ID A0A014NCD6_9GAMM Unreviewed; 1027 AA.
AC A0A014NCD6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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:EXU77073.1};
GN ORFNames=BG55_01770 {ECO:0000313|EMBL:EXU77073.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU77073.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU77073.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU77073.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) 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}.
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:EXU77073.1}.
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DR EMBL; JFHN01000018; EXU77073.1; -; Genomic_DNA.
DR RefSeq; WP_034933648.1; NZ_JFHN01000018.1.
DR AlphaFoldDB; A0A014NCD6; -.
DR STRING; 69222.BG55_01770; -.
DR PATRIC; fig|69222.5.peg.382; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000019918; 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}; Reference proteome {ECO:0000313|Proteomes:UP000019918};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_01687}.
FT DOMAIN 752..1025
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 107
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 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 1003
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 1027 AA; 117360 MW; 31EEB15A3CC61E57 CRC64;
MRTSVSPVLS LQQQLSRRDW ENPGVTQINR LPAHPPFNSY RRAVDARDEI PGSDSRQLLN
GEWKFSYFPQ PEAVPQGWLE QDLPDASLLT VPSNWQLAGF DAPIYTNVQY PIPVDPPRVP
EMNPTGCYSL TFMHDEKPQQ QTRIIFDGVS SAFYLWCNGQ FIGYSQDSRL PAEFDLTPVL
HSGQNRLAVL VLRWSDGSYL EDQDMWRMSG IFRDVSLLHK PVLHLRDVQI ETHLSAEYHT
ARLQVLAVCS QPLAEACQVE VALWQQQSCI ARLRQPLSSQ IIDERGHYRD RTRLTLTVAQ
PELWSAETPQ LYRATITLFD ERGKEMETEA FDVGFRKVEI HQGLLKLNGK PLLIRGTNRH
EHHPENGQVM DEATMIRDIK LMKQHNFNAV RCSHYPNHPL WYRLCDRYGL YVVDEANIET
HGMQPMNQLS DDPLWFNAFS ERVTRMVQRD RNHACIIIWS LGNESGHGSS HDALYRWIKS
TDATRPVQYE GGGADTAATD IICPMYARVD QDQPFPAVPK WAIKKWISLP EETRPLILCE
YAHAMGNSFG GFAKYWQAFR EFPRLQGGFV WDWVDQSLTR YDQHGQPWQA YGGDFGDKPN
DRQFCMNGLV FADRTPHPSL FEAQRAQQFF QFSLESCAPL RITIASEYLF RATDNEQLEW
RIEQNGRAVA EGRQPLTLAA EGRLSLELGA LPELNGEVWL CVAIVQPQAT AWSEAGHRVA
WDQWRLPALL QRPVATEGGQ KPLLSESETE IIVSWQQQSW HFCRQSGELV QWCSENQPQL
LTPLRDAFVR APVDNDIGIS EVTRVDPNAW VERWQWAGFY QLQSELLAFS YDQTADGVQL
ATTQAWQSDG RICFLSRKQY RFNSRGEMNI QTDVTVAAGL PAPARIGLCC QLRQAAETVS
WLGLGPHENY PDRRLAAQFS RWSLPLDSLY TPYVFPGENG LRGGTKELTF GTLTVRGDFH
FSLNRYGQEQ LRKTSHRHLL KEEDGCWLSV DGYHMGVGGD DSWSPSVSPE FLLTASHYAY
AVTLSIR
//
