GLGB2_RHIEC
ID GLGB2_RHIEC Reviewed; 732 AA.
AC Q2JZ21;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE Short=BE 2 {ECO:0000255|HAMAP-Rule:MF_00685};
GN Name=glgB2 {ECO:0000255|HAMAP-Rule:MF_00685};
GN OrderedLocusNames=RHE_PF00275;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OG Plasmid p42f.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(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; CP000138; ABC94165.1; -; Genomic_DNA.
DR RefSeq; WP_011428582.1; NC_007766.1.
DR AlphaFoldDB; Q2JZ21; -.
DR SMR; Q2JZ21; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABC94165; ABC94165; RHE_PF00275.
DR KEGG; ret:RHE_PF00275; -.
DR HOGENOM; CLU_004245_3_2_5; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001936; Plasmid p42f.
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; 2.
DR TIGRFAMs; TIGR01515; branching_enzym; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Plasmid; Reference proteome; Transferase.
FT CHAIN 1..732
FT /note="1,4-alpha-glucan branching enzyme GlgB 2"
FT /id="PRO_0000260683"
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 732 AA; 81931 MW; 23B9D25D7E41BA0E CRC64;
MNVERSEFLA GVGHDALWAL IEGRHGDPFS ILGPHESGGM TIVRVYLPGA EGVDLIEAAS
GRVVTPFSIA HPSGLFAAAM GSRMHYRLRI TWPDGEQITE DPYSFGLLLG ELDLHLISEG
THYSLSRTLG AVEMAIDDVA GVRFAVWAPN ARRVSVVGDF NAWDGRRNPM RLRQSAGVWE
LFMPRLAPGE RYKFEIIDPH GNCLPQKADP VARASEAAPS TASIVASSTR FRWTDDNWMK
GQSRQQRLEG PISVYEVHAG SWLRENGGRS LDWVELSQRL VPYVREMGFT HIELLPIMEH
PFGGSWGYQP LGLFAPTGRY GTPEDLAYFI DRCHGAGIGV ILDWVPAHFP TDVWGLARFD
GTALYEHEDP REGFHRDWNT LIYNLGRNEV KGFLIASALE WLERYHIDGL RVDAVASMLY
RDYSRNEGEW IPNRYGGREN LEAVEFFKHL NSIVHERCPH AMMIAEESTA WPGVTKPPEE
GGLGFDMKWN MGWMHDSLSY IEKDPVYRSY HHGTMTFGMI YAYSERFILP ISHDEVVYGK
GSLLGKMPGD EWQKFANLRS YLAFMWGHPG KKLIFMGGEI AQPSEWNHDA SIAWDVLDQP
AHAGLQRLVK DLNGFYKDEA ALQFGDFHSE GFDWAAADDA VNSVLGMLRY APDRSSSVLV
VSNFTPVPRY GYRIGVPQDG VWIEKVTTDA REYGGSGLVN GAVSSESVPA HGRPHSLWLT
LPPLATVLLK SP
