GLGX_ECOLI
ID GLGX_ECOLI Reviewed; 657 AA.
AC P15067; P76693; Q2M795;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Glycogen debranching enzyme {ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000303|PubMed:8576033};
DE EC=3.2.1.196 {ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000269|PubMed:15687211, ECO:0000269|PubMed:779849, ECO:0000269|PubMed:8576033};
DE AltName: Full=Glycogen operon protein GlgX;
DE AltName: Full=Limit dextrin alpha-1,6-maltotetraose-hydrolase {ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000305};
GN Name=glgX {ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000303|PubMed:2975249,
GN ECO:0000303|PubMed:8576033}; Synonyms=glyX;
GN OrderedLocusNames=b3431, JW3394;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-590.
RC STRAIN=K12;
RX PubMed=2975249; DOI=10.1016/0378-1119(88)90208-9;
RA Romeo T., Kumar A., Preiss J.;
RT "Analysis of the Escherichia coli glycogen gene cluster suggests that
RT catabolic enzymes are encoded among the biosynthetic genes.";
RL Gene 70:363-376(1988).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=779849; DOI=10.1016/0005-2744(76)90235-7;
RA Jeanningros R., Creuzet-Sigal N., Frixon C., Cattaneo J.;
RT "Purification and properties of a debranching enzyme from Escherichia
RT coli.";
RL Biochim. Biophys. Acta 438:186-199(1976).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=8576033; DOI=10.1128/jb.178.4.1012-1017.1996;
RA Yang H., Liu M.-Y., Romeo T.;
RT "Coordinate genetic regulation of glycogen catabolism and biosynthesis in
RT Escherichia coli via the CsrA gene product.";
RL J. Bacteriol. 178:1012-1017(1996).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=BW25113;
RX PubMed=15687211; DOI=10.1128/jb.187.4.1465-1473.2005;
RA Dauvillee D., Kinderf I.S., Li Z., Kosar-Hashemi B., Samuel M.S.,
RA Rampling L., Ball S., Morell M.K.;
RT "Role of the Escherichia coli glgX gene in glycogen metabolism.";
RL J. Bacteriol. 187:1465-1473(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RC STRAIN=K12;
RX PubMed=20187119; DOI=10.1002/prot.22697;
RA Song H.N., Jung T.Y., Park J.T., Park B.C., Myung P.K., Boos W., Woo E.J.,
RA Park K.H.;
RT "Structural rationale for the short branched substrate specificity of the
RT glycogen debranching enzyme GlgX.";
RL Proteins 78:1847-1855(2010).
CC -!- FUNCTION: Removes maltotriose and maltotetraose chains that are
CC attached by 1,6-alpha-linkage to the limit dextrin main chain,
CC generating a debranched limit dextrin. Shows only very little activity
CC with native glycogen. {ECO:0000269|PubMed:15687211,
CC ECO:0000269|PubMed:779849, ECO:0000269|PubMed:8576033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches
CC with degrees of polymerization of three or four glucose residues in
CC limit dextrin.; EC=3.2.1.196; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01248, ECO:0000269|PubMed:15687211,
CC ECO:0000269|PubMed:779849, ECO:0000269|PubMed:8576033};
CC -!- ACTIVITY REGULATION: Inhibited by iodoacetate, p-chloromercuribenzoate,
CC HgCl(2), cupric sulfate and ammonium sulfate.
CC {ECO:0000269|PubMed:779849}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.6 to 6.4. {ECO:0000269|PubMed:779849};
CC Temperature dependence:
CC Optimum temperature is 45-50 degrees Celsius.
CC {ECO:0000269|PubMed:779849};
CC -!- PATHWAY: Glycan degradation; glycogen degradation. {ECO:0000255|HAMAP-
CC Rule:MF_01248, ECO:0000269|PubMed:15687211, ECO:0000269|PubMed:779849}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20187119}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene leads to overproduction of
CC glycogen containing short external chains.
CC {ECO:0000269|PubMed:15687211}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA98735.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; J01616; AAA98735.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U18997; AAA58229.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76456.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77861.1; -; Genomic_DNA.
DR PIR; B65139; BVECGX.
DR RefSeq; NP_417889.1; NC_000913.3.
DR RefSeq; WP_000192523.1; NZ_SSZK01000008.1.
DR PDB; 2WSK; X-ray; 2.25 A; A=1-657.
DR PDBsum; 2WSK; -.
DR AlphaFoldDB; P15067; -.
DR SMR; P15067; -.
DR BioGRID; 4263517; 21.
DR BioGRID; 852250; 6.
DR IntAct; P15067; 15.
DR STRING; 511145.b3431; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR jPOST; P15067; -.
DR PaxDb; P15067; -.
DR PRIDE; P15067; -.
DR EnsemblBacteria; AAC76456; AAC76456; b3431.
DR EnsemblBacteria; BAE77861; BAE77861; BAE77861.
DR GeneID; 947941; -.
DR KEGG; ecj:JW3394; -.
DR KEGG; eco:b3431; -.
DR PATRIC; fig|511145.12.peg.3528; -.
DR EchoBASE; EB0376; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_011725_1_1_6; -.
DR InParanoid; P15067; -.
DR OMA; SEPWDCG; -.
DR PhylomeDB; P15067; -.
DR BioCyc; EcoCyc:EG10381-MON; -.
DR BioCyc; MetaCyc:EG10381-MON; -.
DR BRENDA; 3.2.1.196; 2026.
DR UniPathway; UPA00165; -.
DR EvolutionaryTrace; P15067; -.
DR PRO; PR:P15067; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; IDA:EcoCyc.
DR GO; GO:0004133; F:glycogen debranching enzyme activity; IMP:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0005980; P:glycogen catabolic process; IMP:EcoCyc.
DR CDD; cd02856; E_set_GDE_Isoamylase_N; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR HAMAP; MF_01248; GlgX; 1.
DR InterPro; IPR040784; GlgX_C.
DR InterPro; IPR044505; GlgX_Isoamylase_N_E_set.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR022844; Glycogen_debranch_bac.
DR InterPro; IPR011837; Glycogen_debranch_GlgX.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF18390; GlgX_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR02100; glgX_debranch; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycogen metabolism; Glycosidase;
KW Hydrolase; Reference proteome.
FT CHAIN 1..657
FT /note="Glycogen debranching enzyme"
FT /id="PRO_0000054297"
FT REGION 458..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248,
FT ECO:0000305|PubMed:20187119"
FT ACT_SITE 371
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248,
FT ECO:0000305|PubMed:20187119"
FT SITE 443
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248,
FT ECO:0000305|PubMed:20187119"
FT CONFLICT 288
FT /note="Y -> YY (in Ref. 3; AAA98735)"
FT /evidence="ECO:0000305"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:2WSK"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 279..287
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 311..326
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:2WSK"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 394..405
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 411..418
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 486..505
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 506..513
FT /evidence="ECO:0007829|PDB:2WSK"
FT TURN 514..519
FT /evidence="ECO:0007829|PDB:2WSK"
FT TURN 534..536
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 540..542
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 545..558
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 562..565
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:2WSK"
FT HELIX 589..594
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 597..603
FT /evidence="ECO:0007829|PDB:2WSK"
FT TURN 604..606
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 643..647
FT /evidence="ECO:0007829|PDB:2WSK"
FT STRAND 651..656
FT /evidence="ECO:0007829|PDB:2WSK"
SQ SEQUENCE 657 AA; 73577 MW; AA9EFC1F67FD0420 CRC64;
MTQLAIGKPA PLGAHYDGQG VNFTLFSAHA ERVELCVFDA NGQEHRYDLP GHSGDIWHGY
LPDARPGLRY GYRVHGPWQP AEGHRFNPAK LLIDPCARQI DGEFKDNPLL HAGHNEPDYR
DNAAIAPKCV VVVDHYDWED DAPPRTPWGS TIIYEAHVKG LTYLHPEIPV EIRGTYKALG
HPVMINYLKQ LGITALELLP VAQFASEPRL QRMGLSNYWG YNPVAMFALH PAYACSPETA
LDEFRDAIKA LHKAGIEVIL DIVLNHSAEL DLDGPLFSLR GIDNRSYYWI REDGDYHNWT
GCGNTLNLSH PAVVDYASAC LRYWVETCHV DGFRFDLAAV MGRTPEFRQD APLFTAIQNC
PVLSQVKLIA EPWDIAPGGY QVGNFPPLFA EWNDHFRDAA RRFWLHYDLP LGAFAGRFAA
SSDVFKRNGR LPSAAINLVT AHDGFTLRDC VCFNHKHNEA NGEENRDGTN NNYSNNHGKE
GLGGSLDLVE RRRDSIHALL TTLLLSQGTP MLLAGDEHGH SQHGNNNAYC QDNQLTWLDW
SQASSGLTAF TAALIHLRKR IPALVENRWW EEGDGNVRWL NRYAQPLSTD EWQNGPKQLQ
ILLSDRFLIA INATLEVTEI VLPAGEWHAI PPFAGEDNPV ITAVWQGPAH GLCVFQR
