ID A4J6Y2_DESRM Unreviewed; 537 AA.
AC A4J6Y2;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=(1->4)-alpha-D-glucan branching enzyme {ECO:0000313|EMBL:ABO50835.1};
GN OrderedLocusNames=Dred_2325 {ECO:0000313|EMBL:ABO50835.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50835.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO50835.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50835.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) 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; CP000612; ABO50835.1; -; Genomic_DNA.
DR RefSeq; WP_011878633.1; NC_009253.1.
DR AlphaFoldDB; A4J6Y2; -.
DR STRING; 349161.Dred_2325; -.
DR CAZy; GH57; Glycoside Hydrolase Family 57.
DR KEGG; drm:Dred_2325; -.
DR eggNOG; COG1543; Bacteria.
DR HOGENOM; CLU_008192_1_0_9; -.
DR OrthoDB; 9803279at2; -.
DR Proteomes; UP000001556; Chromosome.
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 Gene3D; 1.20.1430.10; Families 57/38 glycoside transferase, middle domain; 1.
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 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 SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361196};
KW Reference proteome {ECO:0000313|Proteomes:UP000001556}.
FT DOMAIN 8..323
FT /note="Glycoside hydrolase family 57 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03065"
FT DOMAIN 425..525
FT /note="1,4-alpha-glucan branching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09210"
FT ACT_SITE 189
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT ACT_SITE 352
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
SQ SEQUENCE 537 AA; 62747 MW; D9F3A22E4606C40C CRC64;
MTKGYLSIVL HAHLPYVRHP ESEKYLEENW FYEALTETYI PLLDVFNRLA GENVPFRLTF
SISPPLLSML MDPLLQGRYV RHLKKLMELA EKEEVRTRDG HFNSAALMYK ERFQRAYHIF
VHENNCNLVN AFKQLQDRGF LDITTCAATH GFLPIMMTNP EAVRAQIDTA VNLHKKHLGR
APEGIWLPEC GYSPGIDENL KEYGLKYFFT DSHGLLYAYH RPRFANYAPV YCPSGVAAFA
RDIESSKQVW SADEGYPGDA DYREFYRDIG YDLDYEYIKE YIHPDGIRVH TGLKYHRITG
KVDLSHKQPY YPEWASRKAE IHAGNFLFNR EKQVEYLSSI MERHPIIVAP YDAELFGHWW
FEGPQWLEFL IRKMASNQSL KLITPMDYLK QYKVNQVTTP CSSTWGDAGY NGVWLNEKNH
WIYRHLHMAA DRMTELADMF PQANGNLRRA LNQAGRELLL AQSSDWAFII ATGTMVSYAI
RRTKQHLANF LRLYDDIKYC RIDEGFVSHL EWQNNIFPDI DYRSWRSRDA GQQAAIS
//
