ID L5MIU3_MYODS Unreviewed; 761 AA.
AC L5MIU3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=MDA_GLEAN10006318 {ECO:0000313|EMBL:ELK38222.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK38222.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 EMBL; KB099156; ELK38222.1; -; Genomic_DNA.
DR AlphaFoldDB; L5MIU3; -.
DR eggNOG; KOG0470; Eukaryota.
DR Proteomes; UP000010556; 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:0005975; P:carbohydrate metabolic 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 207..551
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 642..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 86152 MW; BE6071E4B9C3BEFC CRC64;
MTGVGNLVLV VEVLPAPMGP NKSRSTVGWW SRYKRFIQTL ENIGENEGGI DKFSRGYESF
GVHRCADGGL YCKEWAPGAE GVFLTGDFND WNPFSYPYKK LEYGKWELYI PPKQDKSVIP
HGSKLKVVIR SKSGEILYRI SPWAKYVARE GDNVNYDWIH WDPEHTYKFK HSRPKKPRGL
RIYESHVGIS SHEGKVASYK HFTCNILPRI KDLGYNCIQL MAIMEHAYYA SFGYQITSFF
AASSRYGTPE ELKELVDTAH SMGIIVLLDM VHSHASKNSE DGLNMFDGTD SCYFHSGPRG
NHDLWDSRLF AYSSWEVLRF LLSNIRWWLE EYGFDGFRFD GVTSMLYHHH GMGQGFSGDY
HEYFGLQVDE DALIYLMLAN HLVHMLYPDS ITIAEDVSGM PAVCCPISQG GCGFDYRLAM
AIPDKWIKLL KEFKDEDWNM GDIVHTLTNR RYLEKCIAYA ESHDQALVGD KTLAFWLMDA
EMYTNMSVLT PFTPVIDRGI QLHKMIRLIT HALGGEGYLN FMGNEFGHPE WLDFPRKGNN
ESYHYARRQF HLTDDDLLRY KFLNNFDREM NQLEERCGWL SAPQAYVSEK HEANKVIAFE
RADLLFIFNF HPTKSYTDYR VGTKSLGKYP FCWAQRVKSH KTQDPTSIVR NSGESQSPAR
LAGTTQKNFP EFRPVAGATG LPDAPPCQVP AGTAGGGTQK QSAAASTATV GGETQKLACS
TSRIQKPNRL QSSPPESSPR PPGTAHSPTH LHAPAAHAAS C
//
