ID   MGTA_THENE              Reviewed;         442 AA.
AC   O86956;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=4-alpha-glucanotransferase;
DE            EC=2.4.1.25;
DE   AltName: Full=Amylomaltase;
DE   AltName: Full=Disproportionating enzyme;
DE            Short=D-enzyme;
DE   AltName: Full=Maltodextrin glycosyltransferase;
GN   Name=mgtA;
OS   Thermotoga neapolitana.
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=2337;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=Z2706-MC24;
RA   Berezina O.V., Zverlov V.V., Lunina N.A., Chekanovskaya L.A.,
RA   Dubinina E.N., Liebl W., Velikodvorskaya G.A.;
RT   "Gene and properties of thermostable 4-alpha-glucanotransferase of
RT   Thermotoga neapolitana.";
RL   Mol. Biol. (Mosk.) 33:801-806(1999).
CC   -!- FUNCTION: Hydrolyzes the 1,4-alpha-glycoside bonds in oligomeric and
CC       polymeric 1,4-alpha-glucans and transfers oligosaccharides (maltotriose
CC       being the shortest one) to acceptor maltodextrins. {ECO:0000269|Ref.1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC         position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC         glucan.; EC=2.4.1.25; Evidence={ECO:0000269|Ref.1};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; AJ009831; CAA08864.1; -; Genomic_DNA.
DR   AlphaFoldDB; O86956; -.
DR   SMR; O86956; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR   GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.90.400.10; -; 1.
DR   InterPro; IPR015261; 4-alpha-glucanotransf_C.
DR   InterPro; IPR006046; Alpha_amylase.
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   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF09178; DUF1945; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Cytoplasm; Glycosyltransferase;
KW   Metal-binding; Transferase.
FT   CHAIN           1..442
FT                   /note="4-alpha-glucanotransferase"
FT                   /id="PRO_0000054337"
FT   ACT_SITE        186
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        216
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            278
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   442 AA;  51935 MW;  AD42748834568CC7 CRC64;
     MIGYQIYVRS FRDGNFDGVG DFKGLKGAIS YLKELGVDFV WLMPVFSSIS FHGYDVVDFY
     SFKAEYGDEK DFREMIEAFH DNGIKVVLDL PIHHTGFLHT WFQKALKGDP HYRDYYVWAS
     EKTDLDERRE WDNERIWHPL EDGRFYRGLF GPLSPDLNYD NPQVFEEMKK VVYHLLEMGV
     DGFRFDAAKH MRDTLEQNVR FWRYFLSDIE GIFLAEIWAE SKVVDEHGRI FGYMLNFDTS
     HCIKEAVWKE NFKVLIESIE RALVGKDYLP VNFTSNHDMS RLASFEGGLS EEKVKLSLSI
     LFTLPGVPLI FYGDELGMKG IYRKPNTEVV LDPFPWSENI SLEGQTFWKW PAYNSPFSGV
     SVEYQKKKRD SILLHIMKWT GFRKENHWLD RANIEFLCKE EKLLHVYRLV DEGRSLKVIH
     NLSNGEMVFE GVRVQPYSTE VI