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Database: UniProt
Entry: A1A831
LinkDB: A1A831
Original site: A1A831 
ID   BGAL_ECOK1              Reviewed;        1024 AA.
AC   A1A831;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   01-OCT-2014, entry version 55.
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=Ecok1_03270; ORFNames=APECO1_1649;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/JB.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA   Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA   Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain
RT   O1:K1:H7 shares strong similarities with human extraintestinal
RT   pathogenic E. coli genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides. {ECO:0000255|HAMAP-
CC       Rule:MF_01687}.
CC   -!- COFACTOR: Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_01687}.
CC   -!- COFACTOR: Binds 1 sodium ion per monomer. {ECO:0000255|HAMAP-
CC       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; CP000468; ABI99820.1; -; Genomic_DNA.
DR   RefSeq; WP_000177871.1; NC_008563.1.
DR   RefSeq; YP_851535.1; NC_008563.1.
DR   ProteinModelPortal; A1A831; -.
DR   SMR; A1A831; 14-1024.
DR   STRING; 405955.APECO1_1649; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   EnsemblBacteria; ABI99820; ABI99820; APECO1_1649.
DR   GeneID; 4494457; -.
DR   KEGG; ecv:APECO1_1649; -.
DR   PATRIC; 18212098; VBIEscCol127180_0353.
DR   eggNOG; COG3250; -.
DR   HOGENOM; HOG000252443; -.
DR   KO; K01190; -.
DR   OMA; NPPFVPK; -.
DR   OrthoDB; EOG6XWV0T; -.
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   1024       Beta-galactosidase.
FT                                /FTId=PRO_0000366995.
FT   REGION      538    541       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   ACT_SITE    462    462       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   ACT_SITE    538    538       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       202    202       Sodium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       417    417       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       419    419       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       462    462       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       598    598       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   METAL       602    602       Sodium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01687}.
FT   METAL       605    605       Sodium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   BINDING     103    103       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   BINDING     202    202       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   BINDING     462    462       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   BINDING     605    605       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   BINDING    1000   1000       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01687}.
FT   SITE        358    358       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01687}.
FT   SITE        392    392       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01687}.
SQ   SEQUENCE   1024 AA;  116488 MW;  BFDCFEAD47258106 CRC64;
     MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR
     FAWFPAPEAV PESWLECDLP DADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPAENP
     TGCYSLTFNI DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLHA
     GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFQVTT RFNDDFSRAV
     LEAEVQMYGE LRDELRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPE
     LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH
     HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG
     MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD
     PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE MRPLILCEYA
     HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
     QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGRTIEVT SEYLFRHSDN EFLHWMVALD
     GKPLASGEVP LDVGPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ
     WRLAENLSVT LPSASHAIPQ LTTSGTDFCI ELGNKRWQFN RQSGFLSQMW IGDEKQLLTP
     LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA
     HAWQHQGKTL FISRKTYRID GHGEMVINVD VAVASDTPHP ARIGLTCQLA QVSERVNWLG
     LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH LWRGDFQFNI
     SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV
     WCQK
//
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