ID   A0A0E0ANW7_9ORYZ        Unreviewed;       953 AA.
AC   A0A0E0ANW7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
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};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM07G25390.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM07G25390.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM07G25390.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0E0ANW7; -.
DR   STRING; 40148.A0A0E0ANW7; -.
DR   EnsemblPlants; OGLUM07G25390.1; OGLUM07G25390.1; OGLUM07G25390.
DR   Gramene; OGLUM07G25390.1; OGLUM07G25390.1; OGLUM07G25390.
DR   eggNOG; ENOG502QR3V; Eukaryota.
DR   HOGENOM; CLU_014132_0_0_1; -.
DR   Proteomes; UP000026961; 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; cd05815; CBM20_DPE2_repeat1; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR034840; CBM20_DPE2_1.
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; 2.
DR   Pfam; PF02446; Glyco_hydro_77; 2.
DR   SMART; SM01065; CBM_2; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 2.
DR   PROSITE; PS51166; CBM20; 2.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961}.
FT   DOMAIN          7..115
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   DOMAIN          150..267
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   REGION          926..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   953 AA;  109672 MW;  6D32DF9E9F491FA5 CRC64;
     MANLSRKKSL NTVTLVFKLP YYTQWGQSLL IAGSEPALGS WNVKQGLSLS PVHQGNELIW
     SGRVSVATGF TCQYNYYVVD DNKNVLRSES GEKRKLVLPE GVQDGDVVEI RDWWQDASEA
     LFLRSAFKNV IFNGSENAKR ELKTTPLNKS LEPEDIVVQF IVSCPRLGAG STVVVTGSNP
     QLGRWQTQDG LKLNYVGDSI WKANCPLRKS EFPIKYPCAN EYSLTSNLHE SPWRGAGVAV
     PIFSIRSNED LGVGEFLDLK LLVDWAVNSG FHLVQLLPIN DTSVHGMWWD SYPYSSLSVF
     ALHPLYLRVQ ALSDAIPGDI KDEISQAKKQ LDKKDVDYEA SLASKLSIAR KIFKLEKDKV
     LNSSSFKQFL SENEEWLKPY AAFCFLRDFF ETSDHSQWGR FSQFSKEKLD KLVSEGTLHH
     DVICFHYYIQ YHLYMQLSEA AAYARKKKVI LKGDLPIGVD RNSVDTWVYP TLFRMNTATG
     APPDYFDKNG QNWGFPTYNW EEMSKDNYGW WRARLTQMAK YFTAYRIDHI LGFFRIWELP
     DHAATGLVGK FRPSIALSQE ELLSEGLWDF DRMSRPYILQ ETLEEKFGSF WTVIAANFLN
     EYKKQHYEFK EDCNTEKKII AKLKNSSEKS LWLEKEDSIR RGLFDLLQNI VLIRDPEDST
     KFYPRFNQED TSSFNDLDEH SKNILRRLYY DYYFARQENL WRQNALKTLP VLLNSSDMLA
     CGEDLGLIPA CVHPKYIIQV MQELGLIGLR IQRMPSEPNL EFGIPSQYSY MTMHTYLGCI
     WQTKNGLEKL FSLMFNFVSY FFQVCAPSCH DCSTLRAWWE EDGGRRSRFY QTVIGSDDEP
     PSRCTPEVAN FIVKQHFDAP SMWAIFPLQD LLALKDKYTT RPAKEETIND PTNPKHYWRF
     RLHVTLDSLL DDKDIQATIK ELVTSSGRSF PGKVDGAEES GEKLAKVQLN GKP
//