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Database: UniProt
Entry: A0A1M4YF79_9BACT
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ID   A0A1M4YF79_9BACT        Unreviewed;      1136 AA.
AC   A0A1M4YF79;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
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   ORFNames=SAMN05444362_103152 {ECO:0000313|EMBL:SHF04308.1};
OS   Dysgonomonas macrotermitis.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC   Dysgonomonas.
OX   NCBI_TaxID=1346286 {ECO:0000313|EMBL:SHF04308.1, ECO:0000313|Proteomes:UP000184480};
RN   [1] {ECO:0000313|Proteomes:UP000184480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27370 {ECO:0000313|Proteomes:UP000184480};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) 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; FQUC01000003; SHF04308.1; -; Genomic_DNA.
DR   RefSeq; WP_062177474.1; NZ_FQUC01000003.1.
DR   AlphaFoldDB; A0A1M4YF79; -.
DR   STRING; 1346286.SAMN05444362_103152; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000184480; 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; 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:UP000184480};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1136
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009908437"
FT   DOMAIN          787..1120
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   1136 AA;  130232 MW;  8F4B6EF0E714FBFE CRC64;
     MKKLLIGCLL YLISVNLPAQ DKLPYWKDIN VFSVNKEDAR SAFVSYSNKS EALTGIYENS
     KYYQLLNGTW KFYFVDSYKQ LPDNITDPNA STDSWHDIKV PGNWEIQGFG TPIYTNHGYE
     FKPRNPTPPL LPEDIPAGIY RRDIEIPADW LGRDIYLHIG GAKSGVYVYI NGQEVGYSED
     SKNPAEFNIN KYVKAGKNVL TLKIFRWTTG SYLECQDFLR ISGIERDVYL WSQPKVALKD
     FWVVSTLDDS YKNGIFKLAL DIENHEKTTQ KTSVSYELLD AKQRSVAAGS SNIEIKANGK
     QAVKFDAILD NVATWTSEKT NLFKLVMTIT SDNGQEVIPF NVGFRRIEIK ESEFEKNGEK
     LRLFYINGQP VKLKGVNIHE VSQIGGHYVT PEEMRRDFEL MKLNNINSVR LAHYPQDRKF
     YEMCDEFGFY VYDEANIESH GMYYTRYLDD VRKGSYGHKD GTKLGTLGHN PDWLNNHLYR
     INNMFQRNKN FPSLTIWSLG NEAGNGYNFY VSYMTLKDLD KDLMNRPVNY ERALWEWNTD
     MFVPQYPSAA WLEEIGSKGA DRPIVLSEYA HAMGNSTGDL YGQWEAIYKY PQLQGGYIWE
     WKDHGVLMKD EETGRPYWGY GGDWGVDQPS DGNFMCDGLL RSDQTPQPGL TEVKYNYQDI
     GFEAIDLEQG VFKIINRFYF TNLSDYLIKY KIYNNGKLLN ETVLDLNTAP QTSAEIKIPY
     SSFKHTASGE YFVNFEVFTK QPTQLVPAGH MVAHDQFQLP LAQEEKTYNR DLNNPSLEYA
     EEGDNVRIHS SKVDFVFNKK QGIVTSYKVD GTEYFHDGFG IQPNFWRGPN DNDYGNGAPL
     RLQTWKQASK NFNVVNVEQM MTTGYTVTMQ VDYLLPAGNY YIMQYSLDRS GVLHISAKFT
     ALAKDADDVK KTQEAETATH SPQAASDFEE KAKQKILEVP RIGVRFRLPL EMDNIKYFGR
     GPQENYIDRN KGTLVGIYTA KAEDLYFGYA RPQENGHHTD SRWFTATMNN GKGLLVKATE
     TIGFNALRNT VEDFDAQEAD APYQWYNFTP EEIANRNEAE AANRRPKQTH ISDITPRNFV
     EICVDMKQQG VGGYDSWGSR PISAATIYSN TDYVWSFTIV PVNNNKDAES KASLKY
//
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