ID F1SK65_PIG Unreviewed; 694 AA.
AC F1SK65;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 5.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN Name=GBE1 {ECO:0000313|Ensembl:ENSSSCP00000012785.5,
GN ECO:0000313|VGNC:VGNC:88374};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000012785.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000012785.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000012785.5,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000012785.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; F1SK65; -.
DR PeptideAtlas; F1SK65; -.
DR Ensembl; ENSSSCT00000013131.5; ENSSSCP00000012785.5; ENSSSCG00000012000.5.
DR VGNC; VGNC:88374; GBE1.
DR eggNOG; KOG0470; Eukaryota.
DR GeneTree; ENSGT00390000017040; -.
DR HOGENOM; CLU_873027_0_0_1; -.
DR TreeFam; TF300783; -.
DR Proteomes; UP000008227; Chromosome 13.
DR Bgee; ENSSSCG00000012000; Expressed in omentum and 44 other cell types or tissues.
DR ExpressionAtlas; F1SK65; baseline and differential.
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; 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 1: Evidence at protein level;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1SK65};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 203..568
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 357
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 412
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 694 AA; 79833 MW; 9565208D90533697 CRC64;
MAASAGAPAP AEGSEEALAS ALADVPELAR LLETDPYLKP YAPDFQRRYK RFNQTLTNFG
ENEGGIDKFS RGYESFGIHR CADGGLYCKE WAPGAEGVFL TGDFNDWNPF SYPYKKLDFG
KWELYIPPKQ NRSVLVPHGS KLKIVIRSKS GEILYRISPW AKYVTREGDN VNYDWTHWDP
EHPYKFKHSK PKKPKGPRIY ESHVGISSYE GKIASYKHFT CNVLPRIKDL GYNCIQLMAI
MEHAYYASFG YQITSFFAAS SRYGTPEELK ELVDTAHSMG ITVLLDLVHS HASKNSEDGL
NMFDGTESCY FHYGPRGNHN LWDSRLFDYS SWEVLRFLLS NIRWWLEEYG FDGFRFDGVT
SMLYYHHGIG QSFSGDYHEY FGLHVDEEAL TYLMLANHLI HTLYPDSITI AEDVSGMPTL
CSPISQGGSG FDYRLAMAIP DKWIQLLKEF KDEDWNMGNI VYTLTNRRHL EKSIAYAESH
DQALVGDKTL AFWLMDAEMY TNMSVLTPFT PVIDRGIQLH KMIRLITHTL GGEGYLNFMG
NEFGHPEWLD FPRKGNDESY HYARRQFHLT DDDLLRYKFL NNFDRDMNKL EERCGWLSAP
QAHVSEKHET NKVIAFERAG LLFVFNFHPS KSYTDYRVGT TLPGKFKIVL DSDAAEYGGH
QRLDHNTDFF SEPFEHNKRP YSLLMPLAIL SAID
//
