(data stored in ACNUC7421 zone)

SWISSPROT: BGAL_ECOL5

ID   BGAL_ECOL5              Reviewed;        1024 AA.
AC   Q0TKT1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 86.
DE   RecName: Full=Beta-galactosidase {ECO:0000255|HAMAP-Rule:MF_01687};
DE            Short=Beta-gal {ECO:0000255|HAMAP-Rule:MF_01687};
DE            EC=3.2.1.23 {ECO:0000255|HAMAP-Rule:MF_01687};
DE   AltName: Full=Lactase {ECO:0000255|HAMAP-Rule:MF_01687};
GN   Name=lacZ {ECO:0000255|HAMAP-Rule:MF_01687}; OrderedLocusNames=ECP_0417;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01687};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01687};
CC       Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_01687};
CC   -!- COFACTOR:
CC       Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01687};
CC       Note=Binds 1 sodium ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01687};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01687}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01687}.
DR   EMBL; CP000247; ABG68450.1; -; Genomic_DNA.
DR   RefSeq; WP_000177876.1; NC_008253.1.
DR   SMR; Q0TKT1; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   PRIDE; Q0TKT1; -.
DR   EnsemblBacteria; ABG68450; ABG68450; ECP_0417.
DR   KEGG; ecp:ECP_0417; -.
DR   eggNOG; ENOG4105CNT; Bacteria.
DR   eggNOG; COG3250; LUCA.
DR   HOGENOM; HOG000252443; -.
DR   KO; K01190; -.
DR   OMA; SNWQLQG; -.
DR   BioCyc; ECOL362663:G1G5S-435-MONOMER; -.
DR   Proteomes; UP000009182; Chromosome.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.70.98.10; -; 1.
DR   HAMAP; MF_01687; Beta_gal; 1.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032312; LacZ_4.
DR   PANTHER; PTHR46323; PTHR46323; 1.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF16353; DUF4981; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF49303; SSF49303; 2.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0TKT1.
DR   SWISS-2DPAGE; Q0TKT1.
KW   Glycosidase; Hydrolase; Magnesium; Metal-binding; Sodium.
FT   CHAIN           1..1024
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000366997"
FT   REGION          538..541
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   ACT_SITE        462
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   ACT_SITE        538
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   METAL           202
FT                   /note="Sodium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   METAL           417
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   METAL           419
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   METAL           462
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   METAL           598
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   METAL           602
FT                   /note="Sodium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   METAL           605
FT                   /note="Sodium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         103
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         202
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         462
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         605
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         1000
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   SITE            358
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   SITE            392
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ   SEQUENCE   1024 AA;  116473 MW;  1596932C64CC1EB5 CRC64;
     MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR
     FAWFPAPEAV PESWLECDLP DADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPAENP
     TGCYSLTFNI DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA
     GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFQVTT RFNDDFSRAV
     LEAEVQMYGE LRDELRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPE
     LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH
     HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG
     MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD
     PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE MRPLILCEYA
     HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
     QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGRTIEVT SEYLFRHSDN EFLHWMVALD
     GKPLASGEVP LDVGPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ
     WRLAENLSVT LPSASHAIPQ LTTSGTDFCI ELGNKRWQFN RQSGFLSQMW IGDEKQLLTP
     LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA
     HAWQHQGKTL FISRKTYRID GHGEMVINVD VAVASDTPHP ARVGLTCQLA QVAERVNWLG
     LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI
     SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGHYHYQLV
     WCQK
//

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