BGAL_SERP5
ID BGAL_SERP5 Reviewed; 1029 AA.
AC A8GGN3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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}; OrderedLocusNames=Spro_3173;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000826; ABV42273.1; -; Genomic_DNA.
DR RefSeq; WP_012145891.1; NC_009832.1.
DR AlphaFoldDB; A8GGN3; -.
DR SMR; A8GGN3; -.
DR STRING; 399741.Spro_3173; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PRIDE; A8GGN3; -.
DR EnsemblBacteria; ABV42273; ABV42273; Spro_3173.
DR KEGG; spe:Spro_3173; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_6; -.
DR OMA; SNWQLQG; -.
DR OrthoDB; 245411at2; -.
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-UniRule.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
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; Sodium.
FT CHAIN 1..1029
FT /note="Beta-galactosidase"
FT /id="PRO_0000367008"
FT ACT_SITE 461
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT ACT_SITE 537
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 203
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 416
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 537..540
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 597
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 601
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 604
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 604
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 1002
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 357
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 391
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1029 AA; 118303 MW; 9FFADB850DE58679 CRC64;
MSSLPYPSLK DLLARRDWQN PACTHYQRLA AHPPFSSWRN LNAARDDKSS ESRQILNGDW
QFSYFDKPQA VPDGWLQQDL TDADTLAVPS NWQLAAYDAP IYTNVRYPIP VNPPQVPEEN
PTGCYSRQFT VDPAWLAEGQ TRIIFDGVNS AFYLWCNGHW VGYSQDSRLP AEFDLSPWLQ
AGENRLAVMV LRWCDGSYLE DQDMWRMSGI FRDVSLLHKP ATHLSDIRIT TPLYDSFRRG
ELVAEVHINQ PAQHRVQLQL WRDGQLVGEK TQAFGSEIID ERGAYEDRTT LCLPVEQPAL
WSAETPTLYR ATVTLLSPEG KIIEVEAYDV GFRQVEISNG LLKLNGQPLL IRGTNRHEHH
PQHGQVMDEA TMRHDILLMK QHNFNAVRCS HYPNHPLWYR LCDRYGLYVV DEANIETHGM
QPMNRLSDDP LWLPAMSERV TRMVQRDRNH PCIIIWSLGN ESGHGCNHDA LYRWVKTQDP
TRPVQYEGGG ANSAATDIIC PMYARVDQDQ PFPAVPKWSI KKWIGLPDEH RPLILCEYAH
AMGNSFGGFD RYWQAFRQYP RLQGGFVWDW VDQALTRSDE NGNPYWAYGG DFGDTPNDRQ
FCLNGLVFPD RTPHPALFEA QRAQQFFQFT FDAETLTLTV NSEYLFRQTD NERLNWRLEL
DGTERASGSF DLNLLPQSSA SFPLLERLPM LHQPGELWLN VEVVQPLATD WSEANHRCAW
DQWLVPRTLH FAPPAVAGSA PQLSQNDQTI DITHGHQRWQ FTRHDGCLSQ WWQHDHSQLL
TPLRDNFIRA PLDNDIGISE VERIDPNAWV ERWKLAGMYR LEERCTLLQA DQLSDGVRVV
SEHLFEADGQ TLLRSRKQWL FDSEGAVSIS VDVDIAASLP PPARIGLSCQ LKEIHPQAQW
LGLGPHENYP DRRLAAQFGR WQQPLEALHT PYIFPGENGL RCETRSLLYG GWHIDGRFHF
SLSRYGLRQL MECSHQHLLQ PEAGTWLSLD GFHMGVGGDD SWSPSVNQDY LLSGSHYHYQ
LRLKRAERS
