ID   GLGB_CRYNB              Reviewed;         682 AA.
AC   P0CN83; Q55ZX8; Q5KP87;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=CNBA3620;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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}.
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DR   EMBL; AAEY01000002; EAL23246.1; -; Genomic_DNA.
DR   RefSeq; XP_777893.1; XM_772800.1.
DR   AlphaFoldDB; P0CN83; -.
DR   SMR; P0CN83; -.
DR   EnsemblFungi; AAW40900; AAW40900; CNA03810.
DR   GeneID; 4933620; -.
DR   KEGG; cnb:CNBA3620; -.
DR   VEuPathDB; FungiDB:CNBA3620; -.
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   3: Inferred from homology;
KW   Glycogen biosynthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..682
FT                   /note="1,4-alpha-glucan-branching enzyme"
FT                   /id="PRO_0000410096"
FT   ACT_SITE        342
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        397
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   682 AA;  78344 MW;  AD1D30BE01EB496F CRC64;
     MTAVSLSDGT AVLKTDPWLE PFSGALRERY AAYQKQRTII EEHEGGLAEF SKGYKSMGFQ
     IDKNGGVRYR EWASNATEAR LIGEFNNWSH TANPMTKSPF GVWECYVPPV SPGVCAIPHD
     SMVKISMTLP GGESIDRIPT WITRVTQDLN ISPIYDGRFW NPPKEQQYQF KHGHSTRPVE
     GLKIYEAHVG ISSPNMRVTT YKEFEVDVLP KIKQLGYNCI QMMAIMEHAY YASFGYQVTN
     FFAASSRFGT PEELKSLVDK AHELGLTVLL DVVHSHASKN ILDGINMYDG SDHLYFHEGG
     RGRHDQWDSR LFNYGQHEVL RFLLSNLRFW MDIYMFDGFR FDGVTSMMYK HHGIGSGFSG
     GYHEYFGDSV DLEAMVYLML ANAMLHETYP HVVTIAEDVS GMPTLCRPVA EGGVGFDYRL
     SMAIPDMWIK LLKEYTDDQW EMGQIVHNLT NRRHLEKSVA YAESHDQALV GDKTLAFWLM
     DKEMYDFMSD LSPLTPIIDR GLALHKMIRF IVHTLGGEAY LNFEGNEFGH PEWMDFPREG
     NGNSFAHARR QFNLVDDKLL RYKYLYEFDV AMNWLEDKYK WLNSPQAYVS LKHEGDKMIV
     FERAGLLFIF NFHPTQSFTD YRVGVDTAGE YKVILTSDET RFGGHNRIDM GGRYFTTPME
     WNGRKNWLQV YSPSRTVLVL GL
//