GenomeNet

Database: UniProt
Entry: R8ARX1_PLESH
LinkDB: R8ARX1_PLESH
Original site: R8ARX1_PLESH 
ID   R8ARX1_PLESH            Unreviewed;      1040 AA.
AC   R8ARX1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   28-JUN-2023, entry version 49.
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:EON89071.1};
GN   ORFNames=PLESHI_07985 {ECO:0000313|EMBL:EON89071.1};
OS   Plesiomonas shigelloides 302-73.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Plesiomonas.
OX   NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON89071.1, ECO:0000313|Proteomes:UP000014012};
RN   [1] {ECO:0000313|EMBL:EON89071.1, ECO:0000313|Proteomes:UP000014012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=302-73 {ECO:0000313|EMBL:EON89071.1,
RC   ECO:0000313|Proteomes:UP000014012};
RX   PubMed=23814109;
RA   Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT   "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL   Genome Announc. 1:e00404-13(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:EON89071.1}.
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; AQQO01000047; EON89071.1; -; Genomic_DNA.
DR   RefSeq; WP_010863220.1; NZ_KB944508.1.
DR   AlphaFoldDB; R8ARX1; -.
DR   PATRIC; fig|1315976.3.peg.1579; -.
DR   HOGENOM; CLU_002346_0_2_6; -.
DR   OrthoDB; 9758603at2; -.
DR   Proteomes; UP000014012; 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; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
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; PS00608; GLYCOSYL_HYDROL_F2_2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000014012};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_01687}.
FT   DOMAIN          761..1035
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
FT   ACT_SITE        457
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   ACT_SITE        533
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         198
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         412
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         414
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         457
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         457
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         533..536
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         593
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         597
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         600
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         600
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   BINDING         1013
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   SITE            353
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT   SITE            387
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
SQ   SEQUENCE   1040 AA;  119033 MW;  E7AB3D9C1787D62E CRC64;
     MNAFSSILQR RDWENPQSVN IHCLQAHSPL SSFRSMTDAR DGVRAQRRLL NGEWKFKLFE
     APEWVEGAFI APHFDDTPWD NIPVPSNWQL HGYDKPIYAN VKYPFNVNPP FVPQDNPTGC
     YRTTFTLTDA ELTNTQRIIF DGVNSAFHLW CNGHWVGYSQ DSRLPAEFDL TPYLTAGENT
     LAVMVLRWSD GSYLEDQDMW WLSGIFRDVT LLSKPQYCIT DVFVTPDLDA CYRDGTLSIQ
     THLCAPETYQ VQVQLFEGEQ PITEPCIARP HNRRIDERGS WRDVVFHSLH VREPKQWSAE
     TPTLYRVVIS LLNEQGQHIE SEAYQVGFRK VEIIDGQLKL NGKALLIRGV NRHEHHPTLG
     HVMTEEDMIR DICLMKQHNF NAVRTAHYPN HPRWYELCDQ YGLYVCDEAN IETHGMQPMC
     RLSSDPQWAH AYMSRYTQMV LRDKNHPSII IWSLGNESGH GSNHDAMYGW SKNFDPSRPV
     QYEGGGANSS ATDIIAPMYA RVETTLADEA VPKWPIKKWI SLPNEQRPLI LCEYAHAMGN
     SLGSFNDYWD AFREYPRLQG GFIWDWVDQG LSQWDEHGQH FWAYGGDFGD EINDRQFCIN
     GLVFPDRTIH PTLEEAKYCQ RMLTVTLQQQ RAADFVLLVR NEQLFRATDN EVLHWSLLEN
     GLVIQTGSVA LNLAADSQQT LAIPCHFQPK AQAVYHLNTD ITLLADTPWA PTGHVCASEQ
     FALTHHAGLH LPCFEPHINA LPAPQLSHNV TRNAQTLQVS SVDNQVQWTW DCHSGLLTDW
     RIAGQAQFLA APHDNFFRAP LDNDIGISEV DNVDPNAWAC RWDLAGINQW TRECIRCQGE
     MLQQTAQVSS TFVYQFNGVV QAITTWTYTL HNSGEMQLAI DVQLAQHLPP MPRIGLELQL
     PLHDNQTSVS WFGLGPFENY PDRLAAARMG VYTQPLAAMH TPYIFPTDSG LRCNTQKLQV
     NQLEISGQFH FAVSRYAQTH LAAAKHTHEL REEDKIYVRI DHQHMGVGGD DSWSPSVHQA
     FQLTDKTYQY RVSMKPRTHH
//
DBGET integrated database retrieval system