GLGB_SHEON
ID GLGB_SHEON Reviewed; 745 AA.
AC Q8EGU7;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 120.
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=SO_1494;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN54555.2; -; Genomic_DNA.
DR RefSeq; NP_717111.2; NC_004347.2.
DR AlphaFoldDB; Q8EGU7; -.
DR SMR; Q8EGU7; -.
DR STRING; 211586.SO_1494; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; Q8EGU7; -.
DR KEGG; son:SO_1494; -.
DR PATRIC; fig|211586.12.peg.1438; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR PhylomeDB; Q8EGU7; -.
DR BioCyc; SONE211586:G1GMP-1380-MON; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
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..745
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188742"
FT ACT_SITE 415
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 468
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 745 AA; 85188 MW; 6194EA3E56302335 CRC64;
MTQAQTYFYD GSDVALLNGQ YTDVFSLLGM HSINEGKALV VRCFLRNAQK VDVISLKDGR
KVASLERVNE AGLFAGTLGR RIKPFLYALR VTYPLCELDI IDPYQFGSLL NREDLYLFGE
GSSEQAYRFL GANWRQVDNV EGVHFCVWAP NAKRVSVVGD FNHWDDTRHV MRQHVANGLW
EIFLPGVVEG SHYKFDLVYQ NGERHAKSDP MATQMECAPH NASIVPKKQQ HQWADTQWMD
KRAATAWHRA PMSIYEVQLG SWRRKGEFGE QYFDYQDLIE QLIPYVKEQG FTHIELMPVS
EYPFDGSWGY QPVGLYAPTY RFGDANGFKA FIDACHQAEI GVLLDWVAAH FPKDPHGLVR
FDGTCLYEHE DPRKGTHPDW DTLIYNYGRG EVRSFLLSNA CYWLREFHLD GLRLDAVSSM
LYLDYSREPG QWLPNAYGGR ENLEAIDFLQ MLNQRLYQAI PGICMIAEES TAFAGVTKPT
DSSGLGFGFK WNMGWMNDSL SYLGRDPIYR QYHHNQLTFS LMYAYSEQFM LSISHDEVVH
GKGSLLHKIP GDDWQKFATL RAYYGFMWGH PGKKLLFMGS EFAQRDEWDH DHSLDWHLLA
FEPHQGVQRW LRDLNQLYRQ FPALSVLDYE PQGFRWLDCD NGRDSIFSFV RYGEGNDVPL
VFVVNMTPTV HQGFRIGLPQ GGDFCEYLNS DSYLYGGSNQ GNGGKIIAQA LPWQGMASSA
LITVPPLGCL ILGPATENIL RESAL
