ID A0A1I3SYX0_9BACL Unreviewed; 951 AA.
AC A0A1I3SYX0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=1,4-alpha-glucan branching enzyme {ECO:0000313|EMBL:SFJ64048.1};
GN ORFNames=SAMN05518846_104357 {ECO:0000313|EMBL:SFJ64048.1};
OS Brevibacillus centrosporus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54910 {ECO:0000313|EMBL:SFJ64048.1, ECO:0000313|Proteomes:UP000198915};
RN [1] {ECO:0000313|Proteomes:UP000198915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK042 {ECO:0000313|Proteomes:UP000198915};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family.
CC {ECO:0000256|ARBA:ARBA00006821, ECO:0000256|RuleBase:RU361196}.
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DR EMBL; FORT01000004; SFJ64048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3SYX0; -.
DR STRING; 1884381.SAMN05518846_104357; -.
DR Proteomes; UP000198915; Unassembled WGS sequence.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:InterPro.
DR GO; GO:0030979; P:alpha-glucan biosynthetic process; IEA:InterPro.
DR CDD; cd10792; GH57N_AmyC_like; 1.
DR CDD; cd03801; GT4_PimA-like; 1.
DR Gene3D; 1.20.1430.10; Families 57/38 glycoside transferase, middle domain; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR InterPro; IPR037090; 57_glycoside_trans_central.
DR InterPro; IPR015293; BE_C.
DR InterPro; IPR040042; Branching_enz_MT3115-like.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR004300; Glyco_hydro_57_N.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR PANTHER; PTHR41695; 1,4-ALPHA-GLUCAN BRANCHING ENZYME RV3031-RELATED; 1.
DR PANTHER; PTHR41695:SF1; 1,4-ALPHA-GLUCAN BRANCHING ENZYME RV3031-RELATED; 1.
DR Pfam; PF09210; BE_C; 1.
DR Pfam; PF03065; Glyco_hydro_57; 1.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361196};
KW Reference proteome {ECO:0000313|Proteomes:UP000198915}.
FT DOMAIN 8..324
FT /note="Glycoside hydrolase family 57 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03065"
FT DOMAIN 423..530
FT /note="1,4-alpha-glucan branching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09210"
FT DOMAIN 569..743
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13439"
FT DOMAIN 753..918
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT ACT_SITE 188
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT ACT_SITE 349
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
SQ SEQUENCE 951 AA; 109101 MW; 6523B1B4D71508B9 CRC64;
MNNGYLSLVL HAHLPYVRHG ERDDYLEERW VYEAMLETYL PLLMVFDKLL ADGIDFRMTL
AVSPTLLSMI DDELIQSRFQ THLAKTVELA GKEVKRTMNA PRENRVAKMY LERFREIATY
CRKLDFQLIS GLKRAQESGC LELITCAATH AFLPYVETEE AIRAQLLAGI ETHERILGKR
PNGIWLPECG FTPGLDRLLK EVGLHYFFVD SHTISHATPT PMRGLYAPLQ TPYDVAAFAR
DEQASRQVWS SFDGYPGDFD YREYYRDIGF DREMDYIAPY IHPEGIRVNT GLKYYRITGK
TGQKDWYEPD WAREKAASHA GHFLYHRERQ VEEASSWLDR EPLVVATYDA ELFGHWWYEG
PLFLDFLLRK TVCDSQHVQL ITPSEYLAKY PAQDRARLPM STWGRNGYGE VWLNEKNGWM
YRHLHQAERD LIAAVHSCEI AKGQNVKKDA WVSRCLKQAA RELMLAQSSD WAFILDGQTV
VDYAVRRFHD HLVRLRELLD MIHTDQQNDA RLVEMEKAYP IFPTMDESYY LPFHSHRVNV
SHQMVAATDY QQAKRKVLML SWEFPPHVVG GLGRAVFDLA RELVRQGTEV HVLTAAAHAE
AGQEMVDGIY VHRLNGYAGS EQGDFLQWVF QLNLAMVDKA EQLSREGLRV DIVHGHDWLV
SWAAMEIKER MAIPLITTIH ALEHGRHQGI HTPLQQRIHE SEHALVSVSD HVIVCSHYMR
GEVQKLFGVP DEKIQVIYNG VELPEDTSVQ EAELRQELSL GEGPILFFVG RLVREKGVHL
LLEAVSRLAW EFPDVRVVIA GKGPSAAELM SLSEQLHIVD KVRFLGFVHD ERRNQLFRMA
DVAVFPSLYE PFGIVALEAM AFGTPLLVAD TGGLREIVRH GENGAMMYAG HVDSLVDQLR
WLLSDPDMRH KLAQRAKADV QQNYDWAKLA AQTAELYHQF TIASKWTATA T
//