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Database: UniProt
Entry: E2ZLD1_9FIRM
LinkDB: E2ZLD1_9FIRM
Original site: E2ZLD1_9FIRM 
ID   E2ZLD1_9FIRM            Unreviewed;       649 AA.
AC   E2ZLD1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE            EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN   Name=glgB {ECO:0000313|EMBL:EFQ05971.1};
GN   ORFNames=HMPREF9436_02487 {ECO:0000313|EMBL:EFQ05971.1};
OS   Faecalibacterium cf. prausnitzii KLE1255.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ05971.1, ECO:0000313|Proteomes:UP000006028};
RN   [1] {ECO:0000313|EMBL:EFQ05971.1, ECO:0000313|Proteomes:UP000006028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ05971.1,
RC   ECO:0000313|Proteomes:UP000006028};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2010) 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:EFQ05971.1}.
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DR   EMBL; AECU01000187; EFQ05971.1; -; Genomic_DNA.
DR   RefSeq; WP_005944535.1; NZ_GL538342.1.
DR   AlphaFoldDB; E2ZLD1; -.
DR   STRING; 748224.HMPREF9436_02487; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_4_0_9; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000006028; 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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
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   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:EFQ05971.1}; Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFQ05971.1}.
FT   DOMAIN          143..488
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        305
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        348
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   649 AA;  74095 MW;  8FC440F56CFE16F8 CRC64;
     MNYPAIPREF FNGDCFDAYR ILGAHPCSDN GIEGWRFAVW APGATAVEVC GGFDGWEAGV
     PMEKADTGVW SAFVPGLAEG DLYKYRVHGA DGSVVMRSDP YAFSTELRPG TASRLAKLDF
     HFDDSAWMER RDKCRNRPLN IYEMHVGSWR HKPGSKQEDG SDGWYNYEEL AKELIPWLLD
     HHFTHVELLP LAEHPFDGSW GYQTTGYFSV TSRYGTPAQF AGFVNACHRM GIGVIMDFVP
     VHFAANADAL AKFDGTHLYE YDSDVGHSEW GTCNFNYYRR EVCSFLNSAA ALWMDVYHCD
     GIRMDAISRA LYWQGDPNRG VNEGAVNFLR SLNHGLNERW PTGIYTAEDS TNFLKVTAPT
     RYDGVGFDYK WDMGWMHDTL DYFATPFGER PNVYGKIVFS MHYFYNELYL LALSHDEVVH
     GKKTIIDKLW GTYAEKCAQL RTLYFYMYMH PGKKLNFMGN EMGHFREWDE KRELDWDLLK
     YPFHDAFQKY FAHLCRVYST EPALYDGEYN PDCFEWVACE SRSEGVYAWL RKGRGENLLC
     IMNTQDHAHK KFPLYLRFPC SAEEVLNTES PEWGGALKGR RKTKLHTTDG GVFGRDYTLT
     VDLPAMGSCL LRLAPEAPNP DAARISANKA LNAKRRAARS TKAAANSNK
//
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