GenomeNet

Database: UniProt
Entry: R1FBN5_9GAMM
LinkDB: R1FBN5_9GAMM
Original site: R1FBN5_9GAMM 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system