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Database: UniProt
Entry: R5LFQ6_9FIRM
LinkDB: R5LFQ6_9FIRM
Original site: R5LFQ6_9FIRM 
ID   R5LFQ6_9FIRM            Unreviewed;       672 AA.
AC   R5LFQ6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=BN569_01046 {ECO:0000313|EMBL:CCY77965.1};
OS   Butyrivibrio crossotus CAG:259.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1263062 {ECO:0000313|EMBL:CCY77965.1, ECO:0000313|Proteomes:UP000018300};
RN   [1] {ECO:0000313|EMBL:CCY77965.1, ECO:0000313|Proteomes:UP000018300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:259 {ECO:0000313|Proteomes:UP000018300};
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   -!- 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:CCY77965.1}.
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DR   EMBL; CAYU010000082; CCY77965.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5LFQ6; -.
DR   Proteomes; UP000018300; 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:InterPro.
DR   CDD; cd02855; E_set_GBE_prok_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
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; 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   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; 3.
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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018300};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          127..209
FT                   /note="Glycoside hydrolase family 13 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02922"
FT   DOMAIN          295..332
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00128"
FT   DOMAIN          564..660
FT                   /note="Alpha-amylase/branching enzyme C-terminal all beta"
FT                   /evidence="ECO:0000259|Pfam:PF02806"
SQ   SEQUENCE   672 AA;  76172 MW;  1FC941065270646E CRC64;
     MDKKLYDLMN WPDIEGIIYS DGCKPKNLLG THSVKGGILI QSFYPAAVGA TVKAADGKTY
     EMEMADEEGY FAVLIPVKSK FAYTVEFRFE DGNTFETDDA YNYPSMIKKS DLKSFIEGNN
     NHVYRFLGAH EMDYKGVKGV DFAIWAPEAL RVSVVGEFNN WDGRIHQLEA IDSTGVFELF
     VPGVKASSLY KFEIRLKGGK VVLITDPFSK MSESKSEPAS FVCDDNFKWS DEEWLSNRKS
     RNKYKEAPMS VYTYSLPDED VTYKEITQAI ENTFSESRFT HVVLKNVINT YTGLYLDYDR
     TGYFSINNRY GSLDDFKTLI NSLHKRNIGV LIQWNFDDIN VGRNEVANIM YSSASYIIEE
     LHADGIVADR LGNAVYLDFE RDKWTSNMFG GRENLEAVDF IRGLNEIFGK QYKDVITVAD
     DRAGWPDVTG SIKEEGALGF DYSINHIFGD NLIYFLGCDP LFRKGRYNKL SLSIVTFYNQ
     DSILAFDADS INMLEAKIPG RIHGDKMANL RAAFAYSFAH PGKKTIYSGN GEETWNTFVK
     ALTDFYNKHS ELSEMDYEID GFEWINNISG NECVLSFVRK SKDGRILVVI ANFTPVIREK
     YKIGVPFEGR YKEIFNTDDE KFGGSGILNK RAVSSKKDEC DGRADSIRLT LPPLGVIVLD
     YTKTVAKKGN TK
//
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