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}.
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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
//