GLGB_ECOLI
ID GLGB_ECOLI Reviewed; 728 AA.
AC P07762; Q2M796;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB;
DE EC=2.4.1.18;
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase;
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme;
DE AltName: Full=Glycogen branching enzyme;
DE Short=BE;
GN Name=glgB; OrderedLocusNames=b3432, JW3395;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3013861; DOI=10.1016/s0021-9258(19)84443-5;
RA Baecker P.A., Greenberg E., Preiss J.;
RT "Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli
RT 1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-alpha-D-(1,4-alpha-D-glucano)-
RT transferase as deduced from the nucleotide sequence of the glg B gene.";
RL J. Biol. Chem. 261:8738-8743(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 113-728.
RX PubMed=12196524; DOI=10.1074/jbc.m205746200;
RA Abad M.C., Binderup K., Rios-Steiner J., Arni R.K., Preiss J., Geiger J.H.;
RT "The X-ray crystallographic structure of Escherichia coli branching
RT enzyme.";
RL J. Biol. Chem. 277:42164-42170(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:0000250}.
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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; M13751; AAA23872.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58230.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76457.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77860.1; -; Genomic_DNA.
DR PIR; A25498; NQECA.
DR RefSeq; NP_417890.1; NC_000913.3.
DR RefSeq; WP_001283723.1; NZ_STEB01000004.1.
DR PDB; 1M7X; X-ray; 2.30 A; A/B/C/D=113-728.
DR PDB; 4LPC; X-ray; 2.39 A; A/B/C/D=117-728.
DR PDB; 4LQ1; X-ray; 2.55 A; A/B/C/D=117-728.
DR PDB; 5E6Y; X-ray; 2.60 A; A/B/C/D=117-728.
DR PDB; 5E6Z; X-ray; 1.88 A; A/B/C/D=117-728.
DR PDB; 5E70; X-ray; 2.33 A; A/B/C/D=117-728.
DR PDBsum; 1M7X; -.
DR PDBsum; 4LPC; -.
DR PDBsum; 4LQ1; -.
DR PDBsum; 5E6Y; -.
DR PDBsum; 5E6Z; -.
DR PDBsum; 5E70; -.
DR AlphaFoldDB; P07762; -.
DR SMR; P07762; -.
DR BioGRID; 4262503; 314.
DR IntAct; P07762; 13.
DR STRING; 511145.b3432; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR jPOST; P07762; -.
DR PaxDb; P07762; -.
DR PRIDE; P07762; -.
DR EnsemblBacteria; AAC76457; AAC76457; b3432.
DR EnsemblBacteria; BAE77860; BAE77860; BAE77860.
DR GeneID; 66672684; -.
DR GeneID; 947940; -.
DR KEGG; ecj:JW3395; -.
DR KEGG; eco:b3432; -.
DR PATRIC; fig|1411691.4.peg.3296; -.
DR EchoBASE; EB0373; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_6; -.
DR InParanoid; P07762; -.
DR OMA; FGMKWMM; -.
DR PhylomeDB; P07762; -.
DR BioCyc; EcoCyc:GLYCOGEN-BRANCH-MON; -.
DR BioCyc; MetaCyc:GLYCOGEN-BRANCH-MON; -.
DR BRENDA; 2.4.1.18; 2026.
DR UniPathway; UPA00164; -.
DR EvolutionaryTrace; P07762; -.
DR PRO; PR:P07762; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IDA:EcoCyc.
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:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycogen biosynthesis;
KW Glycogen metabolism; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..728
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188702"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 458
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:4LQ1"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1M7X"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1M7X"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:1M7X"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1M7X"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:4LPC"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:4LQ1"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 380..396
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 433..448
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:1M7X"
FT TURN 464..467
FT /evidence="ECO:0007829|PDB:1M7X"
FT TURN 470..473
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 483..494
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 497..502
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:1M7X"
FT TURN 512..516
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 519..523
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 543..559
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 560..567
FT /evidence="ECO:0007829|PDB:1M7X"
FT TURN 568..573
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 586..589
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:4LQ1"
FT HELIX 595..610
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:1M7X"
FT TURN 617..621
FT /evidence="ECO:0007829|PDB:4LPC"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 626..633
FT /evidence="ECO:0007829|PDB:1M7X"
FT TURN 634..637
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 638..644
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 650..656
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:4LPC"
FT STRAND 662..665
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 673..680
FT /evidence="ECO:0007829|PDB:1M7X"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:1M7X"
FT STRAND 719..726
FT /evidence="ECO:0007829|PDB:1M7X"
SQ SEQUENCE 728 AA; 84337 MW; 0F20AF3677BF2015 CRC64;
MSDRIDRDVI NALIAGHFAD PFSVLGMHKT TAGLEVRALL PDATDVWVIE PKTGRKLAKL
ECLDSRGFFS GVIPRRKNFF RYQLAVVWHG QQNLIDDPYR FGPLIQEMDA WLLSEGTHLR
PYETLGAHAD TMDGVTGTRF SVWAPNARRV SVVGQFNYWD GRRHPMRLRK ESGIWELFIP
GAHNGQLYKY EMIDANGNLR LKSDPYAFEA QMRPETASLI CGLPEKVVQT EERKKANQFD
APISIYEVHL GSWRRHTDNN FWLSYRELAD QLVPYAKWMG FTHLELLPIN EHPFDGSWGY
QPTGLYAPTR RFGTRDDFRY FIDAAHAAGL NVILDWVPGH FPTDDFALAE FDGTNLYEHS
DPREGYHQDW NTLIYNYGRR EVSNFLVGNA LYWIERFGID ALRVDAVASM IYRDYSRKEG
EWIPNEFGGR ENLEAIEFLR NTNRILGEQV SGAVTMAEES TDFPGVSRPQ DMGGLGFWYK
WNLGWMHDTL DYMKLDPVYR QYHHDKLTFG ILYNYTENFV LPLSHDEVVH GKKSILDRMP
GDAWQKFANL RAYYGWMWAF PGKKLLFMGN EFAQGREWNH DASLDWHLLE GGDNWHHGVQ
RLVRDLNLTY RHHKAMHELD FDPYGFEWLV VDDKERSVLI FVRRDKEGNE IIVASNFTPV
PRHDYRFGIN QPGKWREILN TDSMHYHGSN AGNGGTVHSD EIASHGRQHS LSLTLPPLAT
IWLVREAE
