ID   BE_MYCTO                Reviewed;         526 AA.
AC   P9WQ26; L0TE45; O53278; Q7D694;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Probable 1,4-alpha-glucan branching enzyme MT3115;
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=Branching enzyme;
DE            Short=BE;
GN   OrderedLocusNames=MT3115;
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: Catalyzes the formation of branch points in alpha-glucans by
CC       cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the
CC       cleaved-off oligosaccharide to a new alpha-1,6 position (Probable). Is
CC       probably involved in the biosynthesis of 6-O-methylglucosyl
CC       lipopolysaccharides (MGLP) (By similarity). {ECO:0000250, ECO:0000305}.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47445.1; -; Genomic_DNA.
DR   PIR; B70859; B70859.
DR   RefSeq; WP_003899891.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ26; -.
DR   SMR; P9WQ26; -.
DR   CAZy; GH57; Glycoside Hydrolase Family 57.
DR   EnsemblBacteria; AAK47445; AAK47445; MT3115.
DR   KEGG; mtc:MT3115; -.
DR   PATRIC; fig|83331.31.peg.3357; -.
DR   HOGENOM; CLU_008192_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
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:0030979; P:alpha-glucan biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.1430.10; -; 1.
DR   Gene3D; 3.20.110.10; -; 1.
DR   InterPro; IPR037090; 57_glycoside_trans_central.
DR   InterPro; IPR015293; BE_C.
DR   InterPro; IPR040042; Branching_enz_MT3115-like.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   InterPro; IPR004300; Glyco_hydro_57_N.
DR   PANTHER; PTHR41695; PTHR41695; 1.
DR   Pfam; PF09210; DUF1957; 1.
DR   Pfam; PF03065; Glyco_hydro_57; 1.
DR   SUPFAM; SSF88688; SSF88688; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosyltransferase; Transferase.
FT   CHAIN           1..526
FT                   /note="Probable 1,4-alpha-glucan branching enzyme MT3115"
FT                   /id="PRO_0000426849"
FT   ACT_SITE        205
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        344
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         396
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         462
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   526 AA;  57815 MW;  6095D375968E9589 CRC64;
     MNTSASPVPG LFTLVLHTHL PWLAHHGRWP VGEEWLYQSW AAAYLPLLQV LAALADENRH
     RLITLGMTPV VNAQLDDPYC LNGVHHWLAN WQLRAEEAAS VRYARQSKSA DYPSCTPEAL
     RAFGIRECAD AARALDNFAT RWRHGGSPLL RGLIDAGTVE LLGGPLAHPF QPLLAPRLRE
     FALREGLADA QLRLAHRPKG IWAPECAYAP GMEVDYATAG VSHFMVDGPS LHGDTALGRP
     VGKTDVVAFG RDLQVSYRVW SPKSGYPGHA AYRDFHTYDH LTGLKPARVT GRNVPSEQKA
     PYDPERADRA VDVHVADFVD VVRNRLLSES ERIGRPAHVI AAFDTELFGH WWYEGPTWLQ
     RVLRALPAAG VRVGTLSDAI ADGFVGDPVE LPPSSWGSGK DWQVWSGAKV ADLVQLNSEV
     VDTALTTIDK ALAQTASLDG PLPRDHVADQ ILRETLLTVS SDWPFMVSKD SAADYARYRA
     HLHAHATREI AGALAAGRRD TARRLAEGWN RADGLFGALD ARRLPK