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Database: UniProt
Entry: J7R9R0_KAZNA
LinkDB: J7R9R0_KAZNA
Original site: J7R9R0_KAZNA 
ID   J7R9R0_KAZNA            Unreviewed;       704 AA.
AC   J7R9R0;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=KNAG0H01860 {ECO:0000313|EMBL:CCK71600.1};
GN   OrderedLocusNames=KNAG_0H01860 {ECO:0000313|EMBL:CCK71600.1};
OS   Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS   17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS   naganishii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK71600.1, ECO:0000313|Proteomes:UP000006310};
RN   [1] {ECO:0000313|EMBL:CCK71600.1, ECO:0000313|Proteomes:UP000006310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC   / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2] {ECO:0000313|Proteomes:UP000006310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC   / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Kazachstania naganishii.";
RL   Submitted (AUG-2012) 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; HE978321; CCK71600.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7R9R0; -.
DR   STRING; 1071383.J7R9R0; -.
DR   eggNOG; KOG0470; Eukaryota.
DR   HOGENOM; CLU_011131_2_2_1; -.
DR   OMA; YEMHLGS; -.
DR   OrthoDB; 96at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000006310; Chromosome 8.
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   Reference proteome {ECO:0000313|Proteomes:UP000006310};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          219..573
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        356
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        417
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   704 AA;  81273 MW;  A2ABD1F6A5853A0F CRC64;
     MFNVPENVKA CVEIDPWLKP YAQVLSERRY LADKFYYDIT HATADGSEQT LSKFARDAYK
     SYGLHANPQT KEITYKEWAP NAKNAFLVGD FNNWDKYATQ MTGKDEFGNF YLTLPPTDQN
     EFAIPHDSKL KVMFQLEDNS EIFRIPAWIT RATQPSKETK EQFGPAYEGR FWNPPEQYQF
     RHERPTFNES RDSLRIYEAH IGISSPDPKV TSYKEFTANI LPRIQYLGYN CIQLMAIMEH
     AYYASFGYQV TNFFAASSRF GTPEELKELI DTAHGMGILV LLDVVHSHAS KNVEDGLNNF
     DGSDHQYFHS IASGRGEHPL WDSRLFNYGS FDVQRFLLAN LAFYIDVYQF DGFRFDGVTS
     MLYLHHGVGA GGAFSGDYDE YLSKERSAVD HEALAYLMLA NDLVHELLPE SAITVAEDVS
     GYPTLCLPRH TGGAGFDYRL AMALPDMWIK ILKEKSDEEW DMANIVYTLT NRRYAEKVVA
     YAESHDQALV GDKTLAFWLM DAAMYTDMTV LKQSTPVIDR GIALHKMIRL LTHALGGEAY
     LNFEGNEFGH PEWLDFPNAN NGDSYHYARR QFNLVDDNLL RYKFLNDFDR AMQLCERDHQ
     WLNTPQAYVS LKHEVDKVVA FERNGLLFIF NFHPTNSFTD YRIGVDQPGT YRIVLNSDRE
     EYGGHNRIDE NVRFHTSDLE WNNRRNFVQV YIPNRTAIIL ARDQ
//
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