:1731-1738(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=12;
RX PubMed=16232670; DOI=10.1016/s1389-1723(00)87086-3;
RA Akimoto H., Kushima T., Nakamura T., Ohta K.;
RT "Transcriptional analysis of two endoinulinase genes inuA and inuB in
RT Aspergillus niger and nucleotide sequences of their promoter regions.";
RL J. Biosci. Bioeng. 88:599-604(1999).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=8481000; DOI=10.1128/aem.59.3.729-733.1993;
RA Ohta K., Hamada S., Nakamura T.;
RT "Production of high concentrations of ethanol from inulin by simultaneous
RT saccharification and fermentation using Aspergillus niger and Saccharomyces
RT cerevisiae.";
RL Appl. Environ. Microbiol. 59:729-733(1993).
CC -!- FUNCTION: Endo-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. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (2->1)-beta-D-fructosidic linkages in
CC inulin.; EC=3.2.1.7;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- BIOTECHNOLOGY: Plays an important role in biofuel production. Pure
CC nonhydrolyzed inulin can be directly converted to ethanol in a
CC simultaneous saccharification and fermentation process when combining
CC A.niger and S.cerevisiae. Endoinulinase can digest
CC fructooligosaccharides with high degree of polymerization (DP) values
CC (>20) into short molecules that may be readily hydrolyzed by
CC S.cerevisiae SUC2. Thus, introduction of an endoinulinase gene into
CC S.cerevisiae will improve its inulin utilization and ethanol
CC fermentation through collaboration between the heterologous
CC endoinulinase and the invertase SUC2. {ECO:0000269|PubMed:8481000}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; AB012772; BAA33798.1; -; Genomic_DNA.
DR PIR; JE0301; JE0301.
DR AlphaFoldDB; O74642; -.
DR SMR; O74642; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR CLAE; INU32B_ASPNG; -.
DR VEuPathDB; FungiDB:An11g03200; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1095959; -.
DR VEuPathDB; FungiDB:ATCC64974_89460; -.
DR VEuPathDB; FungiDB:M747DRAFT_330865; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051670; F:inulinase 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..516
FT /note="Extracellular endo-inulinase inuB"
FT /id="PRO_5000049218"
FT ACT_SITE 43
FT /evidence="ECO:0000250"
FT BINDING 40..43
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 175..176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 516 AA; 55805 MW; 0F5112A8AF3CA88D CRC64;
MLNPKVAYMV WMTCLGLTLP SQAQSNDYRP SYHFTPDQYW MNEPNGLIKI GSTWHLFFQH
NPTANVWGNI CWGHATSTDL MHWAYKPTAI ADENGVEAFT GTAYYDPNNT SGLGDSANPP
YLAWFTGYTT SSQTQDQRLA FSVDNGATWT KFQGNPIIST SQEAPHDITG GLESRDPKVF
FHRQSGNWIM VLAHGGQDKL SFWTSADTIH WTWQSDLKST SINGLSSDIT GWEVPDMFEL
PVEGTGETTW VVMMTPAEGS PAGGNGVLAI TGSFDGKTFT ADPVDASTMW LDNGRDFDGA
LSWVNVPASD GRRIIAAVMN SYGSNPPTTT WKGMLSFPRT LSLKKVGTQQ HFVQQPITEL
DTISTSMQTL ANQTITPGQT LLSSIRGTAL DVRVAFYPDA GSVLSLTVRK GASEQTVINY
TQSNATLSVD RTESGDISYD PAAGGVHTAK LEEDGTGLVS IRVLVDTCSV EVFGGQGEAV
ISDLIFPSDS SDGLALEVTG GNAVLQSVDV RSVSLE
