ID A0A022R3B9_ERYGU Unreviewed; 844 AA.
AC A0A022R3B9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=MIMGU_mgv1a001301mg {ECO:0000313|EMBL:EYU35142.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU35142.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU35142.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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}.
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DR EMBL; KI630629; EYU35142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022R3B9; -.
DR STRING; 4155.A0A022R3B9; -.
DR eggNOG; KOG0470; Eukaryota.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
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 GO; GO:0005982; P:starch metabolic process; IBA:GO_Central.
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 Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Plastid {ECO:0000256|ARBA:ARBA00023234};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 335..695
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 478
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 533
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 844 AA; 95693 MW; 0DC51BE0A498B92C CRC64;
MVYTLPGVRL PTVPSAAYKV GSCGMIFSGG KAYESGFQPS MATAPEKVLV PGTESDGSSS
PRENLEIVSG TSQACNLESV DGPIVKEQEQ LIEQQISGEA IKGKDSASVQ LLDEDAGLNT
EGKSYSISKT IADESSMVKE RVIPPPGAGQ KIYEIDTLLT NYREHLDYRY GQYKKLRDAI
DKYEGGLEVF SRGYEKLGFN RSETGITYRE WAPGAKSASL IGDFNNWNAN ADVMTRNEFG
VWEIFLPNNA DGSPAIPHGS RVKIRMDTPS GIKDSIPAWI KFSVQAPGEI PYNGIYYDPP
VEERYVFKHP RPSKPKSLRI YECHVGMSST EPVINTYANF RDEVLPRIKK LGYNAVQIMA
IQEHSYYASF GYHVTNFFAP SSRFGTPDDL KSLIDKAHEL GLVVLMDIVH SHSSNNTLDG
LNMFDGTDSC YFHSGTRGYH WMWDSRLFNY GQWEVLRFLL SNARWWLDEY KFDGFRFDGV
TSMMYTHHGL QMAFTGNYSE YFGFATDVDA VAYLMLVNDL IHGLFPEAIT IGEDVSGMPA
FCIPLQDGGM GFDYRLHMAI ADKWIETLKK RDEEWSMGDI IHTLTNRRWR EKCVCYAESH
DQALVGDKTI AFWLMDKDMY DFMAVDRPST PLIDRGIALH KMIRLITMGL GGEGYLNFMG
NEFGHPEWID FPRGDQHLPD GRVIPGNGNS YDKCRRRFDL GDAEYLRYHG LQEFDQAMQH
LEENYGFMTS EHQYISRKDE ADRVIVFERG NLLFVFNFHW SKSYSDYRVG CLKPGKYKVA
LDSDDKLFGG FGRISHEAEY FTSEGWQDDR PRSFYIYAPS RTAVVYALAE VEAEPIDVQV
SPNV
//
