ID   A0A238XZ09_9ACTN        Unreviewed;       634 AA.
AC   A0A238XZ09;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, 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=SAMN06264365_10492 {ECO:0000313|EMBL:SNR63653.1};
OS   Actinoplanes regularis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=52697 {ECO:0000313|EMBL:SNR63653.1, ECO:0000313|Proteomes:UP000198415};
RN   [1] {ECO:0000313|EMBL:SNR63653.1, ECO:0000313|Proteomes:UP000198415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43151 {ECO:0000313|EMBL:SNR63653.1,
RC   ECO:0000313|Proteomes:UP000198415};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; FZNR01000004; SNR63653.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238XZ09; -.
DR   OrthoDB; 9800174at2; -.
DR   Proteomes; UP000198415; 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; cd11325; AmyAc_GTHase; 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:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   PIRSF; PIRSF000463; GlgB; 3.
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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198415};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          133..533
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        331
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        364
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   634 AA;  70055 MW;  99A02D193A33FD58 CRC64;
     MAASQEHITA GLPRGATLMD GGVAFRFWAP AAQHVYVALD GAVSYLPDPG DELVKDPATG
     DWTGFFPGAG AGTKYRFHVI GPGGAGFKRD PRARELELYG YPECDALVLD DDAYPWHDQD
     WTPPDFADLI VYQFHVGVFP ATDANGRDRR AHRTAKLLDA AQRVPYLAGL GVTAVQPLPV
     VEFQGEWSLG YNGTDLFSPE MDYCVDPHAL APYLDAINDL LAAKGAGPLK FEQLAGQANQ
     LKAFVDICHL HGLAVIFDVV YNHAGGGLDP ESLDYIDLPA DPGPYNNAYF SSEGWAGGRV
     FAFDREPVRE FLTANALMFL NDYHADGLRF DEVSVIDAKG GWAFCQELTR TLRTAKPQAV
     QIAEYWGEFP RLAVQPPPTG MGFDIAYSDH LRNAVRAVLA DRGAGIARLA DGLRFQLESW
     RSYHCLENHD VVLDMDDHRS PRIARLADGS NPRSWYARSR SRVATGLLLT APGVPMLFMG
     QEFLEDKLWS DSPGHTDHLI WWDGALGADR HMADFLRCTR DLIRLRRSLP ALRADGLAVL
     AADEQNRLLA FHRWVPGEGR DVVVVLTFSE STLYDYRLGF PRSGRWREVL NTDYFDHFPN
     PQVSGNSGSI EAANGSATLT VPANALLVFR HDDR
//