GLGB_RHIID
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 25-MAY-2022, entry version 89.
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};
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DR EMBL; AF503447; AAM33305.1; ALT_FRAME; mRNA.
DR EMBL; KI299226; ERZ97888.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NKE1; -.
DR SMR; Q8NKE1; -.
DR STRING; 588596.Q8NKE1; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q8NKE1; -.
DR VEuPathDB; FungiDB:GLOIN_2v1817213; -.
DR eggNOG; KOG0470; Eukaryota.
DR HOGENOM; CLU_011131_2_2_1; -.
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 Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 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; PTHR43651; 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; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 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
