ID   BGAL_ENTCL     STANDARD;      PRT;  1028 AA.
AC   Q47077;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Beta-galactosidase (EC 3.2.1.23) (Lactase).
GN   Name=lacZ;
OS   Enterobacter cloacae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GAO;
RX   MEDLINE=95072316; PubMed=7765512;
RA   Nagano H., Kawaguchi T., Omori M., Shoji Z., Arai M.;
RT   "Molecular cloning and nucleotide sequence of the beta-galactosidase
RT   gene from Enterobacter cloacae GAO.";
RL   Biosci. Biotechnol. Biochem. 58:1866-1869(1994).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; D42077; BAA07673.1; -.
DR   HSSP; P00722; 1BGL.
DR   InterPro; IPR008979; Gal_bind_like.
DR   InterPro; IPR011013; Gal_mut_like.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR006102; Glyco_hydro_2Ig.
DR   InterPro; IPR006104; Glyco_hydro_2SB.
DR   InterPro; IPR006103; Glyco_hydro_2TIM.
DR   InterPro; IPR004200; Glyco_hydro_42C.
DR   InterPro; IPR004199; Glyco_hydro_42N.
DR   Pfam; PF02930; Bgal_small_C; 1.
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   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
KW   Glycosidase; Hydrolase.
FT   ACT_SITE    463    463       Proton donor (By similarity).
FT   ACT_SITE    539    539       Nucleophile (By similarity).
SQ   SEQUENCE   1028 AA;  116678 MW;  F4D61F55F9FEEAEC CRC64;
     MSDTPSLTLS ALLARRDWEN PVVTQWNRLA AHAPLHSWRN EPSARDDAGS ARRQTLNGLW
     RFSYFTAPEQ VPQAWVTEDC ADAVAMPVPS NWQMQGFDTP IYTNVTYPIP VNPPFVPQEN
     PTGCYSLTFE VDDAWLQSGQ TRIIFDGVNS AFHLWCNGQW IGYSQDSRLP AEFDLSAALR
     PGQNRLAVMV LRWCDGSYLE DQDMWRMSGI FRDVTLLHKP ETQIADYHVV TDLNAELDRA
     VLKVDVTLAG AGFADGEVVF TLWRKGEKCA SVSRQPGSAI VDERGSWAER LTVTIPVETP
     ALWSAETPEL YRLTMALLNP QGEVLEIEAC DVGFRRVEIS NGLLKLNGKP LLIRGVNRHE
     HHSENGQVMD EATMRRDIET MKQHSFNAVR CSHYPNHPLW YQLCDRYGLY VVDEANIETH
     GMVPMSRLAD DPRWLPAMSE RVTRMVQRDR NHPSIIIWSL GNESGHGANH DALYRWLKTT
     DPTRPVQYEG GGANTAATDI VCPMYARVDR DQPFPAVPKW SIKKWIGMPD ETRPLILCEY
     AHAMGNSFGG FAKYWQAFRS HPRLQGGFVW DWVDQALTKR DEDGNTFWAY GGDFGDKPND
     RQFCLNGLVF PDRTPHPALY EAHGPQQFFT FTRVSTSPLV IEVQSGYLFR HTDNEVLNWT
     VARDGDVLVA GEVTLAMVPE GTQRLEIALP ELNAGPGEVW LNVEVRQPRA TPWSPAAIAA
     AGSSGRFRLR SLLLRQPRRR AAVLTQTDRI LEIAHRQQRW QFDRASGNLT QWWRNGVETL
     LSPLTDNVSR APLDNDIGVS EATKIDPNAW VERWKAAGMY DLTPRVLHCE AEQHAGEVVV
     TTQHVLEYRG KALFLSRKVW RIDEQGVLHG DIQVDMASDI PEPARIGLSV HLAETPENVR
     WLGLGPHENY PDRKLAAQQG RWTLPLEAMH TPYIFPTENG LRCDTRELVV GMHQLNGHFH
     FSVSRYSQQQ LRETTHHHLL REEPGCWLNL DAFHMGVGGD DSWSPSVSPE FILQTRQLRY
     TFSWQQNP
//