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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
 
 
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