ID R9XIK8_ASHAC Unreviewed; 703 AA.
AC R9XIK8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=1,4-alpha-glucan-branching enzyme {ECO:0000256|ARBA:ARBA00020932};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
DE AltName: Full=Glycogen-branching enzyme {ECO:0000256|ARBA:ARBA00031979};
GN ORFNames=AACERI_AaceriAEL044W {ECO:0000313|EMBL:AGO12315.1};
OS Ashbya aceri (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=566037 {ECO:0000313|EMBL:AGO12315.1, ECO:0000313|Proteomes:UP000016920};
RN [1] {ECO:0000313|Proteomes:UP000016920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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 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 ---------------------------------------------------------------------------
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; CP006024; AGO12315.1; -; Genomic_DNA.
DR AlphaFoldDB; R9XIK8; -.
DR HOGENOM; CLU_011131_2_2_1; -.
DR OrthoDB; 96at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000016920; Chromosome V.
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 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 173..571
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 355
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 415
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 703 AA; 80446 MW; 91599FC9DD2A0C40 CRC64;
MASVPDNVKG VIELDPWLSP YADTLSARRF LADKWKHDIE HAVPGEQRSL VEFARDAYKS
YGLHADARSK SIIYREWAPN AKRAFLVGDF NGWDESTHEL ESKDEFGVFT GVFGPGADGD
FVIPHDSRVK VVFELADGSR IHRLPAWITR ATQPSKETAK EWGPSYEARF WNPATPYKFK
HERPRLDPDL DSLRIYEAHV GISTPEPRVG SYREFTENVL PRIKDLGYNA IQLMAIMEHA
YYASFGYQVT NFFAVSSRYG TPEELKELID TAHGMGIQVL LDVVHSHASK NVSDGLNMFD
GTDYQYFHSI SSGRGEHPLW DSRLFNYGSF EVQRFLLANL AFYIDVYQFD GFRFDGVTSM
LYHHHGVGER GAFSGDYNEY LSDNSGVDHE ALAYLMLAND LIHDMLPANG VTVAEDVSGY
PTLCVPRTIG GCGFDYRLAM ALPDMWIKLL KESRDEDWGM GHIVYTLVNR RYKEKVVAYA
ESHDQALVGD KTLAFWMMDA AMYTDMTVLK ELTPVVDRGI ALHKMIRLIT HSLGGESYLN
FEGNEFGHPE WLDFPNANNG DSYQYARRQF NLVDDDLLRY KHLYAFDKAM QEAECKYKWL
NTAQAYVSLK HETDKVISFE RNGLVFIFNF HPTESFTDYR IGVDQPGAYR IILNSDRQEF
GGHSRIEEDK SVFHTTDLEW NGRRNFIQVY LPSRTALVLA RNP
//
