ID   GLGB_MYCS2              Reviewed;         736 AA.
AC   A0R1Y4; I7FR43;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 120.
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=Glycogen-branching enzyme;
DE            Short=BE;
GN   Name=glgB; OrderedLocusNames=MSMEG_4918, MSMEI_4790;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=20305657; DOI=10.1038/nchembio.340;
RA   Kalscheuer R., Syson K., Veeraraghavan U., Weinrick B., Biermann K.E.,
RA   Liu Z., Sacchettini J.C., Besra G., Bornemann S., Jacobs W.R. Jr.;
RT   "Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an
RT   alpha-glucan pathway.";
RL   Nat. Chem. Biol. 6:376-384(2010).
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: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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene display maltose 1-
CC       phosphate (M1P) accumulation and trehalose sensitivity. These
CC       phenotypes are suppressed in mutants lacking both glgE and treS or both
CC       glgE and mak. {ECO:0000269|PubMed:20305657}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP000480; ABK70471.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP41238.1; -; Genomic_DNA.
DR   RefSeq; WP_011730189.1; NZ_SIJM01000024.1.
DR   RefSeq; YP_889172.1; NC_008596.1.
DR   AlphaFoldDB; A0R1Y4; -.
DR   SMR; A0R1Y4; -.
DR   STRING; 246196.MSMEG_4918; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; 246196-MSMEI_4790; -.
DR   GeneID; 66736221; -.
DR   KEGG; msg:MSMEI_4790; -.
DR   KEGG; msm:MSMEG_4918; -.
DR   PATRIC; fig|246196.19.peg.4798; -.
DR   eggNOG; COG0296; Bacteria.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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; 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; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..736
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000413977"
FT   ACT_SITE        416
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        469
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   736 AA;  82656 MW;  937C85D1A22A6A73 CRC64;
     MTRSSNQLTD AHLRPDPSDI HRLLAGEHHD PHSVLGAHEY PGHTVIRAFR PHAVKVTAVI
     GGERHVMQHL ESGLFAVAVP FTNLIDYRLE IDYPGVGDAV VTHTTADAYR FLPTLGELDL
     HLFAEGRHER LWEILGAHRR TFTTADGPVS GVSFAVWAPN AKGVSLIGEF NHWGGNDAPM
     RVLGSSGVWE LFWPGFPPDG LYKFRVHGAD GSVTDRADPM AFATEVPPHT ASRVTESTYE
     WHDEDWMTRR ASLNPVFEPM STLEVHLLSW RPGLTYRQLA TELTEYVVEQ GFTHVEMLPV
     AEHPFGGSWG YQVTSYYAPT SRLGTPDDFR YLVDALHQAG IGVIVDWVPA HFPKDAWALG
     RFDGTALYEH SDPRRGEQLD WGTYVFDFGR PEVRNFLVAN ALYWLQEFHI DGLRVDAVAS
     MLYLDYSRPE GGWTPNQYGG RENLEAVQFL QEMNATVHKV APGIVTVAEE STSWPGVTRP
     TNLGGLGFSM KWNMGWMNDT LAYISRDPIY RSYHHHEMTF SMLYAYSENY VLPISHDEVV
     HGKGTLWSRM PGGDHEKAAG LRSLLAYQWA HPGKQLLFMG QEFGQRAEWS EERGLDWYQL
     DEQSFSTGVQ NLVRDLNAIY RSRPALWSRD TSPEGYSWID ANDSANNVLS FLRFGNDGSM
     LACVINFAGS EHSQYRLGLP HAGTWREVLN TDADIYNGSG IGNYGAVEAT DEPWHGRPAS
     AVMVLPPLSM LWFEPA
//