(data stored in ACNUC10821 zone)

SWISSPROT: C8U237_ECO10

ID   C8U237_ECO10            Unreviewed;      1024 AA.
AC   C8U237;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|HAMAP-Rule:MF_01687, ECO:0000256|SAAS:SAAS01166384};
DE            Short=Beta-gal {ECO:0000256|HAMAP-Rule:MF_01687};
DE            EC=3.2.1.23 {ECO:0000256|HAMAP-Rule:MF_01687, ECO:0000256|SAAS:SAAS01166384};
DE   AltName: Full=Lactase {ECO:0000256|HAMAP-Rule:MF_01687};
GN   Name=lacZ {ECO:0000256|HAMAP-Rule:MF_01687,
GN   ECO:0000313|EMBL:BAI29195.1};
GN   OrderedLocusNames=ECO103_0326 {ECO:0000313|EMBL:BAI29195.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29195.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29195.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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:0000256|HAMAP-Rule:MF_01687,
CC         ECO:0000256|SAAS:SAAS01166382};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01687};
CC       Note=Binds 2 magnesium ions per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_01687};
CC   -!- COFACTOR:
CC       Name=Na(+); Xref=ChEBI:CHEBI:29101; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01687};
CC       Note=Binds 1 sodium ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_01687};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01687}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01687, ECO:0000256|SAAS:SAAS00568376}.
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DR   EMBL; AP010958; BAI29195.1; -; Genomic_DNA.
DR   RefSeq; WP_000177972.1; NC_013353.1.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   EnsemblBacteria; BAI29195; BAI29195; ECO103_0326.
DR   KEGG; eoh:ECO103_0326; -.
DR   HOGENOM; HOG000252443; -.
DR   KO; K01190; -.
DR   OMA; PSNWQLQ; -.
DR   BioCyc; ECOL585395:ECO103_RS01705-MONOMER; -.
DR   Proteomes; UP000000959; 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; C8U237.
DR   SWISS-2DPAGE; C8U237.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_01687,
KW   ECO:0000256|SAAS:SAAS00422512};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01687,
KW   ECO:0000256|SAAS:SAAS00422513};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01687};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01687};
KW   Sodium {ECO:0000256|HAMAP-Rule:MF_01687}.
FT   DOMAIN      749   1022       Bgal_small_N. {ECO:0000259|SMART:
FT                                SM01038}.
FT   REGION      538    541       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01687}.
FT   ACT_SITE    462    462       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   ACT_SITE    538    538       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   METAL       202    202       Sodium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   METAL       417    417       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   METAL       419    419       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   METAL       462    462       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   METAL       598    598       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   METAL       602    602       Sodium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01687}.
FT   METAL       605    605       Sodium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   BINDING     103    103       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   BINDING     202    202       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   BINDING     462    462       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   BINDING     605    605       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   BINDING    1000   1000       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01687}.
FT   SITE        358    358       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01687}.
FT   SITE        392    392       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01687}.
SQ   SEQUENCE   1024 AA;  116508 MW;  BDDABCBAB29EFCAD CRC64;
     MTMITDSLVV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR
     FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPAENP
     TGCYSLTFNI DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSTFLRA
     GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPS TQISDFHVAT HFNDDFSRAV
     LEAEVQMYGE LRDELRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK
     LWSAEIPNLY RAVVELHTAD GTLIEAEASD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH
     HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG
     MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWNKSVD
     PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA
     HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
     QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN ELLHWMVALD
     GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ
     WRLAANLSVT LPSAPHAIPQ LTTSETDFCI ELDNKRWQFN RQSGFLSQMW IGDEKQLLTP
     LRDQFIRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTV
     HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLTCQLA QVAERVNWLG
     LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGSH QWRGDFQFNI
     SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV
     WCQK
//

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