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Database: UniProt/TrEMBL
Entry: C6UB28_ECOBR
LinkDB: C6UB28_ECOBR
Original site: C6UB28_ECOBR 
ID   C6UB28_ECOBR            Unreviewed;      1024 AA.
AC   C6UB28;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   11-JUN-2014, entry version 39.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase;
GN   Name=lacZ; OrderedLocusNames=ECB_00298;
OS   Escherichia coli (strain B / REL606).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=413997;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / REL606;
RX   PubMed=19786035; DOI=10.1016/j.jmb.2009.09.052;
RA   Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H.,
RA   Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S.,
RA   Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W.,
RA   Daegelen P., Kim J.F.;
RT   "Genome sequences of Escherichia coli B strains REL606 and
RT   BL21(DE3).";
RL   J. Mol. Biol. 394:644-652(2009).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC   -!- COFACTOR: Binds 1 sodium ion per monomer (By similarity).
CC   -!- COFACTOR: Binds 2 magnesium ions per monomer (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
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DR   EMBL; CP000819; ACT37989.1; -; Genomic_DNA.
DR   RefSeq; YP_003043525.1; NC_012967.1.
DR   ProteinModelPortal; C6UB28; -.
DR   SMR; C6UB28; 14-1024.
DR   STRING; 413997.ECB_00298; -.
DR   BindingDB; C6UB28; -.
DR   PRIDE; C6UB28; -.
DR   EnsemblBacteria; ACT37989; ACT37989; ECB_00298.
DR   GeneID; 8175239; -.
DR   KEGG; ebr:ECB_00298; -.
DR   PATRIC; 18232534; VBIEscCol118196_0319.
DR   eggNOG; COG3250; -.
DR   HOGENOM; HOG000252443; -.
DR   KO; K01190; -.
DR   OMA; NPPFVPK; -.
DR   OrthoDB; EOG6XWV0T; -.
DR   BioCyc; ECOL413997:GCQD-484-MONOMER; -.
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-HAMAP.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.320; -; 2.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.20.20.80; -; 1.
DR   HAMAP; MF_01687; Beta_gal; 1.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR011013; Gal_mutarotase_SF_dom.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR013812; Glyco_hydro_2/20_Ig-like.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR006103; Glyco_hydro_2_TIM.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02929; Bgal_small_N; 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;
KW   Complete proteome; Glycosidase; Hydrolase; Magnesium; Metal-binding;
KW   Sodium.
FT   REGION      538    541       Substrate binding (By similarity).
FT   ACT_SITE    462    462       Proton donor (By similarity){EA7}.
FT   ACT_SITE    538    538       Nucleophile (By similarity){EA7}.
FT   METAL       202    202       Sodium (By similarity){EA7}.
FT   METAL       417    417       Magnesium 1 (By similarity){EA7}.
FT   METAL       419    419       Magnesium 1 (By similarity){EA7}.
FT   METAL       462    462       Magnesium 1 (By similarity){EA7}.
FT   METAL       598    598       Magnesium 2 (By similarity){EA7}.
FT   METAL       602    602       Sodium; via carbonyl oxygen (By
FT                                similarity){EA7}.
FT   METAL       605    605       Sodium (By similarity){EA7}.
FT   BINDING     103    103       Substrate (By similarity){EA7}.
FT   BINDING     202    202       Substrate (By similarity){EA7}.
FT   BINDING     462    462       Substrate (By similarity){EA7}.
FT   BINDING     605    605       Substrate (By similarity){EA7}.
FT   BINDING    1000   1000       Substrate (By similarity){EA7}.
FT   SITE        358    358       Transition state stabilizer (By
FT                                similarity).
FT   SITE        392    392       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   1024 AA;  116483 MW;  9D295EF4CEF90B08 CRC64;
     MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR
     FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPTENP
     TGCYSLTFNV DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA
     GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV
     LEAEVQMCGE LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK
     LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH
     HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG
     MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD
     PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA
     HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
     QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN ELLHWMVALD
     GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ
     WRLAENLSVT LPAASHAIPH LTTSEMDFCI ELGNKRWQFN RQSGFLSQMW IGDKKQLLTP
     LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA
     HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLNCQLA QVAERVNWLG
     LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI
     SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV
     WCQK
//
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