ID   Q8KR84_9ENTR            Unreviewed;       598 AA.
AC   Q8KR84;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   03-MAY-2023, entry version 85.
DE   SubName: Full=Isomaltulose synthase {ECO:0000313|EMBL:AAK82938.1};
OS   Klebsiella sp. LX3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=167956 {ECO:0000313|EMBL:AAK82938.1};
RN   [1] {ECO:0000313|EMBL:AAK82938.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LX3 {ECO:0000313|EMBL:AAK82938.1};
RX   PubMed=12039719; DOI=10.1128/AEM.68.6.2676-2682.2002;
RA   Zhang D., Li X., Zhang L.H.;
RT   "Isomaltulose synthase from Klebsiella sp. strain LX3: gene cloning and
RT   characterization and engineering of thermostability.";
RL   Appl. Environ. Microbiol. 68:2676-2682(2002).
RN   [2] {ECO:0007829|PDB:1M53}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 29-598, AND ACTIVE SITE.
RX   PubMed=12819210; DOI=10.1074/jbc.M302616200;
RA   Zhang D., Li N., Lok S.M., Zhang L.H., Swaminathan K.;
RT   "Isomaltulose synthase (PalI) of Klebsiella sp. LX3. Crystal structure and
RT   implication of mechanism.";
RL   J. Biol. Chem. 278:35428-35434(2003).
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DR   EMBL; AY040843; AAK82938.1; -; Genomic_DNA.
DR   PDB; 1M53; X-ray; 2.20 A; A=29-598.
DR   PDBsum; 1M53; -.
DR   AlphaFoldDB; Q8KR84; -.
DR   SMR; Q8KR84; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   BRENDA; 5.4.99.11; 7198.
DR   EvolutionaryTrace; Q8KR84; -.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1M53}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..598
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004309317"
FT   DOMAIN          55..460
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        241
FT                   /note="EMO_00054 nucleophile,EMO_00058 nucleofuge"
FT                   /evidence="ECO:0007829|PDB:1M53"
FT   ACT_SITE        295
FT                   /note="EMO_00068 proton donor"
FT                   /evidence="ECO:0007829|PDB:1M53"
SQ   SEQUENCE   598 AA;  69930 MW;  9F1611F9D0DFE28E CRC64;
     MSFVTLRTGV AVALSSLIIS LACPAVSAAP SLNQDIHVQK ESEYPAWWKE AVFYQIYPRS
     FKDTNDDGIG DIRGIIEKLD YLKSLGIDAI WINPHYDSPN TDNGYDISNY RQIMKEYGTM
     EDFDSLVAEM KKRNMRLMID VVINHTSDQH PWFIQSKSDK NNPYRDYYFW RDGKDNQPPN
     NYPSFFGGSA WQKDAKSGQY YLHYFARQQP DLNWDNPKVR EDLYAMLRFW LDKGVSGMRF
     DTVATYSKIP GFPNLTPEQQ KNFAEQYTMG PNIHRYIQEM NRKVLSRYDV ATAGEIFGVP
     LDRSSQFFDR RRHELNMAFM FDLIRLDRDS NERWRHKSWS LSQFRQIISK MDVTVGKYGW
     NTFFLDNHDN PRAVSHFGDD RPQWREASAK ALATITLTQR ATPFIYQGSE LGMTNYPFRQ
     LNEFDDIEVK GFWQDYVQSG KVTATEFLDN VRLTSRDNSR TPFQWNDTLN AGFTRGKPWF
     HINPNYVEIN AEREETREDS VLNYYKKMIQ LRHHIPALVY GAYQDLNPQD NTVYAYTRTL
     GNERYLVVVN FKEYPVRYTL PANDAIEEVV IDTQQQAAAP HSTSLSLSPW QAGVYKLR
//