ID   A0A0K9Y4T6_9FLAO        Unreviewed;       885 AA.
AC   A0A0K9Y4T6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295};
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=AC804_00935 {ECO:0000313|EMBL:KNB63195.1};
OS   Chryseobacterium sp. Hurlbut01.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1681828 {ECO:0000313|EMBL:KNB63195.1, ECO:0000313|Proteomes:UP000036769};
RN   [1] {ECO:0000313|Proteomes:UP000036769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hurlbut01 {ECO:0000313|Proteomes:UP000036769};
RA   Couger M.B., Youseff N., Elshahed M., French D., Hoff W.;
RT   "Draft Genome Sequence of the Environmental Isolate Chryseobacterium sp.
RT   Hurlbut 01.";
RL   Submitted (JUL-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNB63195.1}.
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DR   EMBL; LGIP01000001; KNB63195.1; -; Genomic_DNA.
DR   RefSeq; WP_050377182.1; NZ_LGIP01000001.1.
DR   AlphaFoldDB; A0A0K9Y4T6; -.
DR   PATRIC; fig|1681828.3.peg.198; -.
DR   Proteomes; UP000036769; 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   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
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; 1.
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:KNB63195.1}.
FT   DOMAIN          117..226
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   885 AA;  104765 MW;  93651BFD372AF77D CRC64;
     MKLYFNVGYH TKSGENLQLV IDENENGSKI HKMFYTEDGI WKCEVDYFSK SISYQYQLID
     DKKSVLRKEF VSHHLNFPHN YKEFLIFDEW NNKNFPENYL NNKVLYNKLN QFVPQKLTVL
     KKHSHLFRIE APVYNPDWEI VIFGNVSALG NWDYEKVVHL SQTDFGIWEV SVQIPENHLI
     EYKYAIFDKV QNRIIDVESG ENRSTKPNLT KDVLQISADH YFKFKSYQMY HAAGVAVPVF
     SLRSENDFGV GEFSDLKKLA DWAKETSLGV IQILPINDTT ANYSWTDSYP YAAVSVYALH
     PQYISLENLD FGLPKELVEE YNTEKTALNS LDLIDYEKMI SGKWKYLKAI FTIEKEKIYK
     DRNFKKFIKD NESWLLPYCA FCVLRDKYKT PNFNDWKTHK KYIAGKILPF FSAKSKDYEA
     SMLHAWVQFQ LHNQLKDSVD YIHSLGVSLK GDLPIGIYRH SVEAWTEPEL FGMDFQAGAP
     PDQFTELGQN WEFPTYNWEA MKADDYQWWK NRFKALEQYF DAMRIDHILG FFRIWRMPVS
     ATQGILGYFY PAVPIVSEEF SARHLPFDYE RYCKPYINDQ ILWDYFNEDS SKALNYINNN
     HNGTYSFKEE FDTQRKLTDY FKKNPSGNSR VEEQLISLCA NVLFLAENRE GKVVYHPRFN
     AFKTESYRYV SEWERKGIYD LYHDYFFKRQ DYLWREKAME KLPVILNSTK MLICGEDLGM
     VPDCVPEVMD DLAIIALKVQ RMPSEQIPFY DPKKAGYMNV VTASSHDSST LRQWWKENPQ
     LTQQYFNQQL MQYGRVPENL EPHLAEIIMK QHLYNDAMLA IFPLQEFLAT DEKLTNPMID
     NERINNPAVF PHYWRYRMHL NVENLMENTS FNQKISDWVN DSGRS
//