ID   M1E1F3_9HYPH            Unreviewed;       557 AA.
AC   M1E1F3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Sucrose isomerase {ECO:0000313|PDB:4GI6, ECO:0000313|PDB:4GI8};
GN   Name=mutB {ECO:0000313|PDB:4GI6, ECO:0000313|PDB:4GI8,
GN   ECO:0000313|PDB:4GI9, ECO:0000313|PDB:4GIA};
OS   Rhizobium sp. MX-45.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=1071045 {ECO:0000313|PDB:4GI8};
RN   [1] {ECO:0007829|PDB:4GI6, ECO:0007829|PDB:4GI8}
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH CALCIUM AND GLUCOSE.
RX   PubMed=23385465; DOI=10.1107/S0907444912045532;
RA   Lipski A., Watzlawick H., Ravaud S., Robert X., Rhimi M., Haser R.,
RA   Mattes R., Aghajari N.;
RT   "Mutations inducing an active-site aperture in Rhizobium sp. sucrose
RT   isomerase confer hydrolytic activity.";
RL   Acta Crystallogr. D 69:298-307(2013).
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DR   PDB; 4GI6; X-ray; 2.15 A; A/B=1-557.
DR   PDB; 4GI8; X-ray; 1.95 A; A/B=1-557.
DR   PDB; 4GI9; X-ray; 2.15 A; A/B=1-557.
DR   PDB; 4GIA; X-ray; 2.01 A; A/B=1-557.
DR   PDBsum; 4GI6; -.
DR   PDBsum; 4GI8; -.
DR   PDBsum; 4GI9; -.
DR   PDBsum; 4GIA; -.
DR   BRENDA; 5.4.99.11; 5351.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR022567; DUF3459.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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; PF11941; DUF3459; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4GI6, ECO:0007829|PDB:4GI8};
KW   Calcium {ECO:0007829|PDB:4GI6, ECO:0007829|PDB:4GI8};
KW   Metal-binding {ECO:0007829|PDB:4GI6, ECO:0007829|PDB:4GI8}.
FT   DOMAIN          14..418
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   BINDING         22
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:4GI6, ECO:0007829|PDB:4GI8"
FT   BINDING         24
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:4GI6, ECO:0007829|PDB:4GI8"
FT   BINDING         26
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:4GI6, ECO:0007829|PDB:4GI8"
FT   BINDING         28
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:4GI6, ECO:0007829|PDB:4GI8"
FT   BINDING         30
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:4GI6, ECO:0007829|PDB:4GI8"
FT   CARBOHYD        254
FT                   /note="Glucose"
FT                   /evidence="ECO:0007829|PDB:4GI6"
FT   CARBOHYD        284
FT                   /note="Glucose"
FT                   /evidence="ECO:0007829|PDB:4GI6"
SQ   SEQUENCE   557 AA;  63830 MW;  536AFD407111E3E4 CRC64;
     KPGAPWWKSA VFYQVYPRSF KDTNGDGIGD FKGLTEKLDY LKGLGIDAIW INPHYASPNT
     DNGYDISDYR EVMKEYGTME DFDRLMAELK KRGMRLMVDV VINHSSDQHE WFKSSRASKD
     NPYRDYYFWR DGKDGHEPNN YPSFFGGSAW EKDPVTGQYY LHYLGRQQPD LNWDTPKLRE
     ELYAMLRFWL DKGVSGMRFD TVATYSKTPG FPDLTPEQMK NFAEAYTQGP NLHRYLQEMH
     EKVFDHYDAV TAGEIFGAPL NQVPLFIDSR RKELDMAFTF DLIRYDRALD RWHTIPRTLA
     DFRQTIDKVD AIAGEYGWNT FFLGNHDNPR AVSHFGDDRP QWREASAKAL ATVTLTQRGT
     PFIFQGDELG MTNYPFKTLQ DFDDIEVKGF FQDYVETGKA TAEELLTNVA LTSRDNARTP
     FQWDDSANAG FTTGKPWLKV NPNYTEINAA REIGDPKSVY SFYRNLISIR HETPALSTGS
     YRDIDPSNAD VYAYTRSQDG ETYLVVVNFK AEPRSFTLPD GMHIAETLIE SSSPAAPAAG
     AASLELQPWQ SGIYKVK
//