ID A0A067EU47_CITSI Unreviewed; 975 AA.
AC A0A067EU47;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=CISIN_1g002027mg {ECO:0000313|EMBL:KDO57420.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO57420.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO57420.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) 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; KK784963; KDO57419.1; -; Genomic_DNA.
DR EMBL; KK784963; KDO57420.1; -; Genomic_DNA.
DR PaxDb; 2711-XP_006482017-1; -.
DR eggNOG; ENOG502QR3V; Eukaryota.
DR Proteomes; UP000027120; 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 CDD; cd05816; CBM20_DPE2_repeat2; 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; 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; 2.
DR Pfam; PF02446; Glyco_hydro_77; 1.
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:UP000027120}.
FT DOMAIN 17..126
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT DOMAIN 161..274
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 933..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 112671 MW; 6A618BDEE15C63BE CRC64;
MANMGLFSGT KSSKPLTMSV KSLTVKFRIP YYTHWGQSLL VCGSEPVLGS WDVKKGFLLS
PVHQDDELIW SGSIAVPIGF SCEYSYYVVD DRKNLLRWEM GKKRKLLLHE TIKDGEVVEL
HDLWQTGGDA LPFRSAFKNV IFRRSFSLDI ERSDGLIQNK LEQEDSVLVR FKICIPNIEE
DASVYVIGST SMLGQWKLQN GLKLSYAGES VWEADCVIQR GDFPIKYKYC KSGKTGNISL
ETGANRNLNV DFSNNQPRYI FLSDGMMREM PWRGAGVAVP MFSVRSEADL GVGEFLDLKL
LVDWAVESGF HLVQLLPIND TSVNRMWWDS YPYSSLSVFA LHPLYLRVQA LSEKMPEDIK
KEIEKAKVQL DKKDVDYEAT LATKLAIARK VFNQEKDLIL NSSAFQNFFS ENEDWLKPYA
AFCFLRDFFD TSDHSQWGRF SHYSKDKLAK LISEDSLHYD IIRFHYYVQF HLHIQLSEAA
EYARKKGVVL KGDLPIGVDR NSVDTWVYPN LFRMNTSTGA PPDYFDKNGQ NWGFPTYNWE
EMSKDNYAWW RARLTQMSKY FTAYRIDHIL GFFRIWELPE HAMTGLIGKF RPSIPLSQEE
LEREGIWDFD RLTRPYIRLE HLQEKFGSSW TYIAANFLSE FQKGRYEFTE DCNTEKKIAA
KLKTCAEKSM LLDSEDKTRR DLFDLIQNIV LIRDPEDSKK FYPRFNLEDT SSFMDLDDHS
KNVLKRLYYD YYFHRQENLW RENALKTLPA LLNSSDMMAC GEDLGLIPSC VHPVMEELGL
IGLRIQRMPS EPGLEFGIPS QYNYMTVCAP SCHDCSTLRA WWEEDEERRR RFFKNVVGSD
ALPPSQCLPD ITHFILRQHV ESPSMWAIFP LQDLLALKED YTTRPATEET INDPTNPRHY
WRYRVHVTLE SLQKDKELKT TVKDLVCASG RSCPPGGQEV ASNTRDKQQV ASSQEKNPIS
KPLSGVPQKG TVAVV
//