ID   A0A2Y9JQH2_ENHLU        Unreviewed;       699 AA.
AC   A0A2Y9JQH2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE            EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN   Name=LOC111148010 {ECO:0000313|RefSeq:XP_022360055.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022360055.1};
RN   [1] {ECO:0000313|RefSeq:XP_022360055.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022360055.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC         primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00000826};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR   RefSeq; XP_022360055.1; XM_022504347.1.
DR   AlphaFoldDB; A0A2Y9JQH2; -.
DR   STRING; 391180.A0A2Y9JQH2; -.
DR   KEGG; elk:111148010; -.
DR   OrthoDB; 96at2759; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR   CDD; cd11321; AmyAc_bac_euk_BE; 1.
DR   CDD; cd02854; E_set_GBE_euk_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR037439; Branching_enzy.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   PIRSF; PIRSF000463; GlgB; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          200..565
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        354
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        409
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   699 AA;  80348 MW;  18E99DBB5EF5C4CC CRC64;
     MAASEAPADS SEAALAAALA DVPELARLLD IDPYLKPFAG DFQRRYKRFN ETLNNIGENE
     GGIDKFSRGY ESFGVHRCAD GGLYCKEWAP GAEGVFLTGD FNDWNPFSYP YKKLDYGKWE
     LYIPPKKNKS LLVPHGSKLK VVIRSKSGEI LYRISPWAKY VTREGDNVNY DWIQWDPEHP
     YKFKHSKPKK PRGLRIYESH VGISSYEGKI ASYKHFTCNV LPRIKDLGYN CIQMMAIMEH
     AYYASFGYQI TSFFAASSRY GTPEELKELV DTAHSMGITV LLDVVHSHAS KNSEDGLNMF
     DGTDSCYFHS GPRGNHDLWD SRLFAYSNWE VLRFLLSNIR WWLEEYGFDG FRFDGVTSML
     YHHHGMGQGF SGDYHEYFGL QVDEDALIYL MLANHLIHTL YPDSVTVAED VSGMPALCSP
     ISQGGVGFDY RLAMAIPDKW IQLLKEYKDE DWNMGNIVYT LTNRRYLEKC IAYAESHDQA
     LVGDKTLAFW LMDAEMYTNM SVLTPFTPVI DRGIQLHKMI RLITHALGGE GYLNFMGNEF
     GHPEWLDFPR KGNNESYHYA RRQFHLTDDD LLRYKFLNNF DRDMNKLEER CGWLSAPQAY
     VSEKHEANKI IAFERAGLLF IFNFHPSKSY TDYRVGTTLP GKFKIVLDTD AAEYGGHQRL
     DHNTDFFSED FKHNERPCSL LVYIPSRVGL VLQNVDMPN
//