ID C6UB28_ECOBR Unreviewed; 1024 AA.
AC C6UB28;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 01-MAY-2013, entry version 32.
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 STRING; 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; DFHVATH; -.
DR ProtClustDB; PRK09525; -.
DR BindingDB; C6UB28; -.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; SSF49785; Gal_bind_like; 1.
DR SUPFAM; SSF74650; Gal_mut_like; 1.
DR SUPFAM; SSF49303; Glyco_hydro_2Ig; 2.
DR SUPFAM; SSF51445; Glyco_hydro_cat; 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).
FT ACT_SITE 538 538 Nucleophile (By similarity).
FT METAL 202 202 Sodium (By similarity).
FT METAL 417 417 Magnesium 1 (By similarity).
FT METAL 419 419 Magnesium 1 (By similarity).
FT METAL 462 462 Magnesium 1 (By similarity).
FT METAL 598 598 Magnesium 2 (By similarity).
FT METAL 602 602 Sodium; via carbonyl oxygen (By
FT similarity).
FT METAL 605 605 Sodium (By similarity).
FT BINDING 103 103 Substrate (By similarity).
FT BINDING 202 202 Substrate (By similarity).
FT BINDING 462 462 Substrate (By similarity).
FT BINDING 605 605 Substrate (By similarity).
FT BINDING 1000 1000 Substrate (By similarity).
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
//
