GLGB_GRABC
ID GLGB_GRABC Reviewed; 734 AA.
AC Q0BU54;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-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};
GN OrderedLocusNames=GbCGDNIH1_0750;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/jb.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI61648.1; -; Genomic_DNA.
DR RefSeq; WP_011631457.1; NC_008343.2.
DR AlphaFoldDB; Q0BU54; -.
DR SMR; Q0BU54; -.
DR STRING; 391165.GbCGDNIH1_0750; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABI61648; ABI61648; GbCGDNIH1_0750.
DR KEGG; gbe:GbCGDNIH1_0750; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_5; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001963; 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; -; 2.
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; 2.
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..734
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260659"
FT ACT_SITE 413
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 466
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 734 AA; 82302 MW; 902B363512AED48E CRC64;
MNALDPDTLI HPDVATAIIH GRHGDPFSVL GIHTTREGVV LRSFQPEATS VVAINPESGQ
EIATLHRVHG DGIFAARLPG RTGYRLKIVT ATGTDIIDDP YVFPNLLGDL DVYLLAEGRH
EDLGRVLGAH VTTMHSPDGR EVEGVRFAVW APNATRASVI GSFNHWDGRC HPMRKRVEAG
VWELFIPGLT AGTIYKYELL GPNGELLPLK ADPVAWYAEI PPATASIVAS PAPFQWTDEQ
WMQQRGRLQA ADQPISIYEV HPTSWMPAKC GDWNTLADRL IPYVQSLGFT HVEFLPVMEH
PFGGSWGYQP LGQFAPMARL GTPESFASLV NRLHEVGIGV ILDWVPAHFP TDAHGLARFD
GTALYEHEDP REGYHYDWNT YIYNLGRNEV RAFLISSAVH WLTYFHADAL RVDAVASMLY
RDYSRKHGEW IPNMYGGREN LESVSFLQHL STVVKSRAPG AVLIAEESTA WPGVTRPAHE
GGLGFDYKWN MGWMHDTLHY MQEDPVNRSW HHDQMTFGLV YAFSEKFVLP LSHDEVVHGK
RSLLGRMPGD EWQRFANLRA YYGFMWTHPG KKLLFMGGEI AQEQEWSEGH GTDWYLLDRP
NHQGVQRLVA DLNMLYRAEP ALYRKDCAWD GFSWLVIDDR TQSVFAYMRY GADSDAPVLV
VCNLTPVPRH DYRIGVPQGG YWREILNTDA GIYGGSNTGN GGGRMADATP SHHHPASLQL
TLPPLATIIL KPES