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Database: UniProt
Entry: A0A0J0XWG8_9TREE
LinkDB: A0A0J0XWG8_9TREE
Original site: A0A0J0XWG8_9TREE 
ID   A0A0J0XWG8_9TREE        Unreviewed;       691 AA.
AC   A0A0J0XWG8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=CC85DRAFT_306626 {ECO:0000313|EMBL:KLT45406.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT45406.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT45406.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT45406.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KQ087181; KLT45406.1; -; Genomic_DNA.
DR   RefSeq; XP_018281897.1; XM_018425702.1.
DR   AlphaFoldDB; A0A0J0XWG8; -.
DR   SMR; A0A0J0XWG8; -.
DR   STRING; 879819.A0A0J0XWG8; -.
DR   GeneID; 28986305; -.
DR   OrthoDB; 96at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000053611; Unassembled WGS sequence.
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   Hydrolase {ECO:0000313|EMBL:KLT45406.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          207..570
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        351
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        406
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   691 AA;  78469 MW;  46807E68B2BB0E2F CRC64;
     MATQTNNGSK TSMMPDDGTG VIQTDPWLEP FAPAIRNRYA GYKKALDFIN QNEGGLDKFS
     QGYKTLGFTV DDKGGVTYRE WAPGAAEARL IGEFNGWSHT ANPMTKSQFG VWECYVPPKS
     PGVPAIPHDS MVKISMTTPS GESLDRLPAW ITRVTQDLNV SPIYDARFWN PPAAETYKFK
     HGHSTNPIEG LKIYEAHVGI SSPAQRVTTY KEFEDDVLPR IKALGYNTIQ MMAVMEHAYY
     ASFGYQVTSF FAASSRYGTP EELKSLIDKA HGMGITVLLD VVHSHACKNV LDGLNMFDGT
     DHCYFHEGAR GRHDLWDSRL FNYGHPEVQR FLLSNLRYWM DEYKFDGFRF DGVTSMMYKH
     HGMGVGFSGG YHEYFGDDVD LEAMTYLMLA NKMIHDLYPQ AITIAEDVSG MPTLCRPVAE
     GGVGFDYRLS MAIPDMWIKI LKEKSDDEWD MGNIVHTLTN RRHQERSVAY AESHDQALVG
     DKTLAFWLMD KEMYDFMSVL SPLTPIIDRG LALHKMIRFV THALGGEAYL NFEGNEFGHP
     EWMDFPREGN GNSFAHARRQ FNLVDDDLLR YKFLNNFDGA MNNLESKYRW LSAPQAYVSL
     KHEGDKVIVF ERAGLLFIFN FHPTNSFTDY RVGVDQPGKY HVVLNTDDEA FGGHARVAKE
     GEYFTTDMEW NGRRNFLQVY IPSRTALVLS L
//
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