ID A0A0U5LA16_9GAMM Unreviewed; 1035 AA.
AC A0A0U5LA16;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=lacZ1 {ECO:0000313|EMBL:CUU25995.1};
GN Synonyms=lacZ {ECO:0000256|HAMAP-Rule:MF_01687};
GN ORFNames=EM595_p0297 {ECO:0000313|EMBL:CUU25995.1};
OS Duffyella gerundensis.
OG Plasmid pEM01 {ECO:0000313|Proteomes:UP000059419}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Duffyella.
OX NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU25995.1, ECO:0000313|Proteomes:UP000059419};
RN [1] {ECO:0000313|Proteomes:UP000059419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC PLASMID=pEM01 {ECO:0000313|Proteomes:UP000059419};
RA Blom J.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; LN907828; CUU25995.1; -; Genomic_DNA.
DR RefSeq; WP_067436342.1; NZ_LN907828.1.
DR AlphaFoldDB; A0A0U5LA16; -.
DR KEGG; ege:EM595_p0297; -.
DR PATRIC; fig|1619313.3.peg.3916; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000059419; Plasmid pEM01.
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}; Reference proteome {ECO:0000313|Proteomes:UP000059419};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_01687}.
FT DOMAIN 760..1033
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT ACT_SITE 469
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT ACT_SITE 545
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 208
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 424
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 426
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 545..548
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 605
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 609
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 612
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 612
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT BINDING 1011
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT SITE 365
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
FT SITE 399
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1035 AA; 118000 MW; 3285F538D8A16ADA CRC64;
MRHLDRPASS GLQFHDVLAR EDWQNQTITH LNRLAAHPTF ASWRDLGAAR ENQPSAQRRL
LDGQWQFAYA RSPFEVDASW LESDLAESRS TTVPSNWQMA GYDAPIYTNV RYPIETTPPR
VPEENPTGCY SLTFSVEENW QTEGQTQIIF DGVNSAFHLW CNGEWIGYSQ DSRLPAAFDL
SAALKPGENR LCVMVMRWSA GTWLEDQDMW RMSGIFRSVW LLNKPTLHLS DVQLTPELDA
LYRDAELVVN VSVAGLKQLP ENLTISVEVW DNAEQVASHR QPPGSPTIDE RGNYAERAVM
RLPVARPALW SAETPHCYRA VVSLWGGDTL IEAEAWDIGF RRVEISNGLL KLNGKPLLIR
GVNRHEHHPE RGQVVTEEDM VQDILLMKQH NFNAVRCSHY PNVPRWYELC NRYGLYVVDE
ANIETHGMVP MNRLSDDPAW LPAWSARVTR MVQCNRNHPS IIIWSLGNES GGGGNHEAMY
HWLKRNDPSR PVQYEGGGAN STTTDILCPM YARVESDLLI PAVPKWGIKK WISLPGEQRP
LILCEYAHAM GNSLGNYADY WQAFRDYPRL QGGFVWDWAD QAITKTFDDG SVGWAYGGDF
GDKPNDRQFC MNGLVFPDRR PHPSLIEAMH AQQYFQFALV SQNPLRISLT SEYLFRTTDN
EELHWRVQAS GETLAAGHTT LALAPEAYAE LTLSEELTLP AGATEVWLTL EVIQPDRTAW
SDAGHRVAWQ QFALAAPLVL QTPSPAADAP ELNHSDTAWT VRSGVQQWII DRQSGLLTHW
QVDGVEQLLT PLRDQFVRAP LDNDIGVSEV ERIDPNAWVE RWKSAGLYHL TARCVQCDAQ
RLSHEVVIDS RWHYLSNDDV VIVSHWRMTF DAQGTLHLAI DGERAGTLPP LPRVGLHFQV
PDQHKPVSWL GFGPHENYPD RRTSACFSRW ERPLDEMSTP YIFPTENGLR CDSKALDWGR
WHVSGDFHFS VQPYSTKQLM ETDHWHWMQP EDGVWITLDG QHMGVGGDDS WTPSVLQQWL
LLETRWQYQL TLHFQ
//
