ID   M7W9X8_ENTHI            Unreviewed;       898 AA.
AC   M7W9X8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00012560};
DE            EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560};
DE   AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423};
DE   AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501};
GN   ORFNames=KM1_073010 {ECO:0000313|EMBL:EMS14681.1};
OS   Entamoeba histolytica HM-3:IMSS.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=885315 {ECO:0000313|EMBL:EMS14681.1, ECO:0000313|Proteomes:UP000030780};
RN   [1] {ECO:0000313|EMBL:EMS14681.1, ECO:0000313|Proteomes:UP000030780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM-3:IMSS {ECO:0000313|EMBL:EMS14681.1,
RC   ECO:0000313|Proteomes:UP000030780};
RA   Inman J., Zafar N., Lorenzi H., Caler E.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000439};
CC   -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC       {ECO:0000256|ARBA:ARBA00005684}.
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DR   EMBL; KB637895; EMS14681.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7W9X8; -.
DR   EnsemblProtists; EMS14681; EMS14681; KM1_073010.
DR   VEuPathDB; AmoebaDB:KM1_073010; -.
DR   Proteomes; UP000030780; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05816; CBM20_DPE2_repeat2; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR034841; CBM20_DPE2_2.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR32518; -; 1.
DR   PANTHER; PTHR32518:SF3; 4-ALPHA-GLUCANOTRANSFERASE; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF02446; Glyco_hydro_77; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 2.
DR   PROSITE; PS51166; CBM20; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Transferase {ECO:0000313|EMBL:EMS14681.1}.
FT   DOMAIN          126..234
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   898 AA;  103473 MW;  238ACFE527A050FB CRC64;
     MVFITIHYST PFGQAVCLEV SGEKKVYKLN YVDNNTWSGE VKFKSTGLIN YRYLITKEDD
     LTEIFRTEGS KESYPHSLDL TNLKSFDKVE VNDIFISGFD AEDTFLTTSY FRKVIYGKRP
     QEKLEIKKLG KTTLLLKVRC TCVPEGQCVF VGGAIESLGK WDVSKAIKMT PTHVPYYEAL
     IDISNETTSF EYKCFIADAN SRANARWEDR SNRVYYIAPV AEEETEEKTK PVDTLIVKED
     NDFSGLYYRG AAVVTPVFSL RTKASCGCGE FLDLKKVVDW CNITGLSLIQ TLPVNDTTVY
     FTWRDSYPYN PNSVQALHPM YLRLSSLTQD PEILAEINSV AQKLNALEQI DYEAVLKEKE
     TITRKIFSKV GTTQKGFDEF KKSAGKWLIP YCVYRALIKS VDTPLPPTPK DFAEVEAMYA
     ANKAECDYYA FVQYNLHLQL KEASDYAADH KVALKGDLPI GVSKRSVECW MYPNLFHLDK
     STGAPPDYFS AGEGQNWGFP TYNWDNMAKD DYAWWKGRLS QMSQYFNAYR IDHILGFFRI
     WAIPAIHRTG LLGRFSPDLP FSRQELEGYG IYDTDRLSYP YIRDHTLDSL FGDEKNFVIS
     KFLVNNYNGT YNLKPEFQSE GAILEKTGLS PQFRESDKKI VNGLKLLLQN VCLIRDEQNP
     NLFVPRIDME KTYSSFNELD HWVQEGLKRL YNDYFYKRHE GLWEATARKR LPAMARASNM
     LVCGEDLGMV PDCVVRVMND MKINCLRIQR LTDTPNTLFY HPADYQYLTV SAPSGHDMST
     IRGWWEEDRY KTQYFWEHLL GRSGAAPFTC PVDAVKTIFD MHLYGPAMLA CFPLQDILSL
     KLKYIEGRDP KLEQINDPSN PIHYWRYRCH VDMDEIIADN DLNNELRTAV EKSGRHLF
//