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Database: UniProt
Entry: R6RGG4_9FIRM
LinkDB: R6RGG4_9FIRM
Original site: R6RGG4_9FIRM 
ID   R6RGG4_9FIRM            Unreviewed;       610 AA.
AC   R6RGG4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=BN661_01193 {ECO:0000313|EMBL:CDC42061.1};
OS   Firmicutes bacterium CAG:449.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263023 {ECO:0000313|EMBL:CDC42061.1, ECO:0000313|Proteomes:UP000018133};
RN   [1] {ECO:0000313|EMBL:CDC42061.1, ECO:0000313|Proteomes:UP000018133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:449 {ECO:0000313|Proteomes:UP000018133};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDC42061.1}.
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DR   EMBL; CBFH010000163; CDC42061.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6RGG4; -.
DR   STRING; 1263023.BN661_01193; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000018133; 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:UP000018133};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          145..492
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        300
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        343
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   610 AA;  71671 MW;  10E8CFBEADF77756 CRC64;
     MAFGLLYDFL MGQTIEAYKY FGAHFVTQNK KEGALFRVYA PMAKDVSVIG EFNNWDPSKH
     QMKKVDVSGV YEVFIEGVKN YQTYKFHIHD ANGNYIDKQD PFAYFSEYRS GSCSKLFDIE
     NFIWHDEKYL KNRNRNFDKP MSIYEIHIGS WLDHPDNRFL SYEEVADKLI KYVLENGFTH
     VELMPITQYP FDGSWGYQAT GFYSTDSRYG NPFQLMSFID RLHQAGIGVI LDYVVVHFAT
     DEFALEKFDG TNLFEYTGEN EYSQWGSKLF DLGKDPVRSF LMSGIDYFIS YFHFDGIRLD
     AISNVIYWHG DSSRGENIGA IEFVKRLNGK IHLKHPDVMM IAEDSSSYQG VTKPLEYGGL
     GFDYKWDLGW MNDTLAYYAK DPIYRKYHHH SLTFSMAYFY SENFLLPLSH DEVVHGKGTI
     INKMWGDYDQ KFAQIRNLYT YMWAHPGKKL NFMGNEIASF DEWSEKKSLP WNLKTYPKHD
     SISRLVRDLN LIYQYEPSMH EEEYNPVHFQ WLMADNASQS IYAFRRSYLE DTLIFIFNMT
     PNYYEYINIG VPFEGEYEEI FNSDKDVYGG YNHYNGLPLQ TMNMSWNNQP YTISIKLASF
     GALILKYKSK
//
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