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-MAY-2013, 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=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.
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; CP000468; ABI99820.1; -; Genomic_DNA.
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; TIREYHI; -.
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 1024 Beta-galactosidase.
FT /FTId=PRO_0000366995.
FT REGION 538 541 Substrate binding (By similarity).
FT ACT_SITE 462 462 Proton donor (By similarity).
FT ACT_SITE 538 538 Nucleophile (By similarity).
FT METAL 202 202 Sodium (By similarity).
FT METAL 417 417 Magnesium 1 (By similarity).
FT METAL 419 419 Magnesium 1 (By similarity).
FT METAL 462 462 Magnesium 1 (By similarity).
FT METAL 598 598 Magnesium 2 (By similarity).
FT METAL 602 602 Sodium; via carbonyl oxygen (By
FT similarity).
FT METAL 605 605 Sodium (By similarity).
FT BINDING 103 103 Substrate (By similarity).
FT BINDING 202 202 Substrate (By similarity).
FT BINDING 462 462 Substrate (By similarity).
FT BINDING 605 605 Substrate (By similarity).
FT BINDING 1000 1000 Substrate (By similarity).
FT SITE 358 358 Transition state stabilizer (By
FT similarity).
FT SITE 392 392 Transition state stabilizer (By
FT similarity).
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
//
