GLGB_ALBFT
ID GLGB_ALBFT Reviewed; 625 AA.
AC Q21WG7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=Rfer_2162;
OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS (Rhodoferax ferrireducens).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=338969;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000267; ABD69886.1; -; Genomic_DNA.
DR RefSeq; WP_011464454.1; NC_007908.1.
DR AlphaFoldDB; Q21WG7; -.
DR SMR; Q21WG7; -.
DR STRING; 338969.Rfer_2162; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q21WG7; -.
DR EnsemblBacteria; ABD69886; ABD69886; Rfer_2162.
DR KEGG; rfr:Rfer_2162; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_4; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000008332; 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..625
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260688"
FT ACT_SITE 302
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 355
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 625 AA; 71407 MW; B90612F59B94E7AA CRC64;
MKSDHDIYLF REGTHAKLYN KLGCHLQSNG GANFAVWAPN AESVSVVGDW NYWSGNVDRL
DLRDDGSGIW QGFVENAVRG QGYKYRIQSS HGSYGVDKAD PFAFYAEPPP ATASRVWSLE
HDWKDDQWMS SRGPKNALDA PMSIYEIHLG SWRRQDGHFL DYRELAHSLA DYVIEMGFTH
VELMPVTEHP FYGSWGYQTT GYFAPTSRFG TPQDFMHFVD HLHQRGIGVL LDWVPSHFPT
DEHGLGYFDG THLFEHSDPR QGFHPEWNSS IFNYGRNEVR SFLISSGLFW LDKYHLDGLR
VDGVASMLYL DYARKEDEWI PNRHGGRENL EAVDFLQTLN KAVYREYPDT LTIAEESTAW
PRVSRPTDMD GLGFGMKWNM GWMHDSLAYM QQEPVHRKYH HHKLTFSLVY AFNENFVLPL
SHDEVVHGKG SLLGKMPGDA WQQFANLRAL FGYMWAHPGK KLLFMGGEFG QRREWTHDGE
LEWWVTKLEG HAGLQRYVAQ LNRVYRSLPA LYQLDFSPAG FEWVEADAAD TSVFAFLRKP
REHGAPVLIV SNMTPVPRTN YMLGVPLAGF WREVINSDAS EFGGSGWGNL GGVEASPVRF
HGRPHSVCLT LPPLSTLIFE HVPHA
