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Database: UniProt
Entry: S0L364_9ENTE
LinkDB: S0L364_9ENTE
Original site: S0L364_9ENTE 
ID   S0L364_9ENTE            Unreviewed;       627 AA.
AC   S0L364;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE            EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN   ORFNames=I573_00121 {ECO:0000313|EMBL:EOT87066.1};
OS   Enterococcus sulfureus ATCC 49903.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1140003 {ECO:0000313|EMBL:EOT87066.1, ECO:0000313|Proteomes:UP000015961};
RN   [1] {ECO:0000313|EMBL:EOT87066.1, ECO:0000313|Proteomes:UP000015961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49903 {ECO:0000313|EMBL:EOT87066.1,
RC   ECO:0000313|Proteomes:UP000015961};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus sulfureus ATCC_49903 (PacBio/Illumina
RT   hybrid assembly).";
RL   Submitted (MAR-2013) 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.
CC       {ECO:0000256|ARBA:ARBA00002953}.
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};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004964}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000256|ARBA:ARBA00009000}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOT87066.1}.
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DR   EMBL; ASWO01000001; EOT87066.1; -; Genomic_DNA.
DR   RefSeq; WP_016184614.1; NZ_KE136393.1.
DR   AlphaFoldDB; S0L364; -.
DR   STRING; 1140003.OMY_00122; -.
DR   PATRIC; fig|1140003.3.peg.120; -.
DR   eggNOG; COG0296; Bacteria.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000015961; Unassembled WGS sequence.
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: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-UniPathway.
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; 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; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015961};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          153..504
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        303
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        354
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   627 AA;  73330 MW;  EC4A4E61961C2E1D CRC64;
     MELKQVEQAK QLFTTGENFY AHHLLGAHQT EDGYVFRVFA PNAKQVWLVG TFNDWDHTLS
     MTKDHESGIW EIHTNLPKEG DLYKFKLEQQ NGRQVYKIDP FAIRFEPRPN NAAILYTVAT
     HKWRDGLYRG RNKRSQTLKR PMNIYEVHAG SWRYHWDGTP FTFKELADEL VPYVKEMGYT
     HIELMPVMEH PLDRSWGYQL TGYFALAENY GTPEEFQAFV DLCHQENIGV LLDWVPGHFC
     VNDDALAYYD GTPTFEYQDE NRAQNIRWGS LNFDLSKPQV QSFLISNALF WIEFFHIDGL
     RVDAVSSMIY LDYDDKGWEP NHLGTNQNLD GVYFLQKLNA VVKLAHPEVL MIAEESSSET
     KITGRVEDHA LGFDYKWDLG WMNDTLAFYE MDPIYRQYHL NKLTFSFMYM ANEQYILPLS
     HDEVVHGKKS LLHKMWGDRY KQFSQLRNLY TYLLTHPGKK LSFMGNEWGQ FLEWKYNEGL
     EWKDLADDMN KKMQAFTIKM NALYKEEQAL WELETSPQES IEFIDADNTK DVVLSFIRKG
     KRKKDFLIVV LNFTPQEQQD FRIKVPYKGT YEELVNTELA EFGGTWTTGQ APFTSVSEAG
     EHFIDMIVPA LGALIIKPTA ITITRKK
//
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