ID   L0FWV5_ECHVK            Unreviewed;      1036 AA.
AC   L0FWV5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE   AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN   OrderedLocusNames=Echvi_2143 {ECO:0000313|EMBL:AGA78394.1};
OS   Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Echinicola.
OX   NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA78394.1, ECO:0000313|Proteomes:UP000010796};
RN   [1] {ECO:0000313|Proteomes:UP000010796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC   {ECO:0000313|Proteomes:UP000010796};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Echinicola vietnamensis DSM 17526.";
RL   Submitted (FEB-2012) 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};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; CP003346; AGA78394.1; -; Genomic_DNA.
DR   RefSeq; WP_015265953.1; NC_019904.1.
DR   AlphaFoldDB; L0FWV5; -.
DR   STRING; 926556.Echvi_2143; -.
DR   KEGG; evi:Echvi_2143; -.
DR   PATRIC; fig|926556.3.peg.2264; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_002346_0_2_10; -.
DR   OrthoDB; 9802773at2; -.
DR   Proteomes; UP000010796; Chromosome.
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; 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; 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.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010796}.
FT   DOMAIN          760..1034
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   1036 AA;  118998 MW;  7C692056D9F84334 CRC64;
     MKSIITSLFC AFICVIKVSG QDRKADPIFE NPHVQEENRL PMRASYFPYE NEALAEKGEK
     AASDRFFDLN GTWKFFWTDH YTKLPKDFYA TGFDDAAWDD FQVPANWEFN GYGTPIYVNH
     PFEFAVDNPN PPFIENEKNP AGVYRRKISL PDGWEDQQVF IHLGAVKSAF RLYVNGVYVG
     LGEDSKLESE FELTDYVQPG ENLITIEVRR WHDGSYLEAQ DFWRISGIER DVYLYSRPKV
     HFYDLFVKSP LTNSYRDGKL DVTVDLWNRT DEQQGENTVM AKLLDPNGNV VFEQTQATIG
     LKRKQGKTVL NFATEIPSVK AWSAETPTLY QLELVLANAA GEPLEVVRQN VGFRTYEVVG
     NQFLVNGKAV LFKGVNRHES HPETHHVITK EQMETDVRIM KELNMNAVRL SHYPNDPYWY
     ELCDKYGFYV IDEANIESHG MYYSPERTLG NAPEWLHAHM LRIKRMVFRD KNHPSVVAWS
     MGNEAGNGYN FYKAYEWIKA YDPSRPVQYE RSTYEWNTDI IVPQYPHPNS MIRYAESNPK
     RPYIMSEYAH AMGNSMGNFR EYWEVIKAYP MLQGGYIWDW VDQGIYKEID GKRVFGYGGD
     WGPEGTPSDD NFLINGVIMA DRRWNPHAYE VRRVHQEVSF ELTEDDRLEI FNEYFFRDLS
     NYTFEAILLK NGEVIKRASI GTFALAPRQH TVVDLPFGLV RDESAEYRLQ VEGRIVQEEG
     RMAPKTLLAE AEFALTDPVL KKFDPQAADV EVREEAGKLW ISNKKFSVFF NVATGQFHDY
     KVGKNTLIVD GPSLSLFRPL VDNDFGGGRG SKLDYQHGKV TSLQKLEHQA AADGTYQVKA
     IYEVLGGDAS FEQVYRFDDG GKIRVDNTFK AIKGDHDYLL KIGTDLKLPG ALDQFKWYGR
     GPWESYADRK YSAQVGLYEG SVMEQYHPYV RPQESGNKTD VRWASVSKSQ NEGLMIYALE
     DLLNVSALPY GIDQLYPGKE KQNIHSGELE PNGYTNLHVD LEQTGVAGIN SWGSIALEAY
     RVSFKDYAFS YVIAPF
//