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Entry: A0A2K3NV42_TRIPR
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ID   A0A2K3NV42_TRIPR        Unreviewed;       832 AA.
AC   A0A2K3NV42;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE            EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN   ORFNames=L195_g003398 {ECO:0000313|EMBL:PNY06916.1};
OS   Trifolium pratense (Red clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=57577 {ECO:0000313|EMBL:PNY06916.1, ECO:0000313|Proteomes:UP000236291};
RN   [1] {ECO:0000313|EMBL:PNY06916.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNY06916.1};
RX   PubMed=24500806; DOI=10.3732/ajb.1300340;
RA   Istvanek J., Jaros M., Krenek A., Repkova J.;
RT   "Genome assembly and annotation for red clover (Trifolium pratense;
RT   Fabaceae).";
RL   Am. J. Bot. 101:327-337(2014).
RN   [2] {ECO:0000313|EMBL:PNY06916.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNY06916.1};
RX   PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA   Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT   "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT   (Trifolium pratense) Breeding.";
RL   Front. Plant Sci. 8:367-367(2017).
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   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004727}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC       {ECO:0000256|ARBA:ARBA00004602}.
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:PNY06916.1}.
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DR   EMBL; ASHM01001576; PNY06916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3NV42; -.
DR   STRING; 57577.A0A2K3NV42; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000236291; Unassembled WGS sequence.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
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   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
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:SF2; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME, CHLOROPLASTIC_AMYLOPLASTIC; 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   Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW   Plastid {ECO:0000256|ARBA:ARBA00023234};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236291};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          286..646
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        427
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        482
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   832 AA;  94882 MW;  F8BD7B3D0C61A038 CRC64;
     MISSLAFNPL ISSSLNIATI ATTHSSRNKQ NLVKQKTVEL TLGYQQNPNG NKVFSFGLKG
     SIYEKVSSGF KSIAVMTDDK STMPSSVEED SENIGILNAD SSLEPYKDHF KYRLKRYLHQ
     KKLIEEYEGS LEEFAKGYLK FGFNREEDGT LYREWAPAAQ EAQIIGDFNG WDGSNHHMKK
     DQFGVWSIKI PDSGGNPAIP HNSRVKFRFK HSDGVWVDRI PAWIKYATVD PARFAAPYDG
     VYWDPPHSER YQFKYPRPPK PKAPRIYEAH VGMSSSEPRI NSYREFADDI LPRIRENNYN
     TVQLMAVMEH SYYASFGYHV TNFFAVSSRS GTPEDLKYLI DKAHSLGLHV LMDVVHSHAS
     NNVTDGLNGF DVGQSSQESY FHTGDRGYHK LWDSRLFNYA NWEVLRFLLS NLRWWLEEYK
     FDGFRFDGVT SMLYHHHGIN MAFTGNYKEY FSEETDVDAV VYLMLANCLV HGILPESTVI
     AEDVSGMPGL GRPVSEVGIG FDYRLAMAIP DKWIDYVKNK KDNEWSMKEI SLNLTNRRYT
     EKCVAYAESH DQSIVGDKTI AFLLMDEEMY SSMSCLTDAS PTIERGIALH KMIHFITMAL
     GGEGYLNFMG NEFGHPEWID FPREGNGWSY EKCRRQWNLA DTDHLRYKFM NAFDKAMNLL
     DDRFSFLAST KQIVSSTNNE DKVIVFERGD LVFVFNFHPE NTYEGYKVGC DLPGKYRVAL
     DSDAREFGGH GRVGHDADHF TSPEGIPGVP ETNFNNRPNS FKILSPPRTC VVYYRVDESQ
     EENKSANLGQ VEETVAAADT DVNIPVDSVE SEDSNFLDRM EENKGGVVVT CY
//
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