ID C5A125_ECOBW Unreviewed; 1080 AA.
AC C5A125;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 01-MAY-2013, 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=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 -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage
CC of indoleglycerol phosphate to indole and glyceraldehyde 3-
CC phosphate (By similarity).
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 + 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 -!- SUBUNIT: Tetramer of two alpha and two beta chains (By
CC 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; DFHVATH; -.
DR ProtClustDB; PRK09525; -.
DR BioCyc; ECOL595496:GI18-515-MONOMER; -.
DR UniPathway; UPA00035; UER00044.
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:0004834; F:tryptophan synthase activity; IEA:InterPro.
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; 3.20.20.70; -; 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; 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 SUPFAM; SSF51366; RibP_bind_barrel; 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
//
