ID BGA2_ECOLI Reviewed; 1030 AA.
AC P06864; P76660; Q2M9D0; Q6BF50;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 4.
DT 27-MAR-2024, entry version 190.
DE RecName: Full=Evolved beta-galactosidase subunit alpha;
DE Short=Beta-gal;
DE EC=3.2.1.23;
DE AltName: Full=Lactase;
GN Name=ebgA; OrderedLocusNames=b3076, JW5511;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2515108; DOI=10.1093/genetics/123.4.635;
RA Hall B.G., Betts P.W., Wootton J.C.;
RT "DNA sequence analysis of artificially evolved ebg enzyme and ebg repressor
RT genes.";
RL Genetics 123:635-648(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3939707; DOI=10.1093/oxfordjournals.molbev.a040372;
RA Stokes H.W., Betts P.W., Hall B.G.;
RT "Sequence of the ebgA gene of Escherichia coli: comparison with the lacZ
RT gene.";
RL Mol. Biol. Evol. 2:469-477(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP SEQUENCE REVISION TO 275 AND 891-892.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP ACTIVE SITE REGIONS.
RX PubMed=6411710; DOI=10.1016/s0021-9258(17)44440-1;
RA Fowler A.V., Smith P.J.;
RT "The active site regions of lacZ and ebg beta-galactosidases are
RT homologous.";
RL J. Biol. Chem. 258:10204-10207(1983).
RN [7]
RP SUBUNIT.
RX PubMed=1540130; DOI=10.1042/bj2820155;
RA Elliott A.C., Sinnott M.L., Smith P.J., Bommuswamy J., Guo Z., Hall B.G.,
RA Zhang Y.;
RT "The catalytic consequences of experimental evolution. Studies on the
RT subunit structure of the second (ebg) beta-galactosidase of Escherichia
RT coli, and on catalysis by ebgab, an experimental evolvant containing two
RT amino acid substitutions.";
RL Biochem. J. 282:155-164(1992).
CC -!- FUNCTION: The wild-type enzyme is an ineffective lactase. Two classes
CC of point mutations dramatically improve activity of the enzyme.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta subunits.
CC {ECO:0000269|PubMed:1540130}.
CC -!- INTERACTION:
CC P06864; P32053: intA; NbExp=3; IntAct=EBI-558098, EBI-552967;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57877.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M64441; AAA61971.1; -; Genomic_DNA.
DR EMBL; X52031; CAA36274.1; -; Genomic_DNA.
DR EMBL; X03228; CAA26977.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U18997; AAA57877.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAT48164.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77126.1; -; Genomic_DNA.
DR PIR; A65096; GBECE.
DR RefSeq; WP_001082856.1; NZ_LN832404.1.
DR RefSeq; YP_026199.1; NC_000913.3.
DR AlphaFoldDB; P06864; -.
DR SMR; P06864; -.
DR BioGRID; 4263419; 6.
DR BioGRID; 851899; 6.
DR DIP; DIP-2893N; -.
DR IntAct; P06864; 7.
DR STRING; 511145.b3076; -.
DR DrugBank; DB00581; Lactulose.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PaxDb; 511145-b3076; -.
DR EnsemblBacteria; AAT48164; AAT48164; b3076.
DR GeneID; 947583; -.
DR KEGG; ecj:JW5511; -.
DR KEGG; eco:b3076; -.
DR PATRIC; fig|511145.12.peg.3170; -.
DR EchoBASE; EB0248; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_6; -.
DR InParanoid; P06864; -.
DR OMA; WCDHGIL; -.
DR OrthoDB; 9758603at2; -.
DR PhylomeDB; P06864; -.
DR BioCyc; EcoCyc:EG10252-MONOMER; -.
DR SABIO-RK; P06864; -.
DR PRO; PR:P06864; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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:0005990; P:lactose catabolic process; IBA:GO_Central.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; 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 PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
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; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..1030
FT /note="Evolved beta-galactosidase subunit alpha"
FT /id="PRO_0000057651"
FT ACT_SITE 449
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:6411710"
FT ACT_SITE 512
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT VARIANT 92
FT /note="D -> N (improve activity)"
FT VARIANT 93
FT /note="E -> K (improve activity)"
FT VARIANT 976
FT /note="W -> C (improve activity)"
FT VARIANT 978
FT /note="S -> G (improve activity)"
FT CONFLICT 275
FT /note="S -> T (in Ref. 1, 2 and 3; AAA57877)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="A -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="T -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="R -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="M -> MM (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 891..892
FT /note="ST -> QA (in Ref. 1, 2 and 3; AAA57877)"
FT /evidence="ECO:0000305"
FT CONFLICT 1026
FT /note="S -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1030 AA; 117879 MW; FEC4D7A558C6EE94 CRC64;
MNRWENIQLT HENRLAPRAY FFSYDSVAQA RTFARETSSL FLPLSGQWNF HFFDHPLQVP
EAFTSELMAD WGHITVPAMW QMEGHGKLQY TDEGFPFPID VPFVPSDNPT GAYQRIFTLS
DGWQGKQTLI KFDGVETYFE VYVNGQYVGF SKGSRLTAEF DISAMVKTGD NLLCVRVMQW
ADSTYVEDQD MWWSAGIFRD VYLVGKHLTH INDFTVRTDF DEAYCDATLS CEVVLENLAA
SPVVTTLEYT LFDGERVVHS SAIDHLAIEK LTSASFAFTV EQPQQWSAES PYLYHLVMTL
KDANGNVLEV VPQRVGFRDI KVRDGLFWIN NRYVMLHGVN RHDNDHRKGR AVGMDRVEKD
LQLMKQHNIN SVRTAHYPND PRFYELCDIY GLFVMAETDV ESHGFANVGD ISRITDDPQW
EKVYVERIVR HIHAQKNHPS IIIWSLGNES GYGCNIRAMY HAAKALDDTR LVHYEEDRDA
EVVDIISTMY TRVPLMNEFG EYPHPKPRII CEYAHAMGNG PGGLTEYQNV FYKHDCIQGH
YVWEWCDHGI QAQDDHGNVW YKFGGDYGDY PNNYNFCLDG LIYSDQTPGP GLKEYKQVIA
PVKIHARDLT RGELKVENKL WFTTLDDYTL HAEVRAEGET LATQQIKLRD VAPNSEAPLQ
ITLPQLDARE AFLNITVTKD SRTRYSEAGH PIATYQFPLK ENTAQPVPFA PNNARPLTLE
DDRLSCTVRG YNFAITFSKM SGKPTSWQVN GESLLTREPK INFFKPMIDN HKQEYEGLWQ
PNHLQIMQEH LRDFAVEQSD GEVLIISRTV IAPPVFDFGM RCTYIWRIAA DGQVNVALSG
ERYGDYPHII PCIGFTMGIN GEYDQVAYYG RGPGENYADS QQANIIDIWR STVDAMFENY
PFPQNNGNRQ HVRWTALTNR HGNGLLVVPQ RPINFSAWHY TQENIHAAQH CNELQRSDDI
TLNLDHQLLG LGSNSWGSEV LDSWRVWFRD FSYGFTLLPV SGGEATAQSL ASYEFGAGFF
STNLHSENKQ
//
