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Database: UniProt
Entry: A0A1C4MWK9_9ACTN
LinkDB: A0A1C4MWK9_9ACTN
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ID   A0A1C4MWK9_9ACTN        Unreviewed;       815 AA.
AC   A0A1C4MWK9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000256|HAMAP-Rule:MF_00685};
DE            EC=2.4.1.18 {ECO:0000256|HAMAP-Rule:MF_00685};
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000256|HAMAP-Rule:MF_00685};
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE   AltName: Full=Glycogen branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE            Short=BE {ECO:0000256|HAMAP-Rule:MF_00685};
GN   Name=glgB {ECO:0000256|HAMAP-Rule:MF_00685};
GN   ORFNames=GA0115251_12863 {ECO:0000313|EMBL:SCD90376.1};
OS   Streptomyces sp. TverLS-915.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839763 {ECO:0000313|EMBL:SCD90376.1, ECO:0000313|Proteomes:UP000198957};
RN   [1] {ECO:0000313|EMBL:SCD90376.1, ECO:0000313|Proteomes:UP000198957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TverLS-915 {ECO:0000313|EMBL:SCD90376.1,
RC   ECO:0000313|Proteomes:UP000198957};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages
CC       in glycogen by scission of a 1,4-alpha-linked oligosaccharide from
CC       growing alpha-1,4-glucan chains and the subsequent attachment of the
CC       oligosaccharide to the alpha-1,6 position. {ECO:0000256|HAMAP-
CC       Rule:MF_00685}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00685};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00685}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000256|ARBA:ARBA00009000, ECO:0000256|HAMAP-
CC       Rule:MF_00685}.
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DR   EMBL; FMCE01000264; SCD90376.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4MWK9; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000198957; Unassembled WGS sequence.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   CDD; cd11322; AmyAc_Glg_BE; 1.
DR   CDD; cd02855; E_set_GBE_prok_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; 2.
DR   HAMAP; MF_00685; GlgB; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR037439; Branching_enzy.
DR   InterPro; IPR006407; GlgB.
DR   InterPro; IPR044143; GlgB_N_E_set_prok.
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   NCBIfam; TIGR01515; branching_enzym; 1.
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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00685};
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW   Rule:MF_00685};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP-
KW   Rule:MF_00685};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00685}; Reference proteome {ECO:0000313|Proteomes:UP000198957};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          332..678
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        484
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        537
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   815 AA;  89067 MW;  164E684F37D204CF CRC64;
     MTPRSSSSSR PAKAAKAAKA ARHKPAAPAP QEPALQDPAP QGPAPQENAA APEPATLPRT
     APVPAPAHEP AAESLGEAAP ASPDAVGAGD RGRLLAGAHH DPHAVLGAHP AADGGGTVVR
     VLKPHARAVT VLLADDGRVP LGADGDGFFS GRLPAGTRPG APYRLLVAYG EDEGAALEDP
     YRFPPALGEM DLHLIGEGRH EELWTALGAR VMERDGVAGT RFTVWAPNAR GVRVIGNFNY
     WDGTGHPMRS LGGTGVWELF LPGLGAGELY KYEITTPEGH HVRKADPMAR RTEVPPATAS
     VVEESAYEWG DAEWLAHRGD RPVHEAPFSV YEVHLASWRP RLTYRELAEE LPAYVKDLGF
     THVELMPIAE HPFGGSWGYQ VTGFYAPTSR LGTPDDFRFL VDSLHRAGIG VLMDWVPAHF
     PRDEWALARF DGRPLYEHAD PQRASHPDWG TLVFDFGRTE VRNFLVANAT YWCEEFHIDG
     LRVDAVASML YLDYSREYGQ WSPNAYGGRE DLDAVRFLQE MNATVYRRNP GVVTVAEEST
     AWDGVTRPTD RSGPGGFGGL GFGLKWNMGW MHDSLEYLAK EPVHRKYHHN ELTFSMVYAY
     SENYVLPISH DEVVHGKGAL VSKIPGDWWQ RRATARAYLG FMWSHPGKQL LFMGQEFAQG
     SEWSEAHGPD WWLLDPAYEA SGDHRGVQHL VRDLNAVYTA TPPLWQRDTD PGGFAWVLGD
     AAEDNVLAYL RHDHEGTPFL AVCNFSPVVR PHYRVGAPEG RWTEALNTDA ARYGGGGVAA
     TPEGGATTGP IGAHGHAQSL ELTLPPLATV WLRRV
//
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