ID D2Y9E3_VIBMI Unreviewed; 1025 AA.
AC D2Y9E3;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:EEW08669.1};
GN ORFNames=VMB_01400 {ECO:0000313|EMBL:EEW08669.1};
OS Vibrio mimicus VM603.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=671074 {ECO:0000313|EMBL:EEW08669.1, ECO:0000313|Proteomes:UP000004827};
RN [1] {ECO:0000313|EMBL:EEW08669.1, ECO:0000313|Proteomes:UP000004827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VM603 {ECO:0000313|EMBL:EEW08669.1,
RC ECO:0000313|Proteomes:UP000004827};
RX PubMed=19860885; DOI=10.1186/1471-2148-9-258;
RA Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T.,
RA Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.;
RT "Genomic taxonomy of Vibrios.";
RL BMC Evol. Biol. 9:258-258(2009).
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:EEW08669.1}.
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DR EMBL; ACYU01000013; EEW08669.1; -; Genomic_DNA.
DR AlphaFoldDB; D2Y9E3; -.
DR Proteomes; UP000004827; 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; 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; BETA-GALACTOSIDASE; 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.
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};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_01687}.
FT DOMAIN 749..1022
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT ACT_SITE 464
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT ACT_SITE 540
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 203
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 203
FT /ligand="substrate"
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 421
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 464
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 540..543
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 600
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 604
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 607
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 607
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 1000
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT SITE 360
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT SITE 394
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1025 AA; 118827 MW; DC894BC50CCB9A87 CRC64;
MEEDLMRNFS DILLSQDWQN PHIVKWHSRT PHVPLHSYRN EQEARLATGG TRCSLNGEWR
FALFEQPEAV EPAVIDVDFD DSAWAHIPVP SNWQMQGFDK PIYTNIQYPF PDRPPYVPQD
NPTGCYRHRF TLEKQALSES TRIVFDGVNS AFHLWCNGQW VGYSQDSRLP AEFELTPYLQ
EGENLLVAMV LRWSDGSYLE DQDMWWLSGI FRYVYLYRKP HLAIEDFFIR TELDALYQHA
ELRVETRLSQ VTRQHQVQIA LFDAQGECVA RAQALHTGQR VVDEKGAWHD KTEHSLTVCS
PKLWSDEAPY LYRCVISLLD EHGAPIEFES AAVGFRKVEI DQGLLKLNGQ PLLIRGVNRH
EHHPELGHVM DEASMRRDIE LMKQNNFNAV RTAHYPNHPR WYELCDEYGL YVVDEANLET
HGQFPMSRLS NDPQWVNAYL QRMIGMVERD KNHPCVIIWS LGNESGIGTN HHTMCQWTKQ
RDPSRPVQYE GGGANTAATD IICPMYARVD QHQPHPAVPK YALKNWISLP EETRPLILCE
YAHAMGNSLG AFYKYWLAFR EFPRLQGGFI WDWVDQGISK WDAEGRHYWG YGGDFGDTIN
DRQFCINGLL FPDRSPHPAL HEVKKVQQPY QFSLSYPKFT IHNERLFAAL SLELVMSVCR
DGQEVYQHRQ PIDIAPQGTI TLDLEPQHMQ PEYEYHLNVA LLCREDQPWS KAGHCIASEQ
WCLQPRRITL PKIAHAPVPQ WQQDGDKVRV EASNHQWQFS CQTGLLEHWW QNSLPVLSEP
LRDNFYRAVL DNDIGTSEAQ HLDPNSWIAR WHSAGLDKLR VECEDLRVTT LSECVEVVVD
FSHYHQQNLV LRSFWCYQIF GDARVDLNVE VMLCSDLPPL PRVGLTLALP STERDVYWFG
RGPHENYPDR LQSAYVDQYT ASIDELHTPY IFPTENGLRC DTRQLQVGVL EVEGHFHFSL
SRYSQAMLDK AKHTNELVAG DKLYLNLDAQ HMGVGGDDSW SQSVHPEFLL TQQRYQYQLT
LRVKA
//
