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 01-MAY-2013, 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=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; FFRAPLD; -.
DR ProtClustDB; PRK09525; -.
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 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
//
