ID R1FBN5_9GAMM Unreviewed; 1020 AA.
AC R1FBN5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|HAMAP-Rule:MF_01687};
DE Short=Beta-gal {ECO:0000256|HAMAP-Rule:MF_01687};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|HAMAP-Rule:MF_01687};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|HAMAP-Rule:MF_01687};
GN Name=lacZ {ECO:0000256|HAMAP-Rule:MF_01687,
GN ECO:0000313|EMBL:EOD57062.1};
GN ORFNames=G113_00265 {ECO:0000313|EMBL:EOD57062.1};
OS Aeromonas molluscorum 848.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1268236 {ECO:0000313|EMBL:EOD57062.1, ECO:0000313|Proteomes:UP000013526};
RN [1] {ECO:0000313|EMBL:EOD57062.1, ECO:0000313|Proteomes:UP000013526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=848 {ECO:0000313|EMBL:EOD57062.1,
RC ECO:0000313|Proteomes:UP000013526};
RX PubMed=23788549;
RA Spataro N., Farfan M., Albarral V., Sanglas A., Loren J.G., Fuste M.C.,
RA Bosch E.;
RT "Draft Genome Sequence of Aeromonas molluscorum Strain 848TT, Isolated from
RT Bivalve Molluscs.";
RL Genome Announc. 1:E00382-13(2013).
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 Evidence={ECO:0000256|ARBA:ARBA00001412, ECO:0000256|HAMAP-
CC Rule:MF_01687};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01687};
CC Note=Binds 2 magnesium ions per monomer. {ECO:0000256|HAMAP-
CC Rule:MF_01687};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01687};
CC Note=Binds 1 sodium ion per monomer. {ECO:0000256|HAMAP-Rule:MF_01687};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01687}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|HAMAP-Rule:MF_01687}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOD57062.1}.
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DR EMBL; AQGQ01000001; EOD57062.1; -; Genomic_DNA.
DR RefSeq; WP_005890703.1; NZ_AQGQ01000001.1.
DR AlphaFoldDB; R1FBN5; -.
DR PATRIC; fig|1268236.3.peg.55; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000013526; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
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 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; 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 PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; LACTASE; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW Rule:MF_01687};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01687};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01687};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01687};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_01687}.
FT DOMAIN 750..1020
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT ACT_SITE 462
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT ACT_SITE 538
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 204
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 417
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 419
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 462
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 538..541
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 598
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 602
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 605
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 605
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 998
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT SITE 358
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT SITE 392
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1020 AA; 114883 MW; D7607DBBECCBE54A CRC64;
MLREILARRD WQNQGVTSVN RLAAHTPLAS WRDEEAARAD LPSDSRLLLD GDWHFSFFET
PELVPEQWVQ QDLADACLIR VPGNWQLDGA YPGTRPQTDG PIYTNIKYPF PCDPPRVPSQ
NPTGCYSRHL HLPANWLASG QTRIILDGVS SACHLFCNGH WVGYSQDSRL PAEFDLTPCL
REGENRIALL VLRWSDGSYL EDQDMWWLSG IFRSVSLLHK PERHIADLRI TPQLDACYRD
AQLKLAVQVA GGAGLSLRAV LYQGEHPVAC LEQGVGTAPI DEKGRFEDRA ELMVKVDNPA
KWSAEAPHLY RLTLTLLDEQ GAPIESEAHD VGFRAVEIQG GLLRLNGQPL LIRGANRHEH
DPTRGHAIDV TSMARDLTLM KQHNFNAVRC AHYPNHPEFY RLCDRLGLYV VDEANLETHG
MSPMGRLAQD SAWATAFLER ITRLVARDFN HPSIIIWSLG NESGYGAAHD AMYAWVKGTD
PSRPVQYEGG GANTPATDII CPMYARTHQD QPFPAVPKWA LAKWIGLPGE QRPLILCEYA
HAMGNSLGGF ADYWQAFRDH PRLQGGFVWD WVDQGLDKLT GDGRHFWAYG GDFGDLQNDR
QFCINGLLFP DRTPHPALFE AKRAQQPFRF KLLSHNPLVV HIESELLFRA TDNERLRWRL
CEQGVVLREG ECPLTLAPQA AHSLTLLPTL PAFAAGTLAW LDLCIEQVDA TPWSAADHEL
ARQQFSLPTP LALPQPRTPA RLEERADTWQ VLAGESQWWL DKASGRITGW RKGGRERLLG
ELADHFYRAP LDNDIGTSEA DHQDPHSWIA RWQQAGLGEL NHRCLGITRV GEASLQVEHG
YFVDEQLRIL TRWRHEFDAG GAMTLAIEAL VSDDFPSLPR IGASLWLAET VDSIEWLGRG
PHENYPDRCL SADLGRWQLP IAELHTPYIF PTDNGLRSQV CELQLGDLRV EGEFHFSISP
YRQAQLAEAR HQTDLTAEGG IHLCLDGFYM GIGGDDSWSQ SVRPEYWLTP GRYYWNSILS
//