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Database: UniProt
Entry: A0A0Q3LY33_AMAAE
LinkDB: A0A0Q3LY33_AMAAE
Original site: A0A0Q3LY33_AMAAE 
ID   A0A0Q3LY33_AMAAE        Unreviewed;       682 AA.
AC   A0A0Q3LY33;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE            EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN   ORFNames=AAES_145717 {ECO:0000313|EMBL:KQK75391.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK75391.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK75391.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK75391.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000256|ARBA:ARBA00009000}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQK75391.1}.
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DR   EMBL; LMAW01002942; KQK75391.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3LY33; -.
DR   Proteomes; UP000051836; 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:InterPro.
DR   CDD; cd11321; AmyAc_bac_euk_BE; 1.
DR   CDD; cd02854; E_set_GBE_euk_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
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; 2.
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:UP000051836};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          174..592
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        365
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        420
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   682 AA;  79074 MW;  20C5B9B2FFE2EE87 CRC64;
     MLLLFYKTFY DRYSLFYNHL KNIEENEGGL DKFSKSYKTF GVNXLADGGI YCKEWAPGAE
     AVFLAGDFND WNPFSHPYKK MEYGKWELLI PPGQDGCPLV PHGSRLKVVI RAQNGDLLYR
     ISPWARYVIR DEDKVNYDWV HWNPPQSYVH KHPSPKRLKS LRIYESHVGI ASPEGKVASY
     KNFTYNVLPR IKDLGYNCVQ LMAIMEHAYY ASFGYQVTSF FAASSRYGTP DDLKEMIDVA
     HSMGITVLLD VVHSHASKNS EDGLNKFDGT DSCFFHSGPK GTHQLWDSRL FDYAKYVFVG
     EIDALAIIPG RLKIIHAVKE LSQFYAXQKC ERMLGYNLSW EVLRFLLSNL RMWIEDYRFD
     GFRFDGVTSM LYHHHGIGTG FSGDYNEYFG LHVDEDALCY LMLANHMIKF LHPECITIAE
     DVSGMPALCR PVEEGGGGFD YRLAMAIPDK WIQIIKELKD EDWNMGNIVH TLTNRRYEEK
     YIAYAESHDQ ALVGDKTLAF RLMDAEMYTN MSVLSPLTAV IDRGIQLHKM IRLITHALGG
     ESYLNFMGNE FGHPEWLDFP RIGNNESYHY ARRQFNLTED HLLRYRFLNA FDRDMNKLEE
     RFGWLASPPL EMKYFLNFIL IFISEAYVSE KHEANKVIAF ERAGLLFVFN FHPYQSYVDY
     RVGIADPGKY PFLYCFACTE KL
//
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