ID   C6W015_DYAFD            Unreviewed;      1129 AA.
AC   C6W015;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, 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   OrderedLocusNames=Dfer_4139 {ECO:0000313|EMBL:ACT95342.1};
OS   Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 /
OS   KCTC 52180 / NS114).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT95342.1, ECO:0000313|Proteomes:UP000002011};
RN   [1] {ECO:0000313|EMBL:ACT95342.1, ECO:0000313|Proteomes:UP000002011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC   {ECO:0000313|Proteomes:UP000002011};
RX   PubMed=21304649; DOI=10.4056/sigs.19262;
RA   Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA   Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA   Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA   Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL   Stand. Genomic Sci. 1:133-140(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,
CC         ECO:0000256|RuleBase:RU361154};
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, ECO:0000256|RuleBase:RU361154}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001619; ACT95342.1; -; Genomic_DNA.
DR   RefSeq; WP_015813585.1; NC_013037.1.
DR   AlphaFoldDB; C6W015; -.
DR   STRING; 471854.Dfer_4139; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   KEGG; dfe:Dfer_4139; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_002346_0_2_10; -.
DR   OrthoDB; 857501at2; -.
DR   Proteomes; UP000002011; 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; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000002011};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1129
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002969326"
FT   DOMAIN          773..1048
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
FT   REGION          1070..1129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1070..1084
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1108..1129
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1129 AA;  127242 MW;  385DCC7E16B634BF CRC64;
     MQFSTPRAFL TLFFLIQIVH HAAHAQAIPE WQDPQVISIN TEKPRADFFP YTTEKAALAM
     DKKGSFVQSL NGSWKFKWAP HPSKAQLNFY DPKVSDASWD NIPVPSNWQV VGAREGRKYD
     RPIFSNIKHP FKATPPRINA DTNAVGMYRT TFTVADVKDK QIFLHFGGVQ SACYVWLNGV
     AIGYHEDGMT PFEFDVTEDV KAGVNNLAVE VINWSDGSYL EDQDYWRLSG IFRDVNLLLL
     PKVVLTDYSV RTILDANHDN ATLKLSAFVK NYGQQPIHAH QVLFTLYDAA KNVVTTPVSQ
     MVGTLEMGRE GAVRAEMPVP SPAKWSAETP NLYMLTVQLM NSDGKVIEAT SQRVGFRDVK
     IKGGQLLVNG KAITIKGVNR HEFDPETGRV ISRESMMRDI TLMKQHNINA VRTSHYPNAS
     EWYDLCDQYG LYVMDEANIE SHELWSKGII LADNPQWRSA FLARGNAMVE RDKNHPSVII
     WSLGNESGMG QNFVDMGDFI KLADPTRPIH YEGRKDYKPT TLSSFDIISV MYPSTQDMTE
     LVKKDKTRPL IVCEYAHGMG NSVGNLKEYW DVIEKYPTMQ GGFIWDWVDQ GLKLKRPDGT
     DYWDYFNYLD GANAGDGLVN PDRTPQPELN EVKKVYQYVK FEMPDTLKTG EKALTLHNTY
     DFQSLNAFEL VWSVIENGKP AGKGGSIANL NALPRHKQQL TIPYELPAAS KPNAEYFLNL
     SLRLKDATLW APKGHEVAWH QVPVVKPATP RPNLSLYGER PLRIAQISSA RVQVAGQDFT
     VVFDKNEGRM ISFKNKKEEM LESGPYANFW RVPTDNDEGG AAKSYATQWR NFGLDTLERV
     SSEMKTQRLT AQIYKVTLSQ TLKQPKGEMD VQSVYMVYAS GDIHVQNTFT PRGEWPPLAK
     IGMQLRMPAT FTKTQWFGNG PHETYADRKT SAKVGIYAGT VAEQHFPYIT PQENGNKTGI
     RWATVTNAEG TGLLVLSDTA FNFNVHDYTD KDLLAAKRRA AVLARGTSTT VNIDLAQMGL
     GGDDSWSPRV HEAYLLPAKT YSYAFRLRPI ESTSNIEQIA AVRLPYVDQK ETNESVSTAE
     TAAATEEAVT EDEEEEEAVT APVRKTTVKK APVRKKVVRK KKPTRRRRR
//