ID BGAL_ECO5E Reviewed; 1024 AA.
AC B5Z2P7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 01-MAY-2013, entry version 34.
DE RecName: Full=Beta-galactosidase;
DE Short=Beta-gal;
DE EC=3.2.1.23;
DE AltName: Full=Lactase;
GN Name=lacZ; OrderedLocusNames=ECH74115_0417;
OS Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=444450;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC4115 / EHEC;
RA Eppinger M., Sebastian Y., Ravel J.;
RT "Complete genome sequence of Escherichia coli O157:H7 str. EC4115.";
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC galactose residues in beta-D-galactosides.
CC -!- COFACTOR: Binds 2 magnesium ions per monomer (By similarity).
CC -!- COFACTOR: Binds 1 sodium ion per monomer (By similarity).
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
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DR EMBL; CP001164; ACI39312.1; -; Genomic_DNA.
DR RefSeq; YP_002268983.1; NC_011353.1.
DR ProteinModelPortal; B5Z2P7; -.
DR SMR; B5Z2P7; 14-1024.
DR STRING; 444450.ECH74115_0417; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; ACI39312; ACI39312; ECH74115_0417.
DR GeneID; 6971849; -.
DR KEGG; ecf:ECH74115_0417; -.
DR PATRIC; 18361667; VBIEscCol74651_0539.
DR eggNOG; COG3250; -.
DR HOGENOM; HOG000252443; -.
DR KO; K01190; -.
DR OMA; TIREYHI; -.
DR ProtClustDB; PRK09525; -.
DR BioCyc; ECOL444450:GHOB-5138-MONOMER; -.
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 CHAIN 1 1024 Beta-galactosidase.
FT /FTId=PRO_0000366994.
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; 116391 MW; BCA3922388694911 CRC64;
MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTNRPSQ QLRSLNGEWQ
FVWFPAPEAV PESWLECDLP DADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPTENP
TGCYSLTFNV DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLLS EFDLSAFLRA
GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT LFNDDFSRAV
LEAEVQMYGE LRDELRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLGLNVENPK
LWSAEIPNIY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH
HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG
MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD
PSRPVQYEGG GADTSATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE MRPLILCEYA
HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD LVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGRTIEVT SEYLFHHSDN ELLHWTVALD
GKPLASGEVP LDVAPQGKQV IELPELPRLE STGQLWLTVH VVQPNATAWS EAGHISAWQQ
WRLAENLSVT LPSAPHAIPQ LTTSETDFCI ELDNKRWQFN RQSGFLSQMW IGDKKQLLTP
LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTV
HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLTCQLA QVAERVNWLG
LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI
SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV
WCQK
//
