ID   A0A0M8Y1U1_9ACTN        Unreviewed;       956 AA.
AC   A0A0M8Y1U1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=ADL05_11590 {ECO:0000313|EMBL:KOX16748.1};
OS   Nocardiopsis sp. NRRL B-16309.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1519494 {ECO:0000313|EMBL:KOX16748.1, ECO:0000313|Proteomes:UP000037694};
RN   [1] {ECO:0000313|Proteomes:UP000037694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16309 {ECO:0000313|Proteomes:UP000037694};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) 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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:KOX16748.1}.
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DR   EMBL; LGEC01000066; KOX16748.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8Y1U1; -.
DR   STRING; 1519494.ADL05_11590; -.
DR   PATRIC; fig|1519494.3.peg.2536; -.
DR   Proteomes; UP000037694; 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; 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; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037694}.
FT   DOMAIN          691..953
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
FT   REGION          667..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   956 AA;  105272 MW;  62BA0099B5FF2DAF CRC64;
     MESHTPSAGT EPPRAAFASD APVLDLDGDW RFRLAPTAEG GPGAFEREDY DDSGWDTLPV
     PSHWQLHGYG APAYTNIAYP FPIDPPHVPD ENPTGEYRRA FDLPGSWPGG SAVLRFEGVE
     SCYAVWLNGH ALGHATGSRL PSEFEVGALL RPGRNVLAVR VHQWSAASYL EDQDMWWLSG
     IFRSVRLLSR SSQGVRDVEV RASYDHASGT GVLRVDADTP GLVTVPELGL VDAPTGTDHE
     VGPVEPWSAE VPRLYDGELV TPGERVALRV GFRTVEISGG LLRVNGRPLL LRGVNRHEWD
     PDRGRAVTRE TMREDVLLMK RHNVNAVRTS HYPPHPDFLD LCDELGLWVV DECDLETHGF
     EDVGWRRNPS DDPLWRDAYL DRMARTVERD KNHPSVILWS LGNESGGGRN LRAMAEWTRR
     RDPGRPVHYE GAADPAYTDL YSRMYATHEE VAAIGRRSGL PEGDPGLIDR PFVMVEYAHA
     MGTGPGGLEE YQRLVEAYPH VQGGFVWEWI DHGIRRREDD GTEWFAYGGD FGEVVHDANF
     VADGLLMPDR TPGPGLAALA KTFEPLRLVP DPEQGTVSVT NTWQVLDTSG VELRWDLREE
     GGLVAEGVLE AEPVGPGETA VLPLPDLPGP RARRRETWLT VSARLAEDRP WADAGHEVAW
     GQARVDRPGA EEPDTGVITP VPPVTEGGTI TVGPAEFDAR TGRALSLAGL PLAALELDVW
     RAPTDNDQAR HGESVEVPWR RAGLDRMTHR VLSVEREGAA LRVRTRVAAA ASELGLLADY
     TWTGDADALV LDLAVEAVGD WPCPLPRVGV RLELPPELGE AEWFGRGPGE AYRDVAQAAR
     VGRFSSSVDA LQTPYLRPQE NGNRTGTRRL DLRSPEGRGL RVEGAPDFDF TARRWSTAAL
     DRARHPHELR PEDRIHLHLD AEHQGIGSAS CGPGVLPEHR LTPGSHRLRL VLRPLG
//