ID   GLGB_PSEA7              Reviewed;         732 AA.
AC   A6V628;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000255|HAMAP-Rule:MF_00685};
DE            EC=2.4.1.18 {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE            Short=BE {ECO:0000255|HAMAP-Rule:MF_00685};
GN   Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=PSPA7_3153;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) 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:0000255|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:0000255|HAMAP-Rule:MF_00685};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00685}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00685}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00685}.
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DR   EMBL; CP000744; ABR83355.1; -; Genomic_DNA.
DR   RefSeq; WP_012075912.1; NC_009656.1.
DR   AlphaFoldDB; A6V628; -.
DR   SMR; A6V628; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABR83355; ABR83355; PSPA7_3153.
DR   KEGG; pap:PSPA7_3153; -.
DR   HOGENOM; CLU_004245_3_2_6; -.
DR   OMA; FGMKWMM; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001582; Chromosome.
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; cd02855; E_set_GBE_prok_N; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
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   PANTHER; PTHR43651; PTHR43651; 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; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 2.
DR   TIGRFAMs; TIGR01515; branching_enzym; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..732
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_1000044993"
FT   ACT_SITE        412
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        465
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   732 AA;  82458 MW;  4A1F2E097DC57035 CRC64;
     MSEPMSERER WQLELDKLQR GLQGDPFAFL GPQRDADGEG GVLRAYLPGA QRVELLDEDG
     ATLAELEQSD PGSGLFQHHL ERLPARYRLR THWPDGVQES EDPYAFGPLL GELDLYLFAE
     GNHRQLASCL GAQLTRHEGV DGVRFAVWAP NAVRVSVVGD FNGWDGRRHP MRRRYPSGVW
     ELFIPRLGAG ELYKYELQGH AGLLPLKADP LALACETPPG TASKTCAALR HEWRDQDWLA
     RRAERQGYAA PLSIYEVHAG SWRHRDGRPP RWSELAEELI PYVRQLGFSH IELMPVMEHP
     FGGSWGYQPL GLFAPTARYG TPEDFAGFVD ACHQAGIGVI LDWVPAHFPT DAHGLGRFDG
     TALYEYEHPF EGFHQDWDTY IYNLGRSEVH GFMLASALHW LRTYHVDGLR VDAVASMLYR
     DYSRKEGEWL PNRHGGRENL EAIDFLHHLN QVVASETPGA LVIAEESTAW PGVSRPVAEG
     GLGFSHKWNM GWMHDSLAYI GEDPLHRRYH HHQLTFGLLY AFSEHFILPI SHDEVVHGKH
     SLLDKMPGDR WQKFANLRLY LSFMWSHPGK KLLFMGCEFG QWREWNHDGE LDWYLLRYPE
     HQGVQDLVAT LNRLYHELPA LHARDGEALG FEWLIGDDQA NSVYAWLRHA AGEPSLLAVH
     NFTPVPRQGY RIGVPQGGDW DVLLNSDAQA YAGSGAGSQG RVASEPAGAH GQAQSLLLEL
     PPLGTLLLRP AG