ID   GLGB_MYCTO              Reviewed;         731 AA.
AC   P9WN44; L0T925; Q10625;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB;
DE            EC=2.4.1.18;
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase;
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme;
DE   AltName: Full=Glycogen-branching enzyme;
DE            Short=BE;
GN   Name=glgB; OrderedLocusNames=MT1368;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Essential enzyme that catalyzes the formation of the alpha-
CC       1,6-glucosidic linkages in glucan chains by scission of a 1,4-alpha-
CC       linked oligosaccharide from growing alpha-1,4-glucan chains and the
CC       subsequent attachment of the oligosaccharide to the alpha-1,6 position.
CC       Is involved in the biosynthesis of both glycogen and capsular alpha-D-
CC       glucan (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45632.1; -; Genomic_DNA.
DR   PIR; B70770; B70770.
DR   RefSeq; WP_010924383.1; NC_002755.2.
DR   AlphaFoldDB; P9WN44; -.
DR   SMR; P9WN44; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; AAK45632; AAK45632; MT1368.
DR   KEGG; mtc:MT1368; -.
DR   HOGENOM; CLU_004245_3_2_11; -.
DR   UniPathway; UPA00164; -.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000001020; 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:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
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; -; 2.
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   Capsule biogenesis/degradation; Carbohydrate metabolism; Disulfide bond;
KW   Glycogen biosynthesis; Glycogen metabolism; Glycosyltransferase;
KW   Transferase.
FT   CHAIN           1..731
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000427191"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        464
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        193..617
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   731 AA;  81734 MW;  1B2BFEF7654AE9A7 CRC64;
     MSRSEKLTGE HLAPEPAEMA RLVAGTHHNP HGILGAHEYD DHTVIRAFRP HAVEVVALVG
     KDRFSLQHLD SGLFAVALPF VDLIDYRLQV TYEGCEPHTV ADAYRFLPTL GEVDLHLFAE
     GRHERLWEVL GAHPRSFTTA DGVVSGVSFA VWAPNAKGVS LIGEFNGWNG HEAPMRVLGP
     SGVWELFWPD FPCDGLYKFR VHGADGVVTD RADAFAFGTE VPQQTASRVT SSDYTWGDDD
     WMAGRALRNP VNEAMSTYEV HLGSWRPGLS YRQLARELTD YIVDQGFTHV ELLPVAEHPF
     AGSWGYQVTS YYAPTSRFGT PDDFRALVDA LHQAGIGVIV DWVPAHFPKD AWALGRFDGT
     PLYEHSDPKR GEQLDWGTYV FDFGRPEVRN FLVANALYWL QEFHIDGLRV DAVASMLYLD
     YSRPEGGWTP NVHGGRENLE AVQFLQEMNA TAHKVAPGIV TIAEESTPWS GVTRPTNIGG
     LGFSMKWNMG WMHDTLDYVS RDPVYRSYHH HEMTFSMLYA FSENYVLPLS HDEVVHGKGT
     LWGRMPGNNH VKAAGLRSLL AYQWAHPGKQ LLFMGQEFGQ RAEWSEQRGL DWFQLDENGF
     SNGIQRLVRD INDIYRCHPA LWSLDTTPEG YSWIDANDSA NNVLSFMRYG SDGSVLACVF
     NFAGAEHRDY RLGLPRAGRW REVLNTDATI YHGSGIGNLG GVDATDDPWH GRPASAVLVL
     PPTSALWLTP A