ID L0KAG2_HALHC Unreviewed; 550 AA.
AC L0KAG2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=Halha_1144 {ECO:0000313|EMBL:AGB41093.1};
OS Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Halobacteroides.
OX NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB41093.1, ECO:0000313|Proteomes:UP000010880};
RN [1] {ECO:0000313|Proteomes:UP000010880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC {ECO:0000313|Proteomes:UP000010880};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Halobacteroides halobius DSM 5150.";
RL Submitted (FEB-2012) 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; CP003359; AGB41093.1; -; Genomic_DNA.
DR RefSeq; WP_015326818.1; NC_019978.1.
DR AlphaFoldDB; L0KAG2; -.
DR STRING; 748449.Halha_1144; -.
DR KEGG; hhl:Halha_1144; -.
DR PATRIC; fig|748449.3.peg.1103; -.
DR eggNOG; COG1543; Bacteria.
DR HOGENOM; CLU_008192_1_0_9; -.
DR OrthoDB; 9803279at2; -.
DR Proteomes; UP000010880; 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:UP000010880}.
FT DOMAIN 10..402
FT /note="Glycoside hydrolase family 57 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03065"
FT DOMAIN 430..530
FT /note="1,4-alpha-glucan branching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09210"
FT ACT_SITE 192
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT ACT_SITE 356
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 410
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 550 AA; 64455 MW; 910CB9BF925E4DFE CRC64;
MGEEKGYLSL VLHAHLPYVR HPEHEEFMEE KWLFEAITET YIPLLDHFES LHKDGIDYRL
TMSLTPPLIS MLTDSLLQKR YLRHLDKLIE LAYKEITRTK NRPKLNKTAY HYLNRFKKSR
EIFTDYYDCN LVKGFKKFQD LGYLEIITCG ATHGYLPLMQ QYPEAVRAQI EVAINTHKKH
LGQAPRGIWL PECAYYPGVD KILKEYGIKF FVVDTHGILH AKPRPKYGVF SPIYTESGVA
AFARDQESSR QVWSSKSGYP GDHNYREFYR DIGFDAPLDY IEPYINPDGI RMNTGIKYYK
ITGDKTSLDN KEPYDYEVAL ERTANHAGDF LSRRIEQIEH LDNLMDRKPV ILSPYDAELF
GHWWYEGPDF LNYLIRKTAC DQDKVKLISP VDYLEEYPKN QVCQPPMCSW GANGYNDVWL
DDSNDWIYRH LHQATEKMIE LATDIDNPAH CTERALNQMA RELLLAQSSD WAFIMMTGTT
VEYAVYRTKA HIHRLSKLYD QIKTGTVDQD WLAELEWKDN IFPEIDYKVY SQDHQVQIKG
ECEEIEIIAT
//
