ID GLGB_RHIID Reviewed; 683 AA. AC Q8NKE1; U9SPI3; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 19-MAR-2014, sequence version 2. DT 24-JAN-2024, entry version 92. DE RecName: Full=1,4-alpha-glucan-branching enzyme; DE EC=2.4.1.18; DE AltName: Full=Glycogen-branching enzyme; GN Name=GLC3; ORFNames=GLOINDRAFT_70859; OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194) OS (Arbuscular mycorrhizal fungus) (Glomus intraradices). OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina; OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus. OX NCBI_TaxID=747089; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194; RX PubMed=12644699; DOI=10.1104/pp.102.007765; RA Bago B., Pfeffer P.E., Abubaker J., Jun J., Allen J.W., Brouillette J., RA Douds D.D., Lammers P.J., Shachar-Hill Y.; RT "Carbon export from arbuscular mycorrhizal roots involves the translocation RT of carbohydrate as well as lipid."; RL Plant Physiol. 131:1496-1507(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 24-683. RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194; RX PubMed=24277808; DOI=10.1073/pnas.1313452110; RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R., RA Charron P., Duensing N., Frei dit Frey N., Gianinazzi-Pearson V., RA Gilbert L.B., Handa Y., Herr J.R., Hijri M., Koul R., Kawaguchi M., RA Krajinski F., Lammers P.J., Masclaux F.G., Murat C., Morin E., RA Ndikumana S., Pagni M., Petitpierre D., Requena N., Rosikiewicz P., RA Riley R., Saito K., San Clemente H., Shapiro H., van Tuinen D., Becard G., RA Bonfante P., Paszkowski U., Shachar-Hill Y.Y., Tuskan G.A., Young J.P.W., RA Sanders I.R., Henrissat B., Rensing S.A., Grigoriev I.V., Corradi N., RA Roux C., Martin F.; RT "Genome of an arbuscular mycorrhizal fungus provides insight into the RT oldest plant symbiosis."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20117-20122(2013). 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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAM33305.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF503447; AAM33305.1; ALT_FRAME; mRNA. DR EMBL; KI299226; ERZ97888.1; -; Genomic_DNA. DR AlphaFoldDB; Q8NKE1; -. DR SMR; Q8NKE1; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR VEuPathDB; FungiDB:GLOIN_2v1817213; -. DR eggNOG; KOG0470; Eukaryota. DR HOGENOM; CLU_011131_2_2_1; -. DR OrthoDB; 96at2759; -. DR UniPathway; UPA00164; -. 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; 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 2: Evidence at transcript level; KW Glycogen biosynthesis; Glycosyltransferase; Transferase. FT CHAIN 1..683 FT /note="1,4-alpha-glucan-branching enzyme" FT /id="PRO_0000188783" FT ACT_SITE 342 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 397 FT /note="Proton donor" FT /evidence="ECO:0000250" FT CONFLICT 474..483 FT /note="TLAFWLMDKE -> NTCLLVNGQG (in Ref. 1; AAM33305)" FT /evidence="ECO:0000305" FT CONFLICT 613 FT /note="H -> L (in Ref. 1; AAM33305)" FT /evidence="ECO:0000305" FT CONFLICT 678 FT /note="L -> P (in Ref. 1; AAM33305)" FT /evidence="ECO:0000305" SQ SEQUENCE 683 AA; 79142 MW; 0AABB4601D69D1CF CRC64; MSPTEMISQE NYEPGICKID PWLKPFAPAI KRRLESYKKW VKEINQNEGG YDKFSRGYER FGLNVLPNGD IIYREWAPNA VAASLIGEFN DWDRSKHPMK KDSFGVWEVH IPAKNGIPTI PHNTKIKISM TTPEGECIDR LPAWIKRVTQ DLNVSLAYDA IFWNPPQKYQ WKNNSPKKPT SLRIYEAHVG ISTNEGRVGT YNEFTDNVLK RIKDLGYNAI QLMAIMEHAY YASFGYQVTS FFGVSSRYGT PEELMRLIDT AHGMGLYVLL DVVHSHACKN VLDGLNMFDG SDHCYFHEGG KGRHDLWDSR LFNYGHWEVL RFLLSNLRFF MEEYRFDGFR FDGVTSMMYH HHGIGTGFSG GYHEYFGDTV DEGGVVYLML ANDMLHKLYP RIITVSEDVS GMPGLCLPVE EGGIGFDYRL AMAIPDMWIK LLKEQRDDDW DMGNICWTLT NRRHMEKTIA YAESHDQALV GDKTLAFWLM DKEMYTHMSD MTPLTPIIDR GLALHKMIRL LTHGLGGEGY LNFEGNEFGH PEWLDFPRAG NNNSFHYARR QWNVVDDDLL RYKYLNEFDK AMQHLEEQYG WLSSPQAYIS LKHNENKLVA FERGNLLWIF NFHPTQSFAD YKIGTEWAGK YSIALNTDRK IFGGHDRIDE SISYHSQPHE WDGRKNYIQV YIPCRVALVL SHC //