BGAL_YERPE
ID BGAL_YERPE Reviewed; 1060 AA.
AC Q7CIZ3; Q74UE1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Beta-galactosidase {ECO:0000255|HAMAP-Rule:MF_01687};
DE Short=Beta-gal {ECO:0000255|HAMAP-Rule:MF_01687};
DE EC=3.2.1.23 {ECO:0000255|HAMAP-Rule:MF_01687};
DE AltName: Full=Lactase {ECO:0000255|HAMAP-Rule:MF_01687};
GN Name=lacZ {ECO:0000255|HAMAP-Rule:MF_01687};
GN OrderedLocusNames=YPO1654, y1817, YP_1785;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01687};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01687};
CC Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC Rule:MF_01687};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01687};
CC Note=Binds 1 sodium ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01687};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01687}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01687}.
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DR EMBL; AE009952; AAM85385.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62012.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL20299.1; -; Genomic_DNA.
DR PIR; AI0201; AI0201.
DR RefSeq; WP_002214048.1; NZ_WUCM01000020.1.
DR RefSeq; YP_002346664.1; NC_003143.1.
DR AlphaFoldDB; Q7CIZ3; -.
DR SMR; Q7CIZ3; -.
DR IntAct; Q7CIZ3; 9.
DR STRING; 214092.YPO1654; -.
DR PaxDb; Q7CIZ3; -.
DR EnsemblBacteria; AAM85385; AAM85385; y1817.
DR EnsemblBacteria; AAS62012; AAS62012; YP_1785.
DR GeneID; 57976920; -.
DR KEGG; ype:YPO1654; -.
DR KEGG; ypk:y1817; -.
DR KEGG; ypm:YP_1785; -.
DR PATRIC; fig|214092.21.peg.2000; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_6; -.
DR OMA; SNWQLQG; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0009341; C:beta-galactosidase complex; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005990; P:lactose catabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.70.98.10; -; 1.
DR HAMAP; MF_01687; Beta_gal; 1.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF16353; DUF4981; 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 Glycosidase; Hydrolase; Magnesium; Metal-binding; Reference proteome;
KW Sodium.
FT CHAIN 1..1060
FT /note="Beta-galactosidase"
FT /id="PRO_0000367015"
FT ACT_SITE 477
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT ACT_SITE 553
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 209
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 434
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 553..556
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 613
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 617
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 620
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 620
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 1035
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 373
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 407
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1060 AA; 122625 MW; 1142D7FC68E46697 CRC64;
MTSQEKVPLQ 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 VPKWSIKKWI
GLPNESRPLI LCEYAHAMGN SFGGFARYWQ AFRQYPRLQG GFIWDWVDQS LTHHNDHGQP
YWAYGGDFGD TPNDRQFCMN GLVFPDRSPH PSLYEAQCAQ QFFQFSLLST TPLVINITSE
YLFRESDNEQ LYWRIMLEGE SVLEGSQPLN LSPESSQCYR LAEKLPTLNK PGQLWLNVEI
RQPKETPWSP AQHRSAWHQW RLPQPLFSPS SDLTNATAHY APQLQHNLQL QHDLQLQQDE
QHIKVTYQQQ CWQFSRQTGR LAQWWVADKP MLLRPLQDQF VRAPLDNDIG ISEATHIDPN
AWVERWKKAG MYQLQQRCLS LHVDHLSHSV QISAEYGYEF EQEPLLHSHW VYRFDRHGRM
TIDVNVRIAT SLPAPARIGM CCQLADISPT VEWLGLGPHE NYPDRQLAAQ YGHWSLPLEQ
MHTAYIFPSE NGLRCNTHTL NYGRWTLTGD FHFGISRYST QQLMVTSHQH LLEPEEGTWL
NIDGFHMGVG GDDSWSPSVH IDDILTRETY QYQICWQYKV
