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Database: UniProt/SWISS-PROT
Entry: BGAL_YERP3
LinkDB: BGAL_YERP3
Original site: BGAL_YERP3 
ID   BGAL_YERP3              Reviewed;        1066 AA.
AC   A7FH78;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   19-FEB-2014, entry version 48.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase;
GN   Name=lacZ; OrderedLocusNames=YpsIP31758_1629;
OS   Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=349747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP 31758;
RX   PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA   Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA   Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT   "The complete genome sequence of Yersinia pseudotuberculosis IP31758,
RT   the causative agent of Far East scarlet-like fever.";
RL   PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS47972.1; -; Genomic_DNA.
DR   RefSeq; YP_001400606.1; NC_009708.1.
DR   ProteinModelPortal; A7FH78; -.
DR   STRING; 349747.YpsIP31758_1629; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   EnsemblBacteria; ABS47972; ABS47972; YpsIP31758_1629.
DR   GeneID; 5387098; -.
DR   KEGG; ypi:YpsIP31758_1629; -.
DR   PATRIC; 18632074; VBIYerPse15693_1985.
DR   eggNOG; COG3250; -.
DR   HOGENOM; HOG000252443; -.
DR   KO; K01190; -.
DR   OMA; QERWYEL; -.
DR   OrthoDB; EOG6XWV0T; -.
DR   ProtClustDB; PRK09525; -.
DR   BioCyc; YPSE349747:GH71-1669-MONOMER; -.
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: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; 3.20.20.80; -; 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; SSF49303; SSF49303; 2.
DR   SUPFAM; SSF49785; SSF49785; 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   Complete proteome; Glycosidase; Hydrolase; Magnesium; Metal-binding;
KW   Sodium.
FT   CHAIN         1   1066       Beta-galactosidase.
FT                                /FTId=PRO_0000367022.
FT   REGION      553    556       Substrate binding (By similarity).
FT   ACT_SITE    477    477       Proton donor (By similarity).
FT   ACT_SITE    553    553       Nucleophile (By similarity).
FT   METAL       209    209       Sodium (By similarity).
FT   METAL       432    432       Magnesium 1 (By similarity).
FT   METAL       434    434       Magnesium 1 (By similarity).
FT   METAL       477    477       Magnesium 1 (By similarity).
FT   METAL       613    613       Magnesium 2 (By similarity).
FT   METAL       617    617       Sodium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       620    620       Sodium (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     209    209       Substrate (By similarity).
FT   BINDING     477    477       Substrate (By similarity).
FT   BINDING     620    620       Substrate (By similarity).
FT   BINDING    1041   1041       Substrate (By similarity).
FT   SITE        373    373       Transition state stabilizer (By
FT                                similarity).
FT   SITE        407    407       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   1066 AA;  123440 MW;  12645739A7CC53AC CRC64;
     MTSQEKVPFQ VQLSLPQILS RRDWENPQIT QYHRLEAHPP FHSWRDVESA QKDRPSPQQQ
     TLNGLWSFSY FTQPEAVPEH WVRCDLAEAK PLPVPANWQL HGYDAPIYTN IQYPIPVNPP
     RVPDLNPTGC YSRDFTLEPS WLASGKTRII FDGVSSAFYL WCNGQWVGYS QDSRLPAEFD
     LTPYLQAGSN RIAVLVLRWS DGSYLEDQDM WRMSGIFRDV KLLHKPEIHL RDIHIMTHLS
     PEFTSANLEV MAAVNIPSLQ LNDPQVTGSY QLRVQLWLAD KLVASLQQPL GTQAIDERGP
     YTDRTQLVLR IDQPLLWSAE QPTLYRAVVS LLNHQQELIE AEAYDVGFRQ VAIHQGLLKI
     NGKAVLIRGV NRHEHHPQTG QAIDEESLLQ DILLMKQHNF NAVRCSHYPN HPLWYRLCDR
     YGLYVVDEAN IETHGMQPMS RLSDDPSWFS AFSERVTRMV QRDRNHPCII IWSLGNESGH
     GATHDALYRW IKTNDPTRPV QYEGGGANTL ATDILCPMYA RVDEDQPFPA VPKWSIKKWV
     GLPNESRPLI LCEYAHAMGN SFGGFARYWQ AFRQYPRLQG GFIWDWVDQS LTHHNDHGQP
     YWAYGGDFGD TPNDRQFCMN GLVFPDRSPH PSLYEAQCAQ QFFQFSLLST TPLVINITSE
     YLFRESDNEQ LYWRIMLEGE SMLEGSQPLN LSPESSQCYR LAEKLPTLNK PGQLWLNVEI
     RQPKETPWSP AQHRSAWHQW RLPQPLFSPS SDLTNATAHY APQLQHNLQL QHNRQLQHDL
     QLQQDEQHIK VTYQQQCWQF SRQTGRLAQW WVADKPMLLR PLQDQFVRAP LDNDIGISEA
     THIDPNAWVE RWKKAGMYQL QQRCLSLHVD HLSHSVQISA EYGYEFEQEP LLHSHWVYRF
     DRHGRMTIDV NVRIATSLPA PARIGMCCQL ADISPTVDWL GLGPHENYPD RQLAAQYGHW
     SLPLEQMHTA YIFPSENGLR CNTHTLNYGR WTLTGDFHFG ISRYSTQQLM VTSHQHLLEP
     EEGTWLNIDG FHMGVGGDDS WSPSVHIDDI LTRETYQYQI CWQYKV
//
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