ID   GLGB_BERDE              Reviewed;         762 AA.
AC   Q9RQI5;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 92.
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};
OS   Bergeriella denitrificans (Neisseria denitrificans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Bergeriella.
OX   NCBI_TaxID=494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14686 / DSM 17675 / CIP 72.16 / JCM 21446 / NBRC 102155 / NCTC
RC   10295;
RX   PubMed=10407163; DOI=10.1016/s0167-4838(99)00101-6;
RA   Buettcher V., Quanz M., Willmitzer L.;
RT   "Molecular cloning, functional expression and purification of a glucan
RT   branching enzyme from Neisseria denitrificans.";
RL   Biochim. Biophys. Acta 1432:406-412(1999).
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; AF102867; AAF04747.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RQI5; -.
DR   SMR; Q9RQI5; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q9RQI5; -.
DR   BRENDA; 2.4.1.18; 3588.
DR   UniPathway; UPA00164; -.
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..762
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000188719"
FT   ACT_SITE        417
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        470
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   762 AA;  86367 MW;  9922F80406DDE3E3 CRC64;
     MNRNRHIRRG YHPEAGERQI IDSLFAATHS DPFAYLGRHR VNDEREAVRV LRPDAHHIDI
     IDRHTGAVIM PSEKIDERGL FAAVLPEHAP DYALLVTYHE GEAAVREEDD YRFGSALQHT
     DAWLLGEGTH LRPYETLGAH FAEMDGVSGV RFAVWAPNAR RVSVIGEFNG WDSRRHAMRP
     HTGNGLWDIF IPGVGLNALY KFSVLDANGN IREKADPYAF GAELRPTTAS VVRGLPAKAE
     APAFRRRANS VEAPISIYEV HLGSWRRNPE NNYWLTYTQL ADELVNYVKD MGFTHIELLP
     LSEYPFDGSW GYQATGLYAP TSRFGSPDEL KALIDAAHAA GISVILDWVA GHFPTDDHGL
     NTFDGTALYE HADPREGYHQ DWNTLIYNFG RNEVKNFLQG NALYWIERFG FDGIRVDAVA
     SMIYRNYSRK DGEWIPNRYG GSENLEAIAF LRQTNAVLKS ETPGAGSFAE ESTSFADVTR
     EAGLNFDFKW NMGWMNDTLR YMQEDPVHRK YHHGKMTFGM MYQYSENFVL PLSHDEVVHG
     KRSLLGKMPG DCWQQFANLR AYYGFMYGFP GKKLLFMGNE FAQGREWNYQ EGLDWHLLDE
     AGGWHKGVQD YVRDLNHIYT AHAPLYQLDQ QPEGFEWLVA DDSDNSVFVF ERRDRAGNRI
     IVISNFTPVV REHYRFGVNA PGRYTEILNS DRTQYQGSGI ANGADITAEN VPSHGKAQSL
     SLTLPPLATV YLYQKAAPAT EIQTALRADK QPAVKDKQAK AK