ID V6IUK3_9BACL Unreviewed; 1015 AA.
AC V6IUK3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN ORFNames=P343_14490 {ECO:0000313|EMBL:EST10803.1};
OS Sporolactobacillus laevolacticus DSM 442.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1395513 {ECO:0000313|EMBL:EST10803.1, ECO:0000313|Proteomes:UP000018296};
RN [1] {ECO:0000313|EMBL:EST10803.1, ECO:0000313|Proteomes:UP000018296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 442 {ECO:0000313|EMBL:EST10803.1,
RC ECO:0000313|Proteomes:UP000018296};
RX PubMed=24371202;
RA Wang H., Wang L., Ju J., Yu B., Ma Y.;
RT "Genome Sequence of Sporolactobacillus laevolacticus DSM442, an Efficient
RT Polymer-Grade D-Lactate Producer from Agricultural Waste Cottonseed as a
RT Nitrogen Source.";
RL Genome Announc. 1:e01100-13(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,
CC ECO:0000256|RuleBase:RU361154};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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:EST10803.1}.
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DR EMBL; AWTC01000016; EST10803.1; -; Genomic_DNA.
DR RefSeq; WP_023511125.1; NZ_AWTC01000016.1.
DR AlphaFoldDB; V6IUK3; -.
DR STRING; 1395513.P343_14490; -.
DR PATRIC; fig|1395513.3.peg.2943; -.
DR eggNOG; COG3250; Bacteria.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000018296; 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: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 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; 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|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000018296}.
FT DOMAIN 737..1008
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1015 AA; 117303 MW; 6DAF25BB1C52A9E0 CRC64;
MNNDKPNISW LQDPTIFRVN RLDAHSDHSY YTSDAEAKQG VMQLRQSLNG NWKFSYARNP
QSRVKDFYQM DVDCRCWEDI KVPGHIQLQG YGRPQYSNLT YPWDGISEVG RPPQIPQDYN
PVGSYVNYFT VNQELQTGPL YLSFQGVESA FFVWLNGRFI GYSESSFNPA EFALSDAVVK
GINKLAVEVY QRSTGSWLED QDFWRFSGIF RDVYLYTTPP IHIFDLFVKT DLDHTYRNAE
LKIDLKLQGE KKGNVSAVLC DHLGNEVGIV PESKIQERMQ LRIHCRDVRL WSAEEPYLYL
LKLIVRDERG QIIEIVPQQV GFRKFEIKEK QMCLNGKRIV FKGVNRHEFD CRRGRSVTRQ
DMLWDIKFLK QHNINAVRTS HYPNQSYWYQ LCDEYGVYVI DENNLETHGT WQLHNGTVPE
HVLPGDKPEW HDNVLDRARS LLERDKNHPS VLIWSCGNES YGGKTIFDVS EYFRKADSSR
IVHYEGIFHD RTFNATSDIE SRMYARVEEI KDYLENDPEK PYISCEYMHA MGNSCGGFHE
YTALEDQYPL YQGGFIWDYI DQFLMTKNRY GKTVLAYGGD FDDRPNDDDF CGDGIVYADR
SPSPKVQEIK YLYQNIKLNV CRDGVEVKNQ NLFIDTSGYE LEYSLNREGQ EIMRHRLLVV
VPAGKSQFVQ LRFSDQLSAG EYTLNAAMKL KQSTRWADKG YPVAFGQFVF QQQAAPTATK
PPASRTMDVI HGTFNLGVRT DHFSAIFSKE KKGLLSLRYH GREFLKQVPM PMFWRALTDN
DNGCRFGYQS GLWLQASLFQ RCIKTRIVEE KDAVTIVYTY QLPLSNQATV DVSYTVRPEE
TIDVSVDYYG EQGLPDLPIF GILLRMDADF NQFRYYGKGP EENYSDRNSG ARLGIFEKKV
VDNVSKYAIP QESGNRTGVR WVNMLDDHGE GLLFEALDQP FELGISPFTA FELQNARHVD
ELPEIHYTNV TLASRQMGVG GDDSWGAPVH QAYHIDASDH LHFAFKIRAA CTDDR
//
