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Database: UniProt
Entry: A0A0B6TF69_9CORY
LinkDB: A0A0B6TF69_9CORY
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ID   A0A0B6TF69_9CORY        Unreviewed;       736 AA.
AC   A0A0B6TF69;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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   ECO:0000313|EMBL:AJK68642.1};
GN   ORFNames=B840_05130 {ECO:0000313|EMBL:AJK68642.1};
OS   Corynebacterium marinum DSM 44953.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1224162 {ECO:0000313|EMBL:AJK68642.1, ECO:0000313|Proteomes:UP000031928};
RN   [1] {ECO:0000313|EMBL:AJK68642.1, ECO:0000313|Proteomes:UP000031928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44953 {ECO:0000313|EMBL:AJK68642.1,
RC   ECO:0000313|Proteomes:UP000031928};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of Corynebacterium marinum DSM 44953.";
RL   Submitted (MAY-2014) 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; CP007790; AJK68642.1; -; Genomic_DNA.
DR   RefSeq; WP_042621244.1; NZ_CP007790.1.
DR   AlphaFoldDB; A0A0B6TF69; -.
DR   STRING; 1224162.B840_05130; -.
DR   KEGG; cmq:B840_05130; -.
DR   HOGENOM; CLU_004245_3_2_11; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000031928; 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; 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; 2.
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; 2.
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:UP000031928};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          259..613
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        464
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   736 AA;  82926 MW;  49DC94F3D55C5C86 CRC64;
     MHDADSGIDQ HLLIPAPDME RLHNCSHHAP HDFYGWHAVE GGSVIRTRQP GAELVEILIH
     NELRAATPVG DDVWVLALPD IYTPDYRLQI TWPEAGTIVS ADPYAFLPTL GNLDIHLVSE
     GRHERLWDVL GANVRSYETA LGTVTGTAFA VWAPNAIGVA VVGEFCVWNA SQYPMRSLGS
     SGVWELFIPD VGAGAAYKFA VQTKEGHRRD KADPMAKAAQ CPPETASVVV DSRYEWCDGE
     WLRNRSSADL LNEPMSIYEV HLGSWKIGKG YRDLTTELVD YVAEQGFTHV ELMPVSEHPF
     GGSWGYQVSG YYAPTARWGS PDELRALIDE FHNRGIGVIV DWVPAHFPKD DWALARFDGP
     ALYEHADWRR GEQKEWGTYV FDFGRNEVRN FLVANALYWI EEFHIDGLRV DAVASMLYLD
     YSREEGEWTP NQYGGRENLD AVQFLQEMNA TVHRTHPGVL TIAEESTSWQ GVTAPTEQGG
     LGFSLKWNMG WMNDTLEYFK LDPIHREHHH NEITFSMIYA YSEKYVLPFS HDEVVHGKGS
     LWGRMPGDDW NKAAGLRALY GYMFSHPGKN LLFMGQEFGQ TGEWDEAHSV DWSNLEGWGH
     EYHEGIQKLV RDIHQVYRSS PALYSQDHTY EGFQWVKGDD AANNILAYLR WGADDSALLA
     VVNLSGSSQE SYPLGTPRAG EWELVLNTDA AEYQGAGNDL PAVVSTDASG WDGFEHKLTL
     HVPANSVQWY RHRRNS
//
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