ID   INU2_ARTGO              Reviewed;         393 AA.
AC   P19870;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Inulin fructotransferase [DFA-I-forming];
DE            EC=4.2.2.17;
DE   AltName: Full=Inulin fructotransferase [depolymerizing, difructofuranose-1,2':2',1-dianhydride-forming];
OS   Arthrobacter globiformis.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21 AND
RP   341-265.
RC   STRAIN=S14-3;
RX   PubMed=8534968; DOI=10.1271/bbb.59.1809;
RA   Haraguchi K., Seki K., Kishimoto M., Nagata T., Kasumi T., Kainuma K.,
RA   Kobayashi S.;
RT   "Cloning and nucleotide sequence of the inulin fructotransferase (DFA I-
RT   producing) gene of Arthrobacter globiformis S14-3.";
RL   Biosci. Biotechnol. Biochem. 59:1809-1812(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=S14-3;
RA   Seki K., Haraguchi K., Kishimoto M., Kobayashi S., Kainuma K.;
RT   "Purification and properties of a novel inulin fructotransferase (DFA I-
RT   producing) from Arthrobacter globiformis S14-3.";
RL   Agric. Biol. Chem. 53:2089-2094(1989).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Produces alpha-D-fructofuranose beta-D-fructofuranose
CC         1,2':2,1'-dianhydride (DFA I) by successively eliminating the
CC         diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-
CC         fructosyl-D-fructosyl disaccharide.; EC=4.2.2.17;
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DR   EMBL; D38528; BAA07533.1; -; Genomic_DNA.
DR   PIR; JC4318; JC4318.
DR   AlphaFoldDB; P19870; -.
DR   SMR; P19870; -.
DR   CAZy; GH91; Glycoside Hydrolase Family 91.
DR   KEGG; ag:BAA07533; -.
DR   BioCyc; MetaCyc:MON-21803; -.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0033997; F:inulin fructotransferase (DFA-I-forming) activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR040526; Beta_helix_2.
DR   InterPro; IPR007742; NosD_dom.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF18835; Beta_helix_2; 1.
DR   Pfam; PF05048; NosD; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosyltransferase; Lyase; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8534968, ECO:0000269|Ref.2"
FT   CHAIN           2..393
FT                   /note="Inulin fructotransferase [DFA-I-forming]"
FT                   /id="PRO_0000084209"
SQ   SEQUENCE   393 AA;  41683 MW;  2F1F15373734BEA9 CRC64;
     MANTVYDVTT WSGATISPYV DIGAVINQII ADIKANQTSQ AARPGAVIYI PPGHYDLLTR
     VVVDVSFLQI KGSGHGFLSE AIRDESSTGS WVETQPGASH IRVKNTDGNR EAFLVSRSGD
     PNVVGRLNSI EFKGFCLDGV TDSKPYSPGN SKIGISVQSD NDSFHVEGMG FVYLEHAIIV
     KGADAPNITN NFIAECGSCI ELTGASQVAK ITNNFLISAW AGYSIYAENA EGPLITGNSL
     LWAANITLSD CNRVSISSNK LLSNFPSMVA LLGNCSENLI AANHFRRVSG DGTSTRFDDL
     FGLVHIEGNN NTVTGNMFSF NVPASSISPS GATPTIILVK SGDSNYLATN NIVSNVSAMV
     VLDGSTTATR IIYSAKNSQL NAYTTSYTLV PTP