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Database: UniProt
Entry: R6DET4_9CLOT
LinkDB: R6DET4_9CLOT
Original site: R6DET4_9CLOT 
ID   R6DET4_9CLOT            Unreviewed;       754 AA.
AC   R6DET4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-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=BN547_01243 {ECO:0000313|EMBL:CDA86275.1};
OS   Clostridium sp. CAG:230.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262782 {ECO:0000313|EMBL:CDA86275.1, ECO:0000313|Proteomes:UP000017961};
RN   [1] {ECO:0000313|EMBL:CDA86275.1, ECO:0000313|Proteomes:UP000017961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:230 {ECO:0000313|Proteomes:UP000017961};
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:CDA86275.1}.
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DR   EMBL; CBCQ010000085; CDA86275.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6DET4; -.
DR   STRING; 1262782.BN547_01243; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000017961; 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; 2.
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 {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:UP000017961};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          275..653
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   754 AA;  86757 MW;  80B146D0B48C2C62 CRC64;
     MDKKLYDLMD WAEIETIVYS EHDHPENILG PHKVKGGVLI QAFLPDAKTV FVRSKKSGMF
     IQMSQTDEDG CFAALMESRK IVSYEYVIDY GDGKEYWQKD PYLYGNLIPE QALEDFNAGK
     AYDIYRYLGA HPVAVKGIGK DVLVDWNPMA ASTKRSDMVQ GTFFAVWAPN AMRVSVVGDF
     NQWDGRRHPM CRLGDSGVFG LFIPDIGCGD IYKYELKYNA RTIALKSDPY GFQYEDSMTM
     ASIITDLQNF LWEDAEWMQK RQKIQITQEA LNIYEVSLDG WLSKEDKDAG KGYRDAAKTL
     AKYVKGMGYT HIQLMPLMER VQKNSYGYPT VGYYAIRSCY GTPKDFMYFV DYMHQNGIGV
     IMEWIPGYFS TQEQGLAMFD GTCLYEHLNP LQGLHPFYDA MLFQYERPEV ANFLLANALY
     WKEMYHLDGI CVGGMETMLY LDYGRKEGEW IPNRYGGNEN LGGIDVLKKL AALFHQKEDG
     AILIAKEEMA SLGVTDPLED NGLGFDLKWN ICWTSDFLKY MKLDPLFRKG SHGLITMEML
     YHYSANFILT ISHRDTWKKK SSLFENMPGT IYDKFSNIRV GFGYMITHPG KKMLFMGEEF
     GVEDRKNTDG SLDWEQAQSK EHAQLQRYVK DLNMLYRNHT ALYVMDYRQD GFEWISCMDA
     DHSIIAFLRK DQDDILLVIC NFTPVLYENF KVGVPFMGRY KEIFNSDRTI YGGAGYANSN
     ELTAKEVSWD GRSHSIAIKL PPYGFCVFRA VPEK
//
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