(data stored in ACNUC7421 zone)

SWISSPROT: GLGB_ASHGO

ID   GLGB_ASHGO              Reviewed;         703 AA.
AC   Q757Q6;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 101.
DE   RecName: Full=1,4-alpha-glucan-branching enzyme;
DE            EC=2.4.1.18;
DE   AltName: Full=Glycogen-branching enzyme;
GN   Name=GLC3; OrderedLocusNames=AEL044W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
DR   EMBL; AE016818; AAS52641.1; -; Genomic_DNA.
DR   RefSeq; NP_984817.1; NM_210171.1.
DR   SMR; Q757Q6; -.
DR   STRING; 33169.AAS52641; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q757Q6; -.
DR   EnsemblFungi; AAS52641; AAS52641; AGOS_AEL044W.
DR   GeneID; 4621011; -.
DR   KEGG; ago:AGOS_AEL044W; -.
DR   HOGENOM; HOG000175159; -.
DR   InParanoid; Q757Q6; -.
DR   KO; K00700; -.
DR   OMA; YEMHLGS; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
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   3: Inferred from homology;
DR   PRODOM; Q757Q6.
DR   SWISS-2DPAGE; Q757Q6.
KW   Glycogen biosynthesis; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..703
FT                   /note="1,4-alpha-glucan-branching enzyme"
FT                   /id="PRO_0000188777"
FT   ACT_SITE        355
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        415
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   703 AA;  80263 MW;  B41AE8250252DBF4 CRC64;
     MAGVPDNVKG VVELDPWLAP YGDILSARRF LADKWRHDIE HAVPGGRRSL VEFARDAYKS
     YGLHADAQSK SITYREWAPN ATRAFLVGDF NGWDETSHEL QNKDEFGVFT GVFGPGADGD
     FMIPHDSRVK VVFELADGSR IHRLPAWIKR ATQPSKETAK EWGPSYEARF WNPASPYKFK
     HERPRLDPNV ESLRIYEAHV GISTPEPRVG SYSEFTKDVL PRIRDLGYNA IQLMAIMEHA
     YYASFGYQVT NFFAVSSRYG TPEELKELID TAHGMGIQVL LDVVHSHASK NVSDGLNMFD
     GTDYQYFHSI SSGRGEHPLW DSRLFNYGSF EVQRFLLANL AFYIDVYQFD GFRFDGVTSM
     LYHHHGVGER GAFSGDYNEY LSDHSGVDHE ALAYLMLAND LIHDMLPANG VTVAEDVSGY
     PTLCLPRSVG GCGFDYRLAM ALPDMWIKLL KESKDEDWSM GHIVYTLVNR RYKEKVVAYA
     ESHDQALVGD KTLAFWMMDA AMYTDMTVLK ELTPVVDRGI ALHKLIRLIT HSLGGESYLN
     FEGNEFGHPE WLDFPNANNG DSYQYARRQF NLVDDGLLRY KHLYAFDKAM QEAEGKHKWL
     NTPQAYVSLK HETDKVISFE RNGLVFIFNF HPTQSFTDYR IGVDEAGAYR IILNSDREEF
     GGHRRIEEEN SVFHTTDLEW NGRRNFIQVY LPSRTALVLA RNP
//

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