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Database: UniProt
Entry: A0A0V1HRW7_9BILA
LinkDB: A0A0V1HRW7_9BILA
Original site: A0A0V1HRW7_9BILA 
ID   A0A0V1HRW7_9BILA        Unreviewed;       687 AA.
AC   A0A0V1HRW7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-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};
DE   Flags: Fragment;
GN   Name=GBE1 {ECO:0000313|EMBL:KRZ13496.1};
GN   ORFNames=T11_7689 {ECO:0000313|EMBL:KRZ13496.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ13496.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ13496.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ13496.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KRZ13496.1}.
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DR   EMBL; JYDP01000032; KRZ13496.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1HRW7; -.
DR   STRING; 268475.A0A0V1HRW7; -.
DR   Proteomes; UP000055024; Unassembled WGS sequence.
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:UP000055024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          203..572
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        342
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        397
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ13496.1"
SQ   SEQUENCE   687 AA;  79517 MW;  8148C18DF8912D7B CRC64;
     LCACQIMSDR PPLLNNLLQL DGYLRNHESE ICRRYGEFKR LVMQINKEES GLDKFSRGYE
     KFGVVVTPEN GVFCQEWAPG ADGLFLIGDF NNWDRTAHPY DRKDFGKWEL YIPPNADGSC
     PIPHKSVLKI MVAKDGGFCD KISPWATYVC CPSDSIVYHH VFYNPPKKYK FLYNKPETPV
     ALRIYECHIG ISSSEGKVAS YVYFANNIIP RIAKQGYNAI QVMAVMEHAY YASFGYQVTN
     FFAASSRYGT PCDLKFLVDK AHELGIFVLL DIVHSHASKN TADGLNQWDG TNGCYFHDNY
     RGYHSVWDSR LFNYSERETL RFLLSNLRWW IEEYHFDGFR FDGVTSMIFH SHGLGQGFSG
     HYDEYFGLSV DTESLLYLTT ANYMLHKFYP SVVTIAEEVS GMPALCRPVE EGGQGFDYRL
     AMAIPDKWIK LLKDCRDEDW SMGDLVFTLE NRRYGEKNIA YAESHDQALV GDKTIAFWLM
     DKEMYTEMST LRPLNSIIDR GIALHKMIRL ITYGLGGEGW LNFMGNEFGH PEWLDFPRQG
     NNSSYHYCRR QWNLVDDPLL RYKFLNNWDR AMNMAEEKYH WLSAGPAYTS WKHDEDKVIA
     FERANLLFVF NFHVNKSYTD YKIGVNKSGK YKMILDSDAE EFGGHQRLDS SCEWFTFPYE
     YANRANHLCV YAPSRCCFVL ALDSDLS
//
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