INUA_ASPNC
ID INUA_ASPNC Reviewed; 516 AA.
AC A5ABL2; Q0ZR34;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Extracellular endo-inulinase inuA;
DE EC=3.2.1.7;
DE Flags: Precursor;
GN Name=inuA; ORFNames=An11g03200;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17005986; DOI=10.1099/mic.0.29051-0;
RA Yuan X.L., Goosen C., Kools H., van der Maarel M.J.E.C.,
RA van den Hondel C.A.M.J.J., Dijkhuizen L., Ram A.F.J.;
RT "Database mining and transcriptional analysis of genes encoding inulin-
RT modifying enzymes of Aspergillus niger.";
RL Microbiology 152:3061-3073(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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).
RN [4]
RP INDUCTION.
RX PubMed=17917744; DOI=10.1007/s00438-007-0290-5;
RA Yuan X.L., Roubos J.A., van den Hondel C.A., Ram A.F.;
RT "Identification of InuR, a new Zn(II)2Cys6 transcriptional activator
RT involved in the regulation of inulinolytic genes in Aspergillus niger.";
RL Mol. Genet. Genomics 279:11-26(2008).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RX PubMed=23683966; DOI=10.1016/j.biortech.2013.04.076;
RA Yuan B., Wang S.A., Li F.L.;
RT "Improved ethanol fermentation by heterologous endoinulinase and inherent
RT invertase from inulin by Saccharomyces cerevisiae.";
RL Bioresour. Technol. 139:402-405(2013).
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:0000269|PubMed:23683966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (2->1)-beta-D-fructosidic linkages in
CC inulin.; EC=3.2.1.7; Evidence={ECO:0000269|PubMed:23683966};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Expression is induced in presence of sucrose or inulin and
CC controlled by the catabolite repressor creA and by the inulinolytic
CC genes regulator inuR. {ECO:0000269|PubMed:17005986,
CC ECO:0000269|PubMed:17917744}.
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:23683966,
CC ECO:0000269|PubMed:8481000}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- CAUTION: Strain CBS 513.88 / FGSC A1513 contains only one gene encoding
CC for an extracellular endo-inulinase (inuA), contrary to other strains
CC containing two genes (inuA and inuB). {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Driving on fumes - Issue 164
CC of September 2014;
CC URL="https://web.expasy.org/spotlight/back_issues/164/";
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DR EMBL; DQ233221; ABB59681.1; -; Genomic_DNA.
DR EMBL; AM270231; CAL00359.1; -; Genomic_DNA.
DR RefSeq; XP_001394322.1; XM_001394285.1.
DR AlphaFoldDB; A5ABL2; -.
DR SMR; A5ABL2; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; A5ABL2; -.
DR EnsemblFungi; CAL00359; CAL00359; An11g03200.
DR GeneID; 4984551; -.
DR KEGG; ang:ANI_1_1796094; -.
DR VEuPathDB; FungiDB:An11g03200; -.
DR HOGENOM; CLU_001528_3_1_1; -.
DR BRENDA; 3.2.1.7; 518.
DR Proteomes; UP000006706; Chromosome 7R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051670; F:inulinase activity; IDA:AspGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:AspGD.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..516
FT /note="Extracellular endo-inulinase inuA"
FT /id="PRO_5000713550"
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 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 516 AA; 55882 MW; 105BF12C6B9F96CF CRC64;
MLNPKVAYMV WMTCLGLTLP SQAQSNDYRP SYHFTPDQYW MNEPNGLIKI GSTWHLFFQH
NPTANVWGNI CWGHATSTDL MHWAHKPTAI ADENGVEAFT GTAYYDPNNA SGLGDSANPP
YLAWFTGYTV SSQTQDQRLA FSVDNGATWT KFQGNPIIST SQEAPHDITG GLESRDPKVF
FHRQSGNWIM VLAHGGQDKL SFWTSADTIN WTWQSDLKST SINGLSSDIT GWEVPDMFEL
PVEGTEETTW VVMMTPAEGS PAGGNGVLAI TGSFDGKSFT ADPVDASTMW LNNGRDFDGA
LSWVNVPASD GRRIIAAVMN SYGSNPPTTT WKGMLSFPRT LSLKKVGTQQ HFVQQPITEL
DTISTSLQTL ENQTITPGQT LLSSIRGTAL DVRVAFYPDA GSVLSLAVRK GASEQTVIKY
TQSDATLSVD RTESGDTSYD PAASGVHTAK LEEDDTGLVS IRVLVDTCSV EVFGGQGEAV
ISDLIFPSDS SDGLALEVTG GNAVLQSVDV RSVSLE
