ID   GLGB_DEBHA              Reviewed;         711 AA.
AC   Q6BXN1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=DEHA2B01672g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   ---------------------------------------------------------------------------
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; CR382134; CAG85024.1; -; Genomic_DNA.
DR   RefSeq; XP_457038.1; XM_457038.1.
DR   AlphaFoldDB; Q6BXN1; -.
DR   SMR; Q6BXN1; -.
DR   STRING; 4959.XP_457038.1; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q6BXN1; -.
DR   EnsemblFungi; CAG85024; CAG85024; DEHA2B01672g.
DR   GeneID; 2913696; -.
DR   KEGG; dha:DEHA2B01672g; -.
DR   VEuPathDB; FungiDB:DEHA2B01672g; -.
DR   eggNOG; KOG0470; Eukaryota.
DR   HOGENOM; CLU_011131_2_2_1; -.
DR   InParanoid; Q6BXN1; -.
DR   OMA; FGMKWMM; -.
DR   OrthoDB; 165238at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000599; Chromosome B.
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   3: Inferred from homology;
KW   Glycogen biosynthesis; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..711
FT                   /note="1,4-alpha-glucan-branching enzyme"
FT                   /id="PRO_0000188781"
FT   ACT_SITE        353
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        414
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   711 AA;  82021 MW;  6900A02ECB5E9D61 CRC64;
     MSLSTGSTGS ERSNQSLIKG ALDLDPWLEP FSGQLIHRQL NLRKWYDEFK QNEGSLTNFA
     SAYEKYGLHA NWDTKEVFIN EYIPNVVEVS LVGDFNNWDT NTHKLKPVND FGLWSLTIKP
     TENNEFAVPH DSRYKISMVT ASGERIYRLC PWLKRATPST ENNLYEGRFW NPQPTETYKF
     KHERPRLESK DGIKIYEAHV GISTPEPKVG SYKNFTTKVL PVIHKLGYNT IQLMAVMEHA
     YYASFGYQVT NFFAISSRFG TPEDLKELID EAHRLGIRVL LDVVHSHSSK NVEDGLNMFN
     GTDHYLFHGG TKGSHELWDS RLFNYSNYET LRFLLSNLRF YIDVFKFDGF RFDGVTSMLY
     KHHGLSFGFS GDYNEYFNSE WVDNDAITYL MLGHKLLDEI SVRENNYKFV SIAEDVSGMP
     TLCLPIGQGG IGFDYRLSMA IPDMWIKIIK HLSDEEWDMG SLVHTLTNRR HGERCISYCE
     SHDQALVGDK TIAFWLMDKE MYTNMSTLTP FTPVIDRGIA LHKMIRLITF SLGGEGYLNF
     EGNEFGHPEW LDFPRKGNGE SYAYARRQFN LIEDDLLRYK FLFAFDGAMQ HLDTKYGILL
     SSQAYVSLKN ENDKVIVFER NGLLFIFNFH PTNSYADYKI GVETPGVYQI VLNSDSLSFG
     GHGRIEETNK ETGEKLQFFT NNERWNDRSN ALFCYIPSRT AIVLQVKEKV V