GLGB_PARXL
ID GLGB_PARXL Reviewed; 736 AA.
AC Q13S07;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=Bxeno_B0164;
GN ORFNames=Bxe_B2863;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000271; ABE33132.1; -; Genomic_DNA.
DR RefSeq; WP_011490512.1; NZ_CP008762.1.
DR AlphaFoldDB; Q13S07; -.
DR SMR; Q13S07; -.
DR STRING; 266265.Bxe_B2863; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABE33132; ABE33132; Bxe_B2863.
DR KEGG; bxb:DR64_5192; -.
DR KEGG; bxe:Bxe_B2863; -.
DR PATRIC; fig|266265.5.peg.4828; -.
DR eggNOG; COG0296; Bacteria.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001817; Chromosome 2.
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..736
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260641"
FT ACT_SITE 415
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 470
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 736 AA; 82135 MW; 4D7D9682B44E3CAC CRC64;
MSEHDPAAGL QPLDIDALVE ARHPDPFSQL GLHHTDAGPV VRALLPNAAH VSVISRADGA
LLGELEQLRP GLFAGRITSA APYRLRIDWH GVVQEIEDTY SFGPVLGDEP LGRLAGGDPY
AVLECLGARP MEVDGVPGVR FAVWAPNARR VSVVGDFNAW DGRRHPMRLR HQAGVWELFV
PRVGPGTRYK YELLSRDGHP LPLKADPCAM QTEKPPGTAS IVAHVDEVEQ FPWSDHEWIQ
SRAGKQTARS PISIYEVHAE SWLRVAEEGQ RGLDWEELAE RMIPYVKSMG FTHVEFMPIA
EHPFGGSWGY QPLGQFAPSA RFGKPEQFAR FVDKAHEAGL GVILDWVPAH FPNDAHGLID
FDGTPLYEHA DPREGYHQDW NTMIYNLGRN EVSAFLIASG LAWLKRYHVD GLRVDAVASM
LYRDYSRAAD QWVPNIYGGR ENLESIAFLK RLNHEVGYVP GVPGAITIAE ESTAWPGVTA
RVEDGGLGFQ FKWNMGWMHD TLHYMEEDPV YRQYHHHNMT FGMVYAYSER FVLPLSHDEV
VHGKGSLLGK MPGDRWQKFA NLRAYFGFMW THPGKKLLFM GGEFGQLAEF NHDASPHWHL
LDDSNHHGVQ MLVRDLNRLY SDEPALYLLD CEPGGFEWLI GDDSGNSVFA YRRTDGAGRE
LVVVCNMTPV PRLGYRIGMP RGGRWVEVLN TDAGVYGGSN MGNGGLIHTD SQSSHGWPHS
AALTLPPLAT IVLRAD
