(data stored in ACNUC7421 zone)

SWISSPROT: BGAL_ECO27

ID   BGAL_ECO27              Reviewed;        1024 AA.
AC   B7UJI9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
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};
GN   OrderedLocusNames=E2348C_0299;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000255|HAMAP-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-
CC       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; FM180568; CAS07847.1; -; Genomic_DNA.
DR   RefSeq; WP_000177864.1; NC_011601.1.
DR   SMR; B7UJI9; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   PRIDE; B7UJI9; -.
DR   EnsemblBacteria; CAS07847; CAS07847; E2348C_0299.
DR   KEGG; ecg:E2348C_0299; -.
DR   KO; K01190; -.
DR   OMA; PSNWQLQ; -.
DR   BioCyc; ECOL574521:E2348C_RS01575-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UJI9.
DR   SWISS-2DPAGE; B7UJI9.
KW   Complete proteome; Glycosidase; Hydrolase; Magnesium; Metal-binding;
KW   Sodium.
FT   CHAIN         1   1024       Beta-galactosidase.
FT                                /FTId=PRO_1000215917.
FT   REGION      538    541       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   ACT_SITE    462    462       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   ACT_SITE    538    538       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       202    202       Sodium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       417    417       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       419    419       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       462    462       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       598    598       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       602    602       Sodium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01687}.
FT   METAL       605    605       Sodium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   BINDING     103    103       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   BINDING     202    202       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   BINDING     462    462       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   BINDING     605    605       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   BINDING    1000   1000       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   SITE        358    358       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01687}.
FT   SITE        392    392       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01687}.
SQ   SEQUENCE   1024 AA;  116417 MW;  D2855B080560328E CRC64;
     MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWQ
     FVWFPAPEAV PESWLECDLP DADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPAENP
     TGCYSLTFNI DECWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA
     GKNRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV
     LEAEVQMYGE LRDELRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPA
     LWSAEIPNIY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH
     HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG
     MVPMNRLTDD PRWLPAMSER VTRMVLRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD
     PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE LRPLILCEYA
     HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
     QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGRTIEVT SEYLFRHSDN ELLHWTVALD
     GKPLASGEVP LDVAPQGKQV IELPELPQPE SAGQLWLTVH VVQPNATAWS EAGHISAWQQ
     WRLAENLSVT LPTASHAIPH LTTSEMDFCI ELGNKRWQFN RQSGFLSQMW IGDEKQLLTP
     LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA
     HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLTCQLA QVAERVNWLG
     LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI
     SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV
     WCQK
//

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