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
//