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Database: UniProt
Entry: F7LY75_9BACE
LinkDB: F7LY75_9BACE
Original site: F7LY75_9BACE 
ID   F7LY75_9BACE            Unreviewed;       670 AA.
AC   F7LY75;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
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=HMPREF0127_00165 {ECO:0000313|EMBL:EGN06252.1};
OS   Bacteroides sp. 1_1_30.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=457387 {ECO:0000313|EMBL:EGN06252.1, ECO:0000313|Proteomes:UP000004085};
RN   [1] {ECO:0000313|EMBL:EGN06252.1, ECO:0000313|Proteomes:UP000004085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_1_30 {ECO:0000313|EMBL:EGN06252.1,
RC   ECO:0000313|Proteomes:UP000004085};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. 1_1_30.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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:EGN06252.1}.
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DR   EMBL; ADCL01000004; EGN06252.1; -; Genomic_DNA.
DR   RefSeq; WP_008640123.1; NZ_JAJKHN010000031.1.
DR   AlphaFoldDB; F7LY75; -.
DR   GeneID; 69480109; -.
DR   PATRIC; fig|457387.3.peg.155; -.
DR   HOGENOM; CLU_011131_2_2_10; -.
DR   Proteomes; UP000004085; 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; cd11321; AmyAc_bac_euk_BE; 1.
DR   CDD; cd02854; E_set_GBE_euk_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; 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; 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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          182..544
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        329
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        383
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   670 AA;  77362 MW;  44651E9E55DF63A3 CRC64;
     MEKTLNLIKN DPWLEPFAGA ITGRHQHVLD KEAELTNKGK QTLSDFASGY LYFGLHRTDK
     GWTFREWAPN ATHIYMVGTF NNWEEKAAYK LKKLKNGNWE INLPADAIHH GDLYKLNVYW
     EGGQGERIPA WATRVVQDEQ TKIFSAQVWA PEKPYKFKKK TFKPDTNPLL IYECHIGMAQ
     REEKVGTYNE FREKILPRIA EEGYNCIQIM AIQEHPYYGS FGYHVSSFFA ASSRFGTPDE
     LKALIDAAHE MGIAVIMDIV HSHAVKNEVE GLGNFAGDPN QYFYPGVRRE HPAWDSLCFD
     YGKNEVIHFL LSNCKYWLEE YKFDGFRFDG VTSMLYYSHG LGEAFCNYGD YFNGHQDDNA
     ICYLTLANEV IHQVNPKAIT IAEEVSGMPG LAAKIEDGGY GFDYRMAMNI PDYWIKTIKE
     KIDEDWKPSS MFWEVTNRRQ DEKTISYAES HDQALVGDKT IIFRLIDADM YWHMQKGDEN
     YVVNRGIALH KMIRLLTSST INGGYLNFMG NEFGHPEWID FPREGNGWSC KYARRQWDLV
     DNKNLTYHYM GDFDKNMLKV LKSVKNFQTT PVQEIWHNDG DQVLAYGRKD LIFVFNFNPK
     QSFTDYGFLV TPGAYEVILN TDDVAFGGNG LADDSVVHFT IADPLYSKEK KEWLKLYIPA
     RTAVVLRKKK
//
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