ID A0A0H5C7P8_CYBJN Unreviewed; 685 AA.
AC A0A0H5C7P8; A0A1E4RV26;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 Name=GLC3 {ECO:0000313|EMBL:CEP24191.1};
GN ORFNames=BN1211_4943 {ECO:0000313|EMBL:CEP24191.1}, CYBJADRAFT_195401
GN {ECO:0000313|EMBL:ODV70925.1};
OS Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=983966 {ECO:0000313|EMBL:CEP24191.1, ECO:0000313|Proteomes:UP000038830};
RN [1] {ECO:0000313|EMBL:CEP24191.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS1600 {ECO:0000313|EMBL:CEP24191.1};
RA Jaenicke S.;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000038830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC NRRL Y-1542 {ECO:0000313|Proteomes:UP000038830};
RX PubMed=26150016; DOI=10.1016/j.jbiotec.2015.06.423;
RA Rupp O., Brinkrolf K., Buerth C., Kunigo M., Schneider J., Jaenicke S.,
RA Goesmann A., Puehler A., Jaeger K.-E., Ernst J.F.;
RT "The structure of the Cyberlindnera jadinii genome and its relation to
RT Candida utilis analyzed by the occurrence of single nucleotide
RT polymorphisms.";
RL J. Biotechnol. 211:20-30(2015).
RN [3] {ECO:0000313|EMBL:ODV70925.1, ECO:0000313|Proteomes:UP000094389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389}, and NRRL Y-1542
RC {ECO:0000313|EMBL:ODV70925.1};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; CDQK01000005; CEP24191.1; -; Genomic_DNA.
DR EMBL; KV453947; ODV70925.1; -; Genomic_DNA.
DR RefSeq; XP_020067964.1; XM_020217558.1.
DR STRING; 983966.A0A0H5C7P8; -.
DR GeneID; 30991954; -.
DR OMA; YEMHLGS; -.
DR OrthoDB; 96at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000038830; Unassembled WGS sequence.
DR Proteomes; UP000094389; 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:ODV70925.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094389};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 158..554
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 398
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 685 AA; 78577 MW; C957E840481B69A5 CRC64;
MSENNVPESV AGAIRDDPWL TPFAHELARR RHAADEWLKT FEQNEGGILS VADGYKTYGF
HEDGTGVHYK EWAPNATQAF LVGDFNDWQF DKEMQKDDFG NFSITLPKGS IPHDSRVKIV
LTLPSGERVY RLPAWITRCT PPPKETKSVS YEARFWNPEH PYQFVNQRPY PSESLRIYEA
HVGISTPEPR IGTYKEFTQN VLPRVKDLGY NAIQLMAIME HAYYASFGYQ VTSFFAASSR
YGTPEDLKEL IDTAHGLGIV VLLDVVHSHA SKNVDDGLNN FDGTEWQYFH SGGKGDHPLW
DSKLFNYGKY EVLRFLLSNL KFYLDVYKFD GFRFDGVTSM LYLHHGVGAG GAFSGDYNEY
LHENSPVDKE ALTYLMLAND LITKVAEKEG TKFISIAEDV SGMPTLGVTR KDGGVGFDYR
LAMALPDMWI KLLKESKDED WDLNKIVHTL TNRRYAERAI AYAESHDQAL VGDKTLAFWL
MDAEMYTNMS VLSPLTPVID RGLALHKIIR LLTHSLGGEG YLNFEGNEFG HPEWLDFPNI
NNGDSYHYAR RQFNLIEDDL LRYKFLYRFD RAMQHLEAKY GWLHKKDQYI SLKNESDKVL
VYEKGGLLFI YNFHHSNSYT DYRCGVEVAG KYKIVLNSDD EEFGGHARVS PDQEFFTTDL
EWNNRKNFIQ VYIPNRTVLV LALAD
//
