ID F6ZHD8_MOUSE Unreviewed; 702 AA.
AC F6ZHD8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 2.
DT 27-MAR-2024, entry version 78.
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:ENSMUSP00000131320.3,
GN ECO:0000313|MGI:MGI:1921435};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000131320.3, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000131320.3, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131320.3,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000131320.3}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131320.3};
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 ProteomicsDB; 335289; -.
DR Antibodypedia; 32014; 420 antibodies from 28 providers.
DR Ensembl; ENSMUST00000023393.15; ENSMUSP00000023393.9; ENSMUSG00000022707.17.
DR Ensembl; ENSMUST00000170464.3; ENSMUSP00000131320.3; ENSMUSG00000022707.17.
DR AGR; MGI:1921435; -.
DR MGI; MGI:1921435; Gbe1.
DR VEuPathDB; HostDB:ENSMUSG00000022707; -.
DR GeneTree; ENSGT00390000017040; -.
DR OMA; YEMHLGS; -.
DR ChiTaRS; Gbe1; mouse.
DR Proteomes; UP000000589; Chromosome 16.
DR Bgee; ENSMUSG00000022707; Expressed in intercostal muscle and 230 other cell types or tissues.
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|EPD:F6ZHD8,
KW ECO:0007829|MaxQB:F6ZHD8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 221..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 702 AA; 80337 MW; BE3D9BA5D1C8C060 CRC64;
MAAPAAPAAG ETGPDARLEA ALADVPELAR LLEIDPYLKP FAADFQRRYK KFSQVLHDIG
ENEGGIDKFS RGYESFGIHR CSDGGIYCKE WAPGAEGVFL TGEFSGWNPF SHPYKKLEYG
KWELYIPPKQ NKSPLIPHGS KLKVVITSKS GEILYRISPW AKYVVRENNN VNYDWIHWAP
EDPYKFKHSR PKKPRSLRIY ESHVGISSHE GKIASYKHFT SNVLPRIKDL GYNCIQLMAI
MEHAYYASFG YQITSFFAAS SRYGTPEELK ELVDTAHSMG IVVLLDVVHS HASKNSEDGL
NMFDGTDSCY FHSGPRGTHD LWDSRLFIYS SWEVLRFLLS NIRWWLEEYC FDGFRFDGVT
SMLYHHHGMG QGFSGDYNEY FGLQVDEDAL IYLMLANHLA HTLYPDSITI AEDVSGMPAL
CSPTSQGGGG FDYRLAMAIP DKWIQLLKEF KDEDWNMGNI VYTLTNRRYL EKCVAYAESH
DQALVGDKTL AFWLMDAEMY TNMSVLAPFT PVIDRGIQLH KMIRLITHGL GGEGYLNFMG
NEFGHPEWLD FPRKGNNESY HYARRQFNLT DDDLLRYKFL NNFDRDMNRL EERCGWLSAP
QAYVSEKHEA NKTITFERAG LLFIFNFHPS KSYTDYRVGT ATPGTFKIVL DSDAAEYGGH
QRLDHNTNYF AEAFEHNGRP YSLLVYIPSR VALILQNVDL QN
//
