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Database: UniProt
Entry: A0A1I3SYX0_9BACL
LinkDB: A0A1I3SYX0_9BACL
Original site: A0A1I3SYX0_9BACL 
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
//
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