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Database: UniProt/TrEMBL
Entry: C5A125_ECOBW
LinkDB: C5A125_ECOBW
Original site: C5A125_ECOBW 
ID   C5A125_ECOBW            Unreviewed;      1080 AA.
AC   C5A125;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   19-FEB-2014, entry version 44.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase;
GN   Name=lacZ; OrderedLocusNames=BWG_3744;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/JB.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L.,
RA   Reeves P.R., Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational
RT   events in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC   -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3-
CC       phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O.
CC   -!- COFACTOR: Binds 1 sodium ion per monomer (By similarity).
CC   -!- COFACTOR: Binds 2 magnesium ions per monomer (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the TrpA family.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
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DR   EMBL; CP001396; ACR62057.1; -; Genomic_DNA.
DR   RefSeq; YP_002928937.1; NC_012759.1.
DR   ProteinModelPortal; C5A125; -.
DR   STRING; 595496.BWG_3744; -.
DR   EnsemblBacteria; ACR62057; ACR62057; BWG_3744.
DR   GeneID; 7954107; -.
DR   KEGG; ebw:BWG_3744; -.
DR   PATRIC; 18277261; VBIEscCol60876_4092.
DR   eggNOG; COG3250; -.
DR   HOGENOM; HOG000252443; -.
DR   KO; K01190; -.
DR   OMA; HRCAWDQ; -.
DR   OrthoDB; EOG6XWV0T; -.
DR   ProtClustDB; PRK09525; -.
DR   BioCyc; ECOL595496:GI18-3906-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
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:0004834; F:tryptophan synthase activity; IEA:InterPro.
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; 3.20.20.70; -; 1.
DR   Gene3D; 3.20.20.80; -; 1.
DR   HAMAP; MF_01687; Beta_gal; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR002028; Trp_synthase_suA.
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   Pfam; PF00290; Trp_syntA; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF49303; SSF49303; 2.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51366; SSF51366; 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   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Glycosidase; Hydrolase; Lyase; Magnesium;
KW   Metal-binding; Sodium; Tryptophan biosynthesis.
FT   REGION      594    597       Substrate binding (By similarity).
FT   ACT_SITE    518    518       Proton donor (By similarity).
FT   ACT_SITE    594    594       Nucleophile (By similarity).
FT   METAL       258    258       Sodium (By similarity).
FT   METAL       473    473       Magnesium 1 (By similarity).
FT   METAL       475    475       Magnesium 1 (By similarity).
FT   METAL       518    518       Magnesium 1 (By similarity).
FT   METAL       654    654       Magnesium 2 (By similarity).
FT   METAL       658    658       Sodium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       661    661       Sodium (By similarity).
FT   BINDING     159    159       Substrate (By similarity).
FT   BINDING     258    258       Substrate (By similarity).
FT   BINDING     518    518       Substrate (By similarity).
FT   BINDING     661    661       Substrate (By similarity).
FT   BINDING    1056   1056       Substrate (By similarity).
FT   SITE        414    414       Transition state stabilizer (By
FT                                similarity).
FT   SITE        448    448       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   1080 AA;  122553 MW;  D1F2C0191BA208FB CRC64;
     MERYESLFAQ LKERKEGAFV PFVTLGDPGI EQSLKIIDTL IEAGADALEL GIPFSDPLAI
     TDSLAVVLQR RDWENPGVTQ LNRLAAHPPF ASWRNSEEAR TDRPSQQLRS LNGEWRFAWF
     PAPEAVPESW LECDLPEADT VVVPSNWQMH GYDAPIYTNV TYPITVNPPF VPTENPTGCY
     SLTFNVDESW LQEGQTRIIF DGVNSAFHLW CNGRWVGYGQ DSRLPSEFDL SAFLRAGENR
     LAVMVLRWSD GSYLEDQDMW RMSGIFRDVS LLHKPTTQIS DFHVATRFND DFSRAVLEAE
     VQMCGELRDY LRVTVSLWQG ETQVASGTAP FGGEIIDERG GYADRVTLRL NVENPKLWSA
     EIPNLYRAVV ELHTADGTLI EAEACDVGFR EVRIENGLLL LNGKPLLIRG VNRHEHHPLH
     GQVMDEQTMV QDILLMKQNN FNAVRCSHYP NHPLWYTLCD RYGLYVVDEA NIETHGMVPM
     NRLTDDPRWL PAMSERVTRM VQRDRNHPSV IIWSLGNESG HGANHDALYR WIKSVDPSRP
     VQYEGGGADT TATDIICPMY ARVDEDQPFP AVPKWSIKKW LSLPGETRPL ILCEYAHAMG
     NSLGGFAKYW QAFRQYPRLQ GGFVWDWVDQ SLIKYDENGN PWSAYGGDFG DTPNDRQFCM
     NGLVFADRTP HPALTEAKHQ QQFFQFRLSG QTIEVTSEYL FRHSDNELLH WMVALDGKPL
     ASGEVPLDVA PQGKQLIELP ELPQPESAGQ LWLTVRVVQP NATAWSEAGH ISAWQQWRLA
     ENLSVTLPAA SHAIPHLTTS EMDFCIELGN KRWQFNRQSG FLSQMWIGDK KQLLTPLRDQ
     FTRAPLDNDI GVSEATRIDP NAWVERWKAA GHYQAEAALL QCTADTLADA VLITTAHAWQ
     HQGKTLFISR KTYRIDGSGQ MAITVDVEVA SDTPHPARIG LNCQLAQVAE RVNWLGLGPQ
     ENYPDRLTAA CFDRWDLPLS DMYTPYVFPS ENGLRCGTRE LNYGPHQWRG DFQFNISRYS
     QQQLMETSHR HLLHAEEGTW LNIDGFHMGI GGDDSWSPSV SAEFQLSAGR YHYQLVWCQK
//
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