GLGB_SALRD
ID GLGB_SALRD Reviewed; 622 AA.
AC Q2S4A0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000255|HAMAP-Rule:MF_00685};
DE EC=2.4.1.18 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE Short=BE {ECO:0000255|HAMAP-Rule:MF_00685};
GN Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=SRU_0846;
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Salinibacter.
OX NCBI_TaxID=309807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31;
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages
CC in glycogen by scission of a 1,4-alpha-linked oligosaccharide from
CC growing alpha-1,4-glucan chains and the subsequent attachment of the
CC oligosaccharide to the alpha-1,6 position. {ECO:0000255|HAMAP-
CC Rule:MF_00685}.
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:0000255|HAMAP-Rule:MF_00685};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00685}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00685}.
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DR EMBL; CP000159; ABC44792.1; -; Genomic_DNA.
DR RefSeq; WP_011403610.1; NC_007677.1.
DR RefSeq; YP_444981.1; NC_007677.1.
DR AlphaFoldDB; Q2S4A0; -.
DR SMR; Q2S4A0; -.
DR STRING; 309807.SRU_0846; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABC44792; ABC44792; SRU_0846.
DR KEGG; sru:SRU_0846; -.
DR PATRIC; fig|309807.25.peg.872; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_10; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000008674; Chromosome.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-UniRule.
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:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02855; E_set_GBE_prok_N; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR HAMAP; MF_00685; GlgB; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
DR InterPro; IPR006407; GlgB.
DR InterPro; IPR044143; GlgB_N_E_set_prok.
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; PTHR43651; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF02922; CBM_48; 1.
DR PIRSF; PIRSF000463; GlgB; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR01515; branching_enzym; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..622
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260696"
FT REGION 581..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 306
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 622 AA; 71450 MW; D14B40C53CD8B114 CRC64;
MPHLTDDDIY YWRQGTHTHS YERMGAHPNQ RGTWFGVWAP NADRVEVTGD FNDWRFGADV
LDRREGGLWE GYVRGAQPGD KYKYHLRAGG EWFDRTDPYA FRMEPPAQNT YEGLSALITD
LDTYTWGDDA WMTTREGPSG IDGPLSIYEV HLGSWRHEEH GASLSYREVA EPLADHVQNL
GFTHVEFLPL AEHPYYGSWG YQILGYYAPT FRYGDPEGLM HLIDTLHQRG IGVIMDWVPG
HFATDPQGLT YFDGSHLFEY EDPLMREHPD WGTRVFDFGK NGVRNFLLSN ALFWMDKYHV
DGLRVDAVAS MLYRDYSREG DWSPNVHGGR ENLGAISLLQ DTNEHVYDEY PEAIMLAEES
TAWPGVTTPT EHGGLGFLYK WNMGWMHDTL EYASKEPVHR KHHHGDLTWT LSWAFSENYT
LPLSHDEVVH GKNSLWSKMP GDDWQKAANL RLLYAHMFGH PGKKLLFMGG EFGQHREWDH
DRALEWDLAD EPLHEGLMEW LGDLNHLYQN APALWNDQED GFEWIAYDDR ENSVLTYRRL
NGDRSLVFVL NFTPVVREDY RIGATGDGRW HERLNSDSDV YGGSNVGNRG AVHSDPVEKH
GHSHSLSLTL PPLGALVLEP AE
